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Database: UniProt
Entry: P31327
LinkDB: P31327
Original site: P31327 
ID   CPSM_HUMAN              Reviewed;        1500 AA.
AC   P31327; B7Z818; J3KQL0; O43774; Q53TL5; Q59HF8; Q7Z5I5;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 2.
DT   13-FEB-2019, entry version 221.
DE   RecName: Full=Carbamoyl-phosphate synthase [ammonia], mitochondrial;
DE            EC=6.3.4.16 {ECO:0000269|PubMed:23649895, ECO:0000269|PubMed:24813853};
DE   AltName: Full=Carbamoyl-phosphate synthetase I;
DE            Short=CPSase I;
DE   Flags: Precursor;
GN   Name=CPS1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS SER-1266;
RP   LEU-1283 AND ASN-1406.
RC   TISSUE=Liver;
RX   PubMed=1840546; DOI=10.1016/0378-1119(91)90336-A;
RA   Haraguchi Y., Uchino T., Takiguchi M., Endo F., Mori M., Matsuda I.;
RT   "Cloning and sequence of a cDNA encoding human carbamyl phosphate
RT   synthetase I: molecular analysis of hyperammonemia.";
RL   Gene 107:335-340(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT CPS1D MET-544, AND
RP   VARIANT ALA-344.
RC   TISSUE=Liver;
RX   PubMed=9711878;
RX   DOI=10.1002/(SICI)1098-1004(1998)12:3<206::AID-HUMU8>3.0.CO;2-E;
RA   Finckh U., Kohlschuetter A., Schaefer H., Sperhake K., Colombo J.-P.,
RA   Gal A.;
RT   "Prenatal diagnosis of carbamoyl phosphate synthetase I deficiency by
RT   identification of a missense mutation in CPS1.";
RL   Hum. Mutat. 12:206-211(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS ALA-344; SER-1376
RP   AND ASN-1406.
RX   PubMed=12853138; DOI=10.1016/S0378-1119(03)00528-6;
RA   Summar M.L., Hall L.D., Eeds A.M., Hutcheson H.B., Kuo A.N.,
RA   Willis A.S., Rubio V., Arvin M.K., Schofield J.P., Dawson E.P.;
RT   "Characterization of genomic structure and polymorphisms in the human
RT   carbamyl phosphate synthetase I gene.";
RL   Gene 311:51-57(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   TISSUE=Testis;
RA   Huo R., Zhu H., Huang X.Y., Xu Z.Y., Lu L., Xu M., Yin L.L., Li J.M.,
RA   Zhou Z.M., Sha J.H.;
RT   "Cloning of an isoform of CPS1 gene related to spermatogenesis.";
RL   Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), VARIANTS CPS1D GLY-457
RP   AND ARG-810, AND VARIANT ASN-1406.
RX   PubMed=12955727; DOI=10.1002/humu.9184;
RA   Funghini S., Donati M.A., Pasquini E., Zammarchi E., Morrone A.;
RT   "Structural organization of the human carbamyl phosphate synthetase I
RT   gene (CPS1) and identification of two novel genetic lesions.";
RL   Hum. Mutat. 22:340-341(2003).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), VARIANT CPS1D SER-843,
RP   AND VARIANT GLU-875.
RX   PubMed=12655559; DOI=10.1002/humu.9118;
RA   Haeberle J., Schmidt E., Pauli S., Rapp B., Christensen E.,
RA   Wermuth B., Koch H.G.;
RT   "Gene structure of human carbamylphosphate synthetase 1 and novel
RT   mutations in patients with neonatal onset.";
RL   Hum. Mutat. 21:444-444(2003).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Testis;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA   Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA   Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA   Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA   Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA   Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA   Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA   Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA   Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA   Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA   Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA   Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA   Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA   Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA   Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA   Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA   Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA   Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA   McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA   Waterston R.H., Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2
RT   and 4.";
RL   Nature 434:724-731(2005).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [10]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [11]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT
RP   ALA-344.
RC   TISSUE=Brain;
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA   Ohara O., Nagase T., Kikuno R.F.;
RT   "Homo sapiens protein coding cDNA.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [12]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 795-1500.
RC   TISSUE=Small intestine;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA   Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [13]
RP   ALLOSTERIC ACTIVATOR NAG BINDING SITE.
RX   PubMed=19754428; DOI=10.1042/BJ20090888;
RA   Pekkala S., Martinez A.I., Barcelona B., Gallego J., Bendala E.,
RA   Yefimenko I., Rubio V., Cervera J.;
RT   "Structural insight on the control of urea synthesis: identification
RT   of the binding site for N-acetyl-L-glutamate, the essential allosteric
RT   activator of mitochondrial carbamoyl phosphate synthetase.";
RL   Biochem. J. 424:211-220(2009).
RN   [14]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [15]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=22002106; DOI=10.1074/mcp.M111.013680;
RA   Ahmad Y., Boisvert F.M., Lundberg E., Uhlen M., Lamond A.I.;
RT   "Systematic analysis of protein pools, isoforms, and modifications
RT   affecting turnover and subcellular localization.";
RL   Mol. Cell. Proteomics 11:M111.013680.01-M111.013680.15(2012).
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1036 AND SER-1079, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [17]
RP   GLUTARYLATION AT LYS-55; LYS-171; LYS-176; LYS-207; LYS-210; LYS-214;
RP   LYS-219; LYS-228; LYS-237; LYS-280; LYS-307; LYS-310; LYS-402;
RP   LYS-412; LYS-453; LYS-458; LYS-527; LYS-532; LYS-553; LYS-728;
RP   LYS-757; LYS-772; LYS-793; LYS-811; LYS-841; LYS-856; LYS-869;
RP   LYS-875; LYS-889; LYS-892; LYS-905; LYS-908; LYS-915; LYS-919;
RP   LYS-1074; LYS-1150; LYS-1168; LYS-1183; LYS-1224; LYS-1356; LYS-1360;
RP   LYS-1479 AND LYS-1486.
RX   PubMed=24703693; DOI=10.1016/j.cmet.2014.03.014;
RA   Tan M., Peng C., Anderson K.A., Chhoy P., Xie Z., Dai L., Park J.,
RA   Chen Y., Huang H., Zhang Y., Ro J., Wagner G.R., Green M.F.,
RA   Madsen A.S., Schmiesing J., Peterson B.S., Xu G., Ilkayeva O.R.,
RA   Muehlbauer M.J., Braulke T., Muehlhausen C., Backos D.S., Olsen C.A.,
RA   McGuire P.J., Pletcher S.D., Lombard D.B., Hirschey M.D., Zhao Y.;
RT   "Lysine glutarylation is a protein posttranslational modification
RT   regulated by SIRT5.";
RL   Cell Metab. 19:605-617(2014).
RN   [18]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148; SER-569; SER-835;
RP   SER-1079; SER-1203; SER-1419 AND SER-1431, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [19]
RP   X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) OF 1343-1478.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Crystal structure of MGS domain of carbamoyl-phosphate synthetase
RT   from Homo sapiens.";
RL   Submitted (FEB-2009) to the PDB data bank.
RN   [20]
RP   VARIANT CPS1D ARG-1054.
RX   PubMed=11388595; DOI=10.1007/s004310100725;
RA   Rapp B., Haberle J., Linnebank M., Wermuth B., Marquardt T., Harms E.,
RA   Koch H.G.;
RT   "Genetic analysis of carbamoylphosphate synthetase I and ornithine
RT   transcarbamylase deficiency using fibroblasts.";
RL   Eur. J. Pediatr. 160:283-287(2001).
RN   [21]
RP   VARIANT CPS1D ARG-337.
RX   PubMed=11474210; DOI=10.1159/000053360;
RA   Aoshima T., Kajita M., Sekido Y., Kikuchi S., Yasuda I., Saheki T.,
RA   Watanabe K., Shimokata K., Niwa T.;
RT   "Novel mutations (H337R and 238-362del) in the CPS1 gene cause
RT   carbamoyl phosphate synthetase I deficiency.";
RL   Hum. Hered. 52:99-101(2001).
RN   [22]
RP   VARIANT ASN-1406, AND INVOLVEMENT IN PHN.
RX   PubMed=11407344; DOI=10.1056/NEJM200106143442404;
RA   Pearson D.L., Dawling S., Walsh W.F., Haines J.L., Christman B.W.,
RA   Bazyk A., Scott N., Summar M.L.;
RT   "Neonatal pulmonary hypertension -- urea-cycle intermediates, nitric
RT   oxide production, and carbamoyl-phosphate synthetase function.";
RL   N. Engl. J. Med. 344:1832-1838(2001).
RN   [23]
RP   VARIANTS CPS1D HIS-850 AND PRO-918.
RX   PubMed=15617192; DOI=10.1023/B:BOLI.0000045842.59768.ea;
RA   Wakutani Y., Nakayasu H., Takeshima T., Adachi M., Kawataki M.,
RA   Kihira K., Sawada H., Bonno M., Yamamoto H., Nakashima K.;
RT   "Mutational analysis of carbamoylphosphate synthetase I deficiency in
RT   three Japanese patients.";
RL   J. Inherit. Metab. Dis. 27:787-788(2004).
RN   [24]
RP   VARIANT CPS1D SER-843, AND VARIANT GLU-875.
RX   PubMed=15164414; DOI=10.1002/pd.884;
RA   Haeberle J., Koch H.G.;
RT   "Genetic approach to prenatal diagnosis in urea cycle defects.";
RL   Prenat. Diagn. 24:378-383(2004).
RN   [25]
RP   VARIANTS CPS1D GLU-301; CYS-389; ARG-390; THR-589; SER-640; LYS-716;
RP   LEU-805; VAL-911; PRO-958; SER-982; PHE-998; LEU-1089; PRO-1203;
RP   ASN-1205; PRO-1331; THR-1378; LEU-1411 AND ALA-1443.
RX   PubMed=16737834; DOI=10.1016/j.ymgme.2006.04.006;
RA   Eeds A.M., Hall L.D., Yadav M., Willis A., Summar S., Putnam A.,
RA   Barr F., Summar M.L.;
RT   "The frequent observation of evidence for nonsense-mediated decay in
RT   RNA from patients with carbamyl phosphate synthetase I deficiency.";
RL   Mol. Genet. Metab. 89:80-86(2006).
RN   [26]
RP   VARIANTS CPS1D GLU-79; ASN-212; ASN-280; PRO-438; HIS-587; ARG-593;
RP   LYS-651; ILE-674; HIS-780; CYS-850; ASP-982; ARG-1103; GLY-1141;
RP   PRO-1195; VAL-1215 AND LYS-1241.
RX   PubMed=17310273; DOI=10.1007/s10038-007-0122-9;
RA   Kurokawa K., Yorifuji T., Kawai M., Momoi T., Nagasaka H.,
RA   Takayanagi M., Kobayashi K., Yoshino M., Kosho T., Adachi M.,
RA   Otsuka H., Yamamoto S., Murata T., Suenaga A., Ishii T., Terada K.,
RA   Shimura N., Kiwaki K., Shintaku H., Yamakawa M., Nakabayashi H.,
RA   Wakutani Y., Nakahata T.;
RT   "Molecular and clinical analyses of Japanese patients with
RT   carbamoylphosphate synthetase 1 (CPS1) deficiency.";
RL   J. Hum. Genet. 52:349-354(2007).
RN   [27]
RP   VARIANTS CPS1D PHE-123; ARG-337; ASN-471; PRO-678; LEU-774; LEU-1411;
RP   GLN-1453; TRP-1453 AND HIS-1491, VARIANT SER-1376, CHARACTERIZATION OF
RP   VARIANTS CPS1D PHE-123; ARG-337; ASN-471; PRO-678; LEU-774; LEU-1411;
RP   GLN-1453; TRP-1453 AND HIS-1491, AND CHARACTERIZATION OF VARIANT
RP   SER-1376.
RX   PubMed=20578160; DOI=10.1002/humu.21272;
RA   Pekkala S., Martinez A.I., Barcelona B., Yefimenko I., Finckh U.,
RA   Rubio V., Cervera J.;
RT   "Understanding carbamoyl-phosphate synthetase I (CPS1) deficiency by
RT   using expression studies and structure-based analysis.";
RL   Hum. Mutat. 31:801-808(2010).
RN   [28]
RP   VARIANT ASN-1406.
RX   PubMed=20520828; DOI=10.1371/journal.pone.0010792;
RA   Moonen R.M., Reyes I., Cavallaro G., Gonzalez-Luis G., Bakker J.A.,
RA   Villamor E.;
RT   "The T1405N carbamoyl phosphate synthetase polymorphism does not
RT   affect plasma arginine concentrations in preterm infants.";
RL   PLoS ONE 5:E10792-E10792(2010).
RN   [29]
RP   VARIANTS CPS1D VAL-43; ASP-58; PHE-65; GLY-71; SER-87; ASP-89;
RP   GLY-165; VAL-224; CYS-233; PRO-243; GLU-258; GLU-263; VAL-304;
RP   GLU-317; HIS-358; LEU-382; ARG-401; ARG-431; VAL-432; THR-438;
RP   GLU-450; PRO-498; GLU-531; GLY-531; MET-544; CYS-587; HIS-587;
RP   LEU-587; LEU-597; MET-622; ASP-628; ARG-632; PRO-638; TYR-648;
RP   VAL-654; LYS-674; SER-698; LYS-718; GLN-721; PRO-724; THR-726;
RP   VAL-767; HIS-780; ILE-792; SER-803; GLY-803; CYS-803; SER-805;
RP   TRP-814; ARG-816; HIS-850; GLU-911; LEU-913; HIS-914; GLY-914;
RP   THR-932; THR-949; CYS-959; CYS-962; GLU-978; VAL-982; HIS-984;
RP   THR-986; CYS-987; SER-992; SER-1016; LEU-1017; ILE-1022; GLY-1034;
RP   ARG-1045; ARG-1059; GLU-1065; CYS-1089; GLU-1155; VAL-1155; LEU-1203;
RP   GLN-1228; ASP-1255; GLN-1262; PRO-1262; HIS-1274; ARG-1327; GLU-1333;
RP   LEU-1371; MET-1391; VAL-1398; LEU-1439; TRP-1453 AND ARG-1462.
RX   PubMed=21120950; DOI=10.1002/humu.21406;
RA   Haberle J., Shchelochkov O.A., Wang J., Katsonis P., Hall L.,
RA   Reiss S., Eeds A., Willis A., Yadav M., Summar S., Lichtarge O.,
RA   Rubio V., Wong L.J., Summar M.;
RT   "Molecular defects in human carbamoyl phosphate synthetase I:
RT   mutational spectrum, diagnostic and protein structure
RT   considerations.";
RL   Hum. Mutat. 32:579-589(2011).
RN   [30]
RP   VARIANTS VAL-530 AND ASN-1406.
RX   PubMed=21767969; DOI=10.1016/j.ymgme.2011.06.022;
RG   NISC Comparative Sequencing Program;
RA   Solomon B.D., Pineda-Alvarez D.E., Hadley D.W., Teer J.K.,
RA   Cherukuri P.F., Hansen N.F., Cruz P., Young A.C., Blakesley R.W.,
RA   Lanpher B., Mayfield Gibson S., Sincan M., Chandrasekharappa S.C.,
RA   Mullikin J.C.;
RT   "Personalized genomic medicine: lessons from the exome.";
RL   Mol. Genet. Metab. 104:189-191(2011).
RN   [31]
RP   VARIANTS CPS1D SER-341; ARG-661; ASP-964 AND ARG-1167.
RX   PubMed=22173106; DOI=10.1016/j.gene.2011.11.052;
RA   Funghini S., Thusberg J., Spada M., Gasperini S., Parini R.,
RA   Ventura L., Meli C., De Cosmo L., Sibilio M., Mooney S.D.,
RA   Guerrini R., Donati M.A., Morrone A.;
RT   "Carbamoyl phosphate synthetase 1 deficiency in Italy: clinical and
RT   genetic findings in a heterogeneous cohort.";
RL   Gene 493:228-234(2012).
RN   [32]
RP   VARIANTS CPS1D ASP-355; CYS-389; ARG-390; PRO-438; MET-544; THR-1378;
RP   SER-1381 AND ALA-1443, VARIANTS ALA-344 AND SER-1376, CHARACTERIZATION
RP   OF VARIANTS CPS1D ASP-355; CYS-389; ARG-390; PRO-438; MET-544;
RP   THR-1378; SER-1381 AND ALA-1443, CHARACTERIZATION OF VARIANTS ALA-344
RP   AND SER-1376, SUBUNIT, PROTEOLYTIC CLEAVAGE, BIOPHYSICOCHEMICAL
RP   PROPERTIES, ACTIVITY REGULATION, AND CATALYTIC ACTIVITY.
RX   PubMed=23649895; DOI=10.1002/humu.22349;
RA   Diez-Fernandez C., Martinez A.I., Pekkala S., Barcelona B.,
RA   Perez-Arellano I., Guadalajara A.M., Summar M., Cervera J., Rubio V.;
RT   "Molecular characterization of carbamoyl-phosphate synthetase (CPS1)
RT   deficiency using human recombinant CPS1 as a key tool.";
RL   Hum. Mutat. 34:1149-1159(2013).
RN   [33]
RP   VARIANT ASN-1406.
RX   PubMed=24237036; DOI=10.1021/pr400544j;
RA   Song C., Wang F., Cheng K., Wei X., Bian Y., Wang K., Tan Y., Wang H.,
RA   Ye M., Zou H.;
RT   "Large-scale quantification of single amino-acid variations by a
RT   variation-associated database search strategy.";
RL   J. Proteome Res. 13:241-248(2014).
RN   [34]
RP   VARIANTS CPS1D ARG-401; ARG-632; SER-843; CYS-850; HIS-850; PRO-871;
RP   VAL-911; GLU-911; LEU-913; HIS-914; GLY-914; PRO-918; THR-932;
RP   ASN-937; THR-949; PRO-958; CYS-959; CYS-962; ASP-964; ASP-1194 AND
RP   ARG-1462, VARIANT GLU-875, CHARACTERIZATION OF VARIANTS CPS1D SER-843;
RP   CYS-850; HIS-850; PRO-871; VAL-911; GLU-911; LEU-913; HIS-914;
RP   GLY-914; PRO-918; THR-932; ASN-937; THR-949; PRO-958; CYS-959; CYS-962
RP   AND ASP-964, CATALYTIC ACTIVITY, AND CHARACTERIZATION OF VARIANT
RP   GLU-875.
RX   PubMed=24813853; DOI=10.1016/j.ymgme.2014.04.003;
RA   Diez-Fernandez C., Hu L., Cervera J., Haeberle J., Rubio V.;
RT   "Understanding carbamoyl phosphate synthetase (CPS1) deficiency by
RT   using the recombinantly purified human enzyme: effects of CPS1
RT   mutations that concentrate in a central domain of unknown function.";
RL   Mol. Genet. Metab. 112:123-132(2014).
RN   [35]
RP   VARIANTS CPS1D TYR-123; TRP-174; GLY-803; HIS-850; PHE-1254 AND
RP   1363-LEU--ILE-1366 DEL.
RX   PubMed=26440671; DOI=10.1007/s00431-015-2644-z;
RA   Ali E.Z., Khalid M.K., Yunus Z.M., Yakob Y., Chin C.B., Latif K.A.,
RA   Hock N.L.;
RT   "Carbamoylphosphate synthetase 1 (CPS1) deficiency: clinical,
RT   biochemical, and molecular characterization in Malaysian patients.";
RL   Eur. J. Pediatr. 175:339-346(2016).
RN   [36]
RP   VARIANT GLU-875.
RX   PubMed=27535533; DOI=10.1038/nature19057;
RG   Exome Aggregation Consortium;
RA   Lek M., Karczewski K.J., Minikel E.V., Samocha K.E., Banks E.,
RA   Fennell T., O'Donnell-Luria A.H., Ware J.S., Hill A.J., Cummings B.B.,
RA   Tukiainen T., Birnbaum D.P., Kosmicki J.A., Duncan L.E., Estrada K.,
RA   Zhao F., Zou J., Pierce-Hoffman E., Berghout J., Cooper D.N.,
RA   Deflaux N., DePristo M., Do R., Flannick J., Fromer M., Gauthier L.,
RA   Goldstein J., Gupta N., Howrigan D., Kiezun A., Kurki M.I.,
RA   Moonshine A.L., Natarajan P., Orozco L., Peloso G.M., Poplin R.,
RA   Rivas M.A., Ruano-Rubio V., Rose S.A., Ruderfer D.M., Shakir K.,
RA   Stenson P.D., Stevens C., Thomas B.P., Tiao G., Tusie-Luna M.T.,
RA   Weisburd B., Won H.H., Yu D., Altshuler D.M., Ardissino D.,
RA   Boehnke M., Danesh J., Donnelly S., Elosua R., Florez J.C.,
RA   Gabriel S.B., Getz G., Glatt S.J., Hultman C.M., Kathiresan S.,
RA   Laakso M., McCarroll S., McCarthy M.I., McGovern D., McPherson R.,
RA   Neale B.M., Palotie A., Purcell S.M., Saleheen D., Scharf J.M.,
RA   Sklar P., Sullivan P.F., Tuomilehto J., Tsuang M.T., Watkins H.C.,
RA   Wilson J.G., Daly M.J., MacArthur D.G.;
RT   "Analysis of protein-coding genetic variation in 60,706 humans.";
RL   Nature 536:285-291(2016).
CC   -!- FUNCTION: Involved in the urea cycle of ureotelic animals where
CC       the enzyme plays an important role in removing excess ammonia from
CC       the cell.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 ATP + hydrogencarbonate + NH4(+) = 2 ADP + carbamoyl
CC         phosphate + 2 H(+) + phosphate; Xref=Rhea:RHEA:18029,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228,
CC         ChEBI:CHEBI:456216; EC=6.3.4.16;
CC         Evidence={ECO:0000269|PubMed:23649895,
CC         ECO:0000269|PubMed:24813853};
CC   -!- ACTIVITY REGULATION: Requires N-acetyl-L-glutamate (NAG) as an
CC       allosteric activator. Activated by glycerol in the absence of NAG,
CC       whereas in the presence of NAG it is inhibited by increasing
CC       concentrations of glycerol. {ECO:0000269|PubMed:19754428,
CC       ECO:0000269|PubMed:23649895}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.47 mM for ATP {ECO:0000269|PubMed:23649895};
CC         KM=4.0 mM for HCO(3)(-) {ECO:0000269|PubMed:23649895};
CC         KM=1.00 mM for NH(4)(+) {ECO:0000269|PubMed:23649895};
CC         Vmax=1.22 umol/min/mg enzyme for ATP
CC         {ECO:0000269|PubMed:23649895};
CC         Vmax=1.23 umol/min/mg enzyme for HCO(3)(-)
CC         {ECO:0000269|PubMed:23649895};
CC         Vmax=1.19 umol/min/mg enzyme for NH(4)(+)
CC         {ECO:0000269|PubMed:23649895};
CC   -!- SUBUNIT: Can form homooligomers (monomers as predominant form and
CC       dimers). {ECO:0000269|PubMed:23649895}.
CC   -!- INTERACTION:
CC       P10398:ARAF; NbExp=3; IntAct=EBI-536811, EBI-365961;
CC       P04049:RAF1; NbExp=4; IntAct=EBI-536811, EBI-365996;
CC       P63104:YWHAZ; NbExp=2; IntAct=EBI-536811, EBI-347088;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:22002106}.
CC       Nucleus, nucleolus {ECO:0000269|PubMed:22002106}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=P31327-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P31327-2; Sequence=VSP_009332;
CC       Name=3;
CC         IsoId=P31327-3; Sequence=VSP_046685;
CC         Note=Ref.11 (BAD92037) sequence is in conflict in position:
CC         5:I->IF. {ECO:0000305};
CC   -!- TISSUE SPECIFICITY: Primarily in the liver and small intestine.
CC   -!- DOMAIN: The type-1 glutamine amidotransferase domain is defective.
CC   -!- PTM: Undergoes proteolytic cleavage in the C-terminal region
CC       corresponding to the loss of approximately 12 AA residues from the
CC       C-terminus. {ECO:0000269|PubMed:23649895}.
CC   -!- PTM: Succinylated at Lys-287 and Lys-1291. Desuccinylated at Lys-
CC       1291 by SIRT5, leading to activation (By similarity).
CC       {ECO:0000250|UniProtKB:Q8C196}.
CC   -!- PTM: Glutarylated. Glutarylation levels increase during fasting.
CC       Deglutarylated by SIRT5 at Lys-55, Lys-219, Lys-412, Lys-889, Lys-
CC       892, Lys-915, Lys-1360 and Lys-1486, leading to activation.
CC       {ECO:0000269|PubMed:24703693}.
CC   -!- DISEASE: Carbamoyl phosphate synthetase 1 deficiency (CPS1D)
CC       [MIM:237300]: An autosomal recessive disorder of the urea cycle
CC       causing hyperammonemia. It can present as a devastating metabolic
CC       disease dominated by severe hyperammonemia in neonates or as a
CC       more insidious late-onset condition, generally manifesting as
CC       life-threatening hyperammonemic crises under catabolic situations.
CC       Clinical features include protein intolerance, intermittent
CC       ataxia, seizures, lethargy, developmental delay and mental
CC       retardation. {ECO:0000269|PubMed:11388595,
CC       ECO:0000269|PubMed:11474210, ECO:0000269|PubMed:12655559,
CC       ECO:0000269|PubMed:12955727, ECO:0000269|PubMed:15164414,
CC       ECO:0000269|PubMed:15617192, ECO:0000269|PubMed:16737834,
CC       ECO:0000269|PubMed:17310273, ECO:0000269|PubMed:20578160,
CC       ECO:0000269|PubMed:21120950, ECO:0000269|PubMed:22173106,
CC       ECO:0000269|PubMed:23649895, ECO:0000269|PubMed:24813853,
CC       ECO:0000269|PubMed:26440671, ECO:0000269|PubMed:9711878}. Note=The
CC       disease is caused by mutations affecting the gene represented in
CC       this entry.
CC   -!- DISEASE: Pulmonary hypertension, neonatal (PHN) [MIM:615371]: A
CC       disease characterized by elevated pulmonary artery pressure.
CC       Pulmonary hypertension in the neonate is associated with multiple
CC       underlying problems such as respiratory distress syndrome,
CC       meconium aspiration syndrome, congenital diaphragmatic hernia,
CC       bronchopulmonary dysplasia, sepsis, or congenital heart disease.
CC       {ECO:0000269|PubMed:11407344}. Note=Disease susceptibility is
CC       associated with variations affecting the gene represented in this
CC       entry. CPS1 variants influence the availability of precursors for
CC       nitric oxide (NO) synthesis and play a role in clinical situations
CC       where endogenous NO production is critically important, such as
CC       neonatal pulmonary hypertension, increased pulmonary artery
CC       pressure following surgical repair of congenital heart defects or
CC       hepatovenocclusive disease following bone marrow transplantation.
CC       Infants with neonatal pulmonary hypertension homozygous for Thr-
CC       1406 have lower L-arginine concentrations than neonates homozygous
CC       for Asn-1406 (PubMed:11407344). {ECO:0000269|PubMed:11407344}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD92037.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=LOVD-Leiden Open Variation Database;
CC       Note=Carbamoyl-Phosphate Synthetase 1 (CPS1);
CC       URL="http://chromium.lovd.nl/lovd2/home.php?select_db=CPS1";
DR   EMBL; D90282; BAA14328.1; -; mRNA.
DR   EMBL; Y15793; CAA75785.1; -; mRNA.
DR   EMBL; AF154830; AAD38072.1; -; mRNA.
DR   EMBL; AY317138; AAP84318.1; -; mRNA.
DR   EMBL; AY167007; AAO31763.1; -; Genomic_DNA.
DR   EMBL; AY166970; AAO31763.1; JOINED; Genomic_DNA.
DR   EMBL; AY166971; AAO31763.1; JOINED; Genomic_DNA.
DR   EMBL; AY166972; AAO31763.1; JOINED; Genomic_DNA.
DR   EMBL; AY166973; AAO31763.1; JOINED; Genomic_DNA.
DR   EMBL; AY166974; AAO31763.1; JOINED; Genomic_DNA.
DR   EMBL; AY166975; AAO31763.1; JOINED; Genomic_DNA.
DR   EMBL; AY166976; AAO31763.1; JOINED; Genomic_DNA.
DR   EMBL; AY166977; AAO31763.1; JOINED; Genomic_DNA.
DR   EMBL; AY166978; AAO31763.1; JOINED; Genomic_DNA.
DR   EMBL; AY166979; AAO31763.1; JOINED; Genomic_DNA.
DR   EMBL; AY166980; AAO31763.1; JOINED; Genomic_DNA.
DR   EMBL; AY166981; AAO31763.1; JOINED; Genomic_DNA.
DR   EMBL; AY166982; AAO31763.1; JOINED; Genomic_DNA.
DR   EMBL; AY166983; AAO31763.1; JOINED; Genomic_DNA.
DR   EMBL; AY166984; AAO31763.1; JOINED; Genomic_DNA.
DR   EMBL; AY166985; AAO31763.1; JOINED; Genomic_DNA.
DR   EMBL; AY166986; AAO31763.1; JOINED; Genomic_DNA.
DR   EMBL; AY166987; AAO31763.1; JOINED; Genomic_DNA.
DR   EMBL; AY166988; AAO31763.1; JOINED; Genomic_DNA.
DR   EMBL; AY166989; AAO31763.1; JOINED; Genomic_DNA.
DR   EMBL; AY166990; AAO31763.1; JOINED; Genomic_DNA.
DR   EMBL; AY166991; AAO31763.1; JOINED; Genomic_DNA.
DR   EMBL; AY166992; AAO31763.1; JOINED; Genomic_DNA.
DR   EMBL; AY166993; AAO31763.1; JOINED; Genomic_DNA.
DR   EMBL; AY166994; AAO31763.1; JOINED; Genomic_DNA.
DR   EMBL; AY166995; AAO31763.1; JOINED; Genomic_DNA.
DR   EMBL; AY166996; AAO31763.1; JOINED; Genomic_DNA.
DR   EMBL; AY166997; AAO31763.1; JOINED; Genomic_DNA.
DR   EMBL; AY166998; AAO31763.1; JOINED; Genomic_DNA.
DR   EMBL; AY166999; AAO31763.1; JOINED; Genomic_DNA.
DR   EMBL; AY167000; AAO31763.1; JOINED; Genomic_DNA.
DR   EMBL; AY167001; AAO31763.1; JOINED; Genomic_DNA.
DR   EMBL; AY167002; AAO31763.1; JOINED; Genomic_DNA.
DR   EMBL; AY167003; AAO31763.1; JOINED; Genomic_DNA.
DR   EMBL; AY167004; AAO31763.1; JOINED; Genomic_DNA.
DR   EMBL; AY167005; AAO31763.1; JOINED; Genomic_DNA.
DR   EMBL; AY167006; AAO31763.1; JOINED; Genomic_DNA.
DR   EMBL; AF536523; AAN77181.1; -; Genomic_DNA.
DR   EMBL; AK302778; BAH13804.1; -; mRNA.
DR   EMBL; AC007970; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC008172; AAY14960.1; -; Genomic_DNA.
DR   EMBL; CH471063; EAW70492.1; -; Genomic_DNA.
DR   EMBL; BC140943; AAI40944.1; -; mRNA.
DR   EMBL; AB208800; BAD92037.1; ALT_INIT; mRNA.
DR   EMBL; BX640601; CAE45707.1; -; mRNA.
DR   CCDS; CCDS2393.1; -. [P31327-1]
DR   CCDS; CCDS46505.1; -. [P31327-3]
DR   CCDS; CCDS46506.1; -. [P31327-2]
DR   PIR; JQ1348; JQ1348.
DR   RefSeq; NP_001116105.1; NM_001122633.2. [P31327-3]
DR   RefSeq; NP_001116106.1; NM_001122634.3. [P31327-2]
DR   RefSeq; NP_001866.2; NM_001875.4. [P31327-1]
DR   RefSeq; XP_011508943.1; XM_011510641.2.
DR   RefSeq; XP_011508944.1; XM_011510642.2.
DR   RefSeq; XP_011508945.1; XM_011510643.2.
DR   RefSeq; XP_011508946.1; XM_011510644.2.
DR   UniGene; Hs.149252; -.
DR   PDB; 2YVQ; X-ray; 1.98 A; A=1343-1478.
DR   PDB; 4UTR; X-ray; 2.90 A; C=524-531.
DR   PDB; 4UTV; X-ray; 2.40 A; C=524-531.
DR   PDB; 4UTX; X-ray; 3.10 A; C=524-531.
DR   PDB; 4UTZ; X-ray; 3.30 A; D=524-531.
DR   PDB; 4UU7; X-ray; 3.00 A; D=524-531.
DR   PDB; 4UU8; X-ray; 2.90 A; D=524-531.
DR   PDB; 4UUA; X-ray; 2.80 A; D=524-531.
DR   PDB; 4UUB; X-ray; 2.90 A; D=524-531.
DR   PDB; 5DOT; X-ray; 2.40 A; A/B=40-1500.
DR   PDB; 5DOU; X-ray; 2.60 A; A/B/C/D=40-1500.
DR   PDB; 5OJO; X-ray; 3.10 A; C=524-531.
DR   PDBsum; 2YVQ; -.
DR   PDBsum; 4UTR; -.
DR   PDBsum; 4UTV; -.
DR   PDBsum; 4UTX; -.
DR   PDBsum; 4UTZ; -.
DR   PDBsum; 4UU7; -.
DR   PDBsum; 4UU8; -.
DR   PDBsum; 4UUA; -.
DR   PDBsum; 4UUB; -.
DR   PDBsum; 5DOT; -.
DR   PDBsum; 5DOU; -.
DR   PDBsum; 5OJO; -.
DR   ProteinModelPortal; P31327; -.
DR   SMR; P31327; -.
DR   BioGrid; 107764; 72.
DR   IntAct; P31327; 31.
DR   MINT; P31327; -.
DR   STRING; 9606.ENSP00000402608; -.
DR   ChEMBL; CHEMBL2362990; -.
DR   DrugBank; DB06775; Carglumic Acid.
DR   MEROPS; C26.951; -.
DR   iPTMnet; P31327; -.
DR   PhosphoSitePlus; P31327; -.
DR   SwissPalm; P31327; -.
DR   BioMuta; CPS1; -.
DR   DMDM; 4033707; -.
DR   EPD; P31327; -.
DR   jPOST; P31327; -.
DR   PaxDb; P31327; -.
DR   PeptideAtlas; P31327; -.
DR   PRIDE; P31327; -.
DR   ProteomicsDB; 54782; -.
DR   ProteomicsDB; 54783; -. [P31327-2]
DR   Ensembl; ENST00000233072; ENSP00000233072; ENSG00000021826. [P31327-1]
DR   Ensembl; ENST00000430249; ENSP00000402608; ENSG00000021826. [P31327-3]
DR   Ensembl; ENST00000451903; ENSP00000406136; ENSG00000021826. [P31327-2]
DR   GeneID; 1373; -.
DR   KEGG; hsa:1373; -.
DR   UCSC; uc002vee.5; human. [P31327-1]
DR   CTD; 1373; -.
DR   DisGeNET; 1373; -.
DR   EuPathDB; HostDB:ENSG00000021826.14; -.
DR   GeneCards; CPS1; -.
DR   GeneReviews; CPS1; -.
DR   HGNC; HGNC:2323; CPS1.
DR   HPA; CAB003781; -.
DR   HPA; HPA021400; -.
DR   MalaCards; CPS1; -.
DR   MIM; 237300; phenotype.
DR   MIM; 608307; gene.
DR   MIM; 615371; phenotype.
DR   neXtProt; NX_P31327; -.
DR   OpenTargets; ENSG00000021826; -.
DR   Orphanet; 147; Carbamoyl-phosphate synthetase 1 deficiency.
DR   PharmGKB; PA26840; -.
DR   eggNOG; KOG0370; Eukaryota.
DR   eggNOG; COG0458; LUCA.
DR   eggNOG; COG0505; LUCA.
DR   GeneTree; ENSGT00940000157192; -.
DR   HOGENOM; HOG000234583; -.
DR   HOVERGEN; HBG000279; -.
DR   InParanoid; P31327; -.
DR   KO; K01948; -.
DR   OMA; AVFPFNK; -.
DR   OrthoDB; 1095345at2759; -.
DR   PhylomeDB; P31327; -.
DR   TreeFam; TF331485; -.
DR   BioCyc; MetaCyc:HS00415-MONOMER; -.
DR   BRENDA; 6.3.4.16; 2681.
DR   Reactome; R-HSA-70635; Urea cycle.
DR   SABIO-RK; P31327; -.
DR   ChiTaRS; CPS1; human.
DR   EvolutionaryTrace; P31327; -.
DR   GenomeRNAi; 1373; -.
DR   PRO; PR:P31327; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   Bgee; ENSG00000021826; Expressed in 155 organ(s), highest expression level in liver.
DR   ExpressionAtlas; P31327; baseline and differential.
DR   Genevisible; P31327; HS.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:Ensembl.
DR   GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR   GO; GO:0042645; C:mitochondrial nucleoid; IDA:BHF-UCL.
DR   GO; GO:0005730; C:nucleolus; IDA:HPA.
DR   GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:Ensembl.
DR   GO; GO:0004087; F:carbamoyl-phosphate synthase (ammonia) activity; IMP:BHF-UCL.
DR   GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:InterPro.
DR   GO; GO:0004175; F:endopeptidase activity; IEA:Ensembl.
DR   GO; GO:0016595; F:glutamate binding; IEA:Ensembl.
DR   GO; GO:0072341; F:modified amino acid binding; IDA:UniProtKB.
DR   GO; GO:0005543; F:phospholipid binding; IEA:Ensembl.
DR   GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR   GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR   GO; GO:0055081; P:anion homeostasis; IEA:Ensembl.
DR   GO; GO:0006526; P:arginine biosynthetic process; IBA:GO_Central.
DR   GO; GO:0070409; P:carbamoyl phosphate biosynthetic process; IMP:UniProtKB.
DR   GO; GO:1903718; P:cellular response to ammonia; IMP:BHF-UCL.
DR   GO; GO:0071320; P:cellular response to cAMP; IEA:Ensembl.
DR   GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IEA:Ensembl.
DR   GO; GO:0071377; P:cellular response to glucagon stimulus; IEA:Ensembl.
DR   GO; GO:0071400; P:cellular response to oleic acid; IEA:Ensembl.
DR   GO; GO:0019240; P:citrulline biosynthetic process; NAS:BHF-UCL.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:InterPro.
DR   GO; GO:0070365; P:hepatocyte differentiation; IEA:Ensembl.
DR   GO; GO:0050667; P:homocysteine metabolic process; IDA:UniProtKB.
DR   GO; GO:0007494; P:midgut development; IEA:Ensembl.
DR   GO; GO:0046209; P:nitric oxide metabolic process; IMP:BHF-UCL.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IBA:GO_Central.
DR   GO; GO:0014075; P:response to amine; IEA:Ensembl.
DR   GO; GO:0043200; P:response to amino acid; IEA:Ensembl.
DR   GO; GO:0071548; P:response to dexamethasone; IEA:Ensembl.
DR   GO; GO:0032094; P:response to food; IEA:Ensembl.
DR   GO; GO:0060416; P:response to growth hormone; IEA:Ensembl.
DR   GO; GO:0032496; P:response to lipopolysaccharide; IDA:UniProtKB.
DR   GO; GO:0042594; P:response to starvation; IEA:Ensembl.
DR   GO; GO:0010043; P:response to zinc ion; IEA:Ensembl.
DR   GO; GO:0019433; P:triglyceride catabolic process; IMP:BHF-UCL.
DR   GO; GO:0000050; P:urea cycle; TAS:Reactome.
DR   GO; GO:0042311; P:vasodilation; IMP:BHF-UCL.
DR   CDD; cd01744; GATase1_CPSase; 1.
DR   Gene3D; 1.10.1030.10; -; 1.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   Gene3D; 3.40.50.1380; -; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 3.50.30.20; -; 1.
DR   HAMAP; MF_01209; CPSase_S_chain; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR006275; CarbamoylP_synth_lsu.
DR   InterPro; IPR005480; CarbamoylP_synth_lsu_oligo.
DR   InterPro; IPR036897; CarbamoylP_synth_lsu_oligo_sf.
DR   InterPro; IPR006274; CarbamoylP_synth_ssu.
DR   InterPro; IPR002474; CarbamoylP_synth_ssu_N.
DR   InterPro; IPR036480; CarbP_synth_ssu_N_sf.
DR   InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR005483; CbamoylP_synth_lsu_CPSase_dom.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR035686; CPSase_GATase1.
DR   InterPro; IPR017926; GATASE.
DR   InterPro; IPR011607; MGS-like_dom.
DR   InterPro; IPR036914; MGS-like_dom_sf.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   Pfam; PF02786; CPSase_L_D2; 2.
DR   Pfam; PF02787; CPSase_L_D3; 1.
DR   Pfam; PF00988; CPSase_sm_chain; 1.
DR   Pfam; PF00117; GATase; 1.
DR   Pfam; PF02142; MGS; 1.
DR   PRINTS; PR00098; CPSASE.
DR   SMART; SM01096; CPSase_L_D3; 1.
DR   SMART; SM01097; CPSase_sm_chain; 1.
DR   SMART; SM00851; MGS; 1.
DR   SUPFAM; SSF48108; SSF48108; 1.
DR   SUPFAM; SSF52021; SSF52021; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
DR   SUPFAM; SSF52335; SSF52335; 1.
DR   SUPFAM; SSF52440; SSF52440; 2.
DR   TIGRFAMs; TIGR01369; CPSaseII_lrg; 1.
DR   TIGRFAMs; TIGR01368; CPSaseIIsmall; 1.
DR   PROSITE; PS50975; ATP_GRASP; 2.
DR   PROSITE; PS00866; CPSASE_1; 2.
DR   PROSITE; PS00867; CPSASE_2; 2.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
DR   PROSITE; PS51855; MGS; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Allosteric enzyme; Alternative splicing;
KW   ATP-binding; Complete proteome; Disease mutation; Glycoprotein;
KW   Ligase; Mitochondrion; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Polymorphism; Reference proteome; Repeat; Transit peptide; Urea cycle.
FT   TRANSIT       1     38       Mitochondrion. {ECO:0000250}.
FT   CHAIN        39   1500       Carbamoyl-phosphate synthase [ammonia],
FT                                mitochondrial.
FT                                /FTId=PRO_0000029897.
FT   DOMAIN      219    404       Glutamine amidotransferase type-1.
FT   DOMAIN      551    743       ATP-grasp 1.
FT   DOMAIN     1093   1284       ATP-grasp 2.
FT   DOMAIN     1355   1500       MGS-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01202}.
FT   REGION       39    218       Anthranilate phosphoribosyltransferase
FT                                homolog.
FT   BINDING    1391   1391       Allosteric activator. {ECO:0000305}.
FT   BINDING    1394   1394       Allosteric activator. {ECO:0000305}.
FT   BINDING    1410   1410       Allosteric activator. {ECO:0000305}.
FT   BINDING    1437   1437       Allosteric activator. {ECO:0000305}.
FT   BINDING    1440   1440       Allosteric activator. {ECO:0000305}.
FT   BINDING    1449   1449       Allosteric activator. {ECO:0000305}.
FT   MOD_RES      55     55       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES      55     55       N6-glutaryllysine; alternate.
FT                                {ECO:0000269|PubMed:24703693}.
FT   MOD_RES      55     55       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES      57     57       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES      57     57       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     119    119       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     119    119       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     148    148       Phosphoserine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   MOD_RES     157    157       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     157    157       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     171    171       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     171    171       N6-glutaryllysine; alternate.
FT                                {ECO:0000269|PubMed:24703693}.
FT   MOD_RES     176    176       N6-glutaryllysine.
FT                                {ECO:0000269|PubMed:24703693}.
FT   MOD_RES     182    182       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     197    197       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     207    207       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     207    207       N6-glutaryllysine; alternate.
FT                                {ECO:0000269|PubMed:24703693}.
FT   MOD_RES     207    207       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     210    210       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     210    210       N6-glutaryllysine; alternate.
FT                                {ECO:0000269|PubMed:24703693}.
FT   MOD_RES     214    214       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     214    214       N6-glutaryllysine; alternate.
FT                                {ECO:0000269|PubMed:24703693}.
FT   MOD_RES     214    214       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     219    219       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     219    219       N6-glutaryllysine; alternate.
FT                                {ECO:0000269|PubMed:24703693}.
FT   MOD_RES     228    228       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     228    228       N6-glutaryllysine; alternate.
FT                                {ECO:0000269|PubMed:24703693}.
FT   MOD_RES     237    237       N6-glutaryllysine.
FT                                {ECO:0000269|PubMed:24703693}.
FT   MOD_RES     280    280       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     280    280       N6-glutaryllysine; alternate.
FT                                {ECO:0000269|PubMed:24703693}.
FT   MOD_RES     287    287       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     287    287       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     307    307       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     307    307       N6-glutaryllysine; alternate.
FT                                {ECO:0000269|PubMed:24703693}.
FT   MOD_RES     307    307       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     310    310       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     310    310       N6-glutaryllysine; alternate.
FT                                {ECO:0000269|PubMed:24703693}.
FT   MOD_RES     400    400       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     402    402       N6-glutaryllysine; alternate.
FT                                {ECO:0000269|PubMed:24703693}.
FT   MOD_RES     402    402       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     412    412       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     412    412       N6-glutaryllysine; alternate.
FT                                {ECO:0000269|PubMed:24703693}.
FT   MOD_RES     412    412       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     453    453       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     453    453       N6-glutaryllysine; alternate.
FT                                {ECO:0000269|PubMed:24703693}.
FT   MOD_RES     458    458       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     458    458       N6-glutaryllysine; alternate.
FT                                {ECO:0000269|PubMed:24703693}.
FT   MOD_RES     458    458       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     522    522       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     522    522       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     527    527       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     527    527       N6-glutaryllysine; alternate.
FT                                {ECO:0000269|PubMed:24703693}.
FT   MOD_RES     527    527       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     532    532       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     532    532       N6-glutaryllysine; alternate.
FT                                {ECO:0000269|PubMed:24703693}.
FT   MOD_RES     537    537       Phosphoserine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     540    540       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P07756}.
FT   MOD_RES     553    553       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     553    553       N6-glutaryllysine; alternate.
FT                                {ECO:0000269|PubMed:24703693}.
FT   MOD_RES     553    553       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     560    560       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     560    560       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     569    569       Phosphoserine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   MOD_RES     575    575       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     575    575       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     612    612       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     612    612       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     630    630       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     728    728       N6-glutaryllysine.
FT                                {ECO:0000269|PubMed:24703693}.
FT   MOD_RES     751    751       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     751    751       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     757    757       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     757    757       N6-glutaryllysine; alternate.
FT                                {ECO:0000269|PubMed:24703693}.
FT   MOD_RES     757    757       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     772    772       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     772    772       N6-glutaryllysine; alternate.
FT                                {ECO:0000269|PubMed:24703693}.
FT   MOD_RES     793    793       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     793    793       N6-glutaryllysine; alternate.
FT                                {ECO:0000269|PubMed:24703693}.
FT   MOD_RES     793    793       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     811    811       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     811    811       N6-glutaryllysine; alternate.
FT                                {ECO:0000269|PubMed:24703693}.
FT   MOD_RES     831    831       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     831    831       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     835    835       Phosphoserine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   MOD_RES     841    841       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     841    841       N6-glutaryllysine; alternate.
FT                                {ECO:0000269|PubMed:24703693}.
FT   MOD_RES     856    856       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     856    856       N6-glutaryllysine; alternate.
FT                                {ECO:0000269|PubMed:24703693}.
FT   MOD_RES     869    869       N6-glutaryllysine.
FT                                {ECO:0000269|PubMed:24703693}.
FT   MOD_RES     875    875       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     875    875       N6-glutaryllysine; alternate.
FT                                {ECO:0000269|PubMed:24703693}.
FT   MOD_RES     875    875       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     889    889       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     889    889       N6-glutaryllysine; alternate.
FT                                {ECO:0000269|PubMed:24703693}.
FT   MOD_RES     889    889       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     892    892       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     892    892       N6-glutaryllysine; alternate.
FT                                {ECO:0000269|PubMed:24703693}.
FT   MOD_RES     892    892       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     896    896       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P07756}.
FT   MOD_RES     898    898       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P07756}.
FT   MOD_RES     905    905       N6-glutaryllysine.
FT                                {ECO:0000269|PubMed:24703693}.
FT   MOD_RES     908    908       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     908    908       N6-glutaryllysine; alternate.
FT                                {ECO:0000269|PubMed:24703693}.
FT   MOD_RES     915    915       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     915    915       N6-glutaryllysine; alternate.
FT                                {ECO:0000269|PubMed:24703693}.
FT   MOD_RES     915    915       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     919    919       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     919    919       N6-glutaryllysine; alternate.
FT                                {ECO:0000269|PubMed:24703693}.
FT   MOD_RES     919    919       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES     935    935       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES    1036   1036       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES    1074   1074       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES    1074   1074       N6-glutaryllysine; alternate.
FT                                {ECO:0000269|PubMed:24703693}.
FT   MOD_RES    1074   1074       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES    1079   1079       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163,
FT                                ECO:0000244|PubMed:24275569}.
FT   MOD_RES    1090   1090       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P07756}.
FT   MOD_RES    1093   1093       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P07756}.
FT   MOD_RES    1100   1100       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES    1100   1100       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES    1149   1149       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES    1150   1150       N6-glutaryllysine.
FT                                {ECO:0000269|PubMed:24703693}.
FT   MOD_RES    1168   1168       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES    1168   1168       N6-glutaryllysine; alternate.
FT                                {ECO:0000269|PubMed:24703693}.
FT   MOD_RES    1168   1168       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES    1183   1183       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES    1183   1183       N6-glutaryllysine; alternate.
FT                                {ECO:0000269|PubMed:24703693}.
FT   MOD_RES    1183   1183       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES    1203   1203       Phosphoserine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   MOD_RES    1222   1222       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES    1224   1224       N6-glutaryllysine.
FT                                {ECO:0000269|PubMed:24703693}.
FT   MOD_RES    1232   1232       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES    1232   1232       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES    1269   1269       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES    1269   1269       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES    1291   1291       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES    1291   1291       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES    1356   1356       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES    1356   1356       N6-glutaryllysine; alternate.
FT                                {ECO:0000269|PubMed:24703693}.
FT   MOD_RES    1356   1356       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES    1360   1360       N6-glutaryllysine; alternate.
FT                                {ECO:0000269|PubMed:24703693}.
FT   MOD_RES    1360   1360       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES    1419   1419       Phosphoserine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   MOD_RES    1431   1431       Phosphoserine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   MOD_RES    1444   1444       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES    1444   1444       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES    1471   1471       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES    1471   1471       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES    1479   1479       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES    1479   1479       N6-glutaryllysine; alternate.
FT                                {ECO:0000269|PubMed:24703693}.
FT   MOD_RES    1479   1479       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES    1486   1486       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   MOD_RES    1486   1486       N6-glutaryllysine; alternate.
FT                                {ECO:0000269|PubMed:24703693}.
FT   MOD_RES    1486   1486       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8C196}.
FT   CARBOHYD    537    537       O-linked (GlcNAc) serine; alternate.
FT                                {ECO:0000250}.
FT   CARBOHYD   1331   1331       O-linked (GlcNAc) serine. {ECO:0000250}.
FT   CARBOHYD   1332   1332       O-linked (GlcNAc) threonine.
FT                                {ECO:0000250}.
FT   VAR_SEQ       1    451       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:14702039,
FT                                ECO:0000303|Ref.4}.
FT                                /FTId=VSP_009332.
FT   VAR_SEQ       1      1       M -> MPQIIKM (in isoform 3).
FT                                {ECO:0000303|Ref.11}.
FT                                /FTId=VSP_046685.
FT   VARIANT      43     43       A -> V (in CPS1D).
FT                                {ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_066171.
FT   VARIANT      58     58       G -> D (in CPS1D).
FT                                {ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_066172.
FT   VARIANT      65     65       S -> F (in CPS1D; dbSNP:rs375979196).
FT                                {ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_066173.
FT   VARIANT      71     71       V -> G (in CPS1D).
FT                                {ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_066174.
FT   VARIANT      79     79       G -> E (in CPS1D).
FT                                {ECO:0000269|PubMed:17310273}.
FT                                /FTId=VAR_063560.
FT   VARIANT      87     87       P -> S (in CPS1D).
FT                                {ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_066175.
FT   VARIANT      89     89       Y -> D (in CPS1D).
FT                                {ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_066176.
FT   VARIANT     123    123       S -> F (in CPS1D; modestly decreases
FT                                enzyme activity).
FT                                {ECO:0000269|PubMed:20578160}.
FT                                /FTId=VAR_064062.
FT   VARIANT     123    123       S -> Y (in CPS1D; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:26440671}.
FT                                /FTId=VAR_075404.
FT   VARIANT     165    165       D -> G (in CPS1D).
FT                                {ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_066177.
FT   VARIANT     174    174       R -> W (in CPS1D; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:26440671}.
FT                                /FTId=VAR_075405.
FT   VARIANT     212    212       Y -> N (in CPS1D).
FT                                {ECO:0000269|PubMed:17310273}.
FT                                /FTId=VAR_063561.
FT   VARIANT     224    224       D -> V (in CPS1D).
FT                                {ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_066178.
FT   VARIANT     233    233       R -> C (in CPS1D; dbSNP:rs767905306).
FT                                {ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_066179.
FT   VARIANT     243    243       H -> P (in CPS1D; dbSNP:rs752902711).
FT                                {ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_066180.
FT   VARIANT     258    258       G -> E (in CPS1D).
FT                                {ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_066181.
FT   VARIANT     263    263       G -> E (in CPS1D; dbSNP:rs1471393474).
FT                                {ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_066182.
FT   VARIANT     280    280       K -> N (in CPS1D; dbSNP:rs753751183).
FT                                {ECO:0000269|PubMed:17310273}.
FT                                /FTId=VAR_063562.
FT   VARIANT     301    301       G -> E (in CPS1D; dbSNP:rs973321068).
FT                                {ECO:0000269|PubMed:16737834}.
FT                                /FTId=VAR_066104.
FT   VARIANT     304    304       A -> V (in CPS1D; associated with T-986;
FT                                dbSNP:rs775920437).
FT                                {ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_066183.
FT   VARIANT     317    317       G -> E (in CPS1D; dbSNP:rs1273594946).
FT                                {ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_066184.
FT   VARIANT     337    337       H -> R (in CPS1D; modestly decreases
FT                                enzyme activity; dbSNP:rs28940283).
FT                                {ECO:0000269|PubMed:11474210,
FT                                ECO:0000269|PubMed:20578160}.
FT                                /FTId=VAR_014077.
FT   VARIANT     341    341       L -> S (in CPS1D).
FT                                {ECO:0000269|PubMed:22173106}.
FT                                /FTId=VAR_075806.
FT   VARIANT     344    344       T -> A (polymorphism; no negative effect
FT                                on protein stability, enzyme activity and
FT                                thermal stability; dbSNP:rs1047883).
FT                                {ECO:0000269|PubMed:12853138,
FT                                ECO:0000269|PubMed:23649895,
FT                                ECO:0000269|PubMed:9711878,
FT                                ECO:0000269|Ref.11}.
FT                                /FTId=VAR_006834.
FT   VARIANT     344    344       T -> S (in dbSNP:rs1047883).
FT                                /FTId=VAR_061752.
FT   VARIANT     355    355       N -> D (in CPS1D; around 80% decrease in
FT                                enzyme activity; significant reduction in
FT                                thermal stability; approximately 4-fold
FT                                decrease in the apparent Vmax for ATP,
FT                                bicarbonate and ammonia;
FT                                dbSNP:rs1472190012).
FT                                {ECO:0000269|PubMed:23649895}.
FT                                /FTId=VAR_075406.
FT   VARIANT     358    358       D -> H (in CPS1D; dbSNP:rs149930500).
FT                                {ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_066185.
FT   VARIANT     382    382       P -> L (in CPS1D; dbSNP:rs201407486).
FT                                {ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_066186.
FT   VARIANT     389    389       Y -> C (in CPS1D; around 40% decrease in
FT                                enzyme activity; significant loss of
FT                                thermal stability).
FT                                {ECO:0000269|PubMed:16737834,
FT                                ECO:0000269|PubMed:23649895}.
FT                                /FTId=VAR_066105.
FT   VARIANT     390    390       L -> R (in CPS1D; significant loss of
FT                                protein stability).
FT                                {ECO:0000269|PubMed:16737834,
FT                                ECO:0000269|PubMed:23649895}.
FT                                /FTId=VAR_066106.
FT   VARIANT     401    401       G -> R (in CPS1D; unknown pathological
FT                                significance; associated with N-937 in a
FT                                patient; dbSNP:rs760895692).
FT                                {ECO:0000269|PubMed:21120950,
FT                                ECO:0000269|PubMed:24813853}.
FT                                /FTId=VAR_066187.
FT   VARIANT     431    431       G -> R (in CPS1D; dbSNP:rs778766382).
FT                                {ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_066188.
FT   VARIANT     432    432       G -> V (in CPS1D).
FT                                {ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_066189.
FT   VARIANT     438    438       A -> P (in CPS1D; almost complete loss of
FT                                enzyme activity; dbSNP:rs772497399).
FT                                {ECO:0000269|PubMed:17310273,
FT                                ECO:0000269|PubMed:23649895}.
FT                                /FTId=VAR_063563.
FT   VARIANT     438    438       A -> T (in CPS1D; dbSNP:rs772497399).
FT                                {ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_066190.
FT   VARIANT     450    450       K -> E (in CPS1D).
FT                                {ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_066191.
FT   VARIANT     457    457       V -> G (in CPS1D; dbSNP:rs371350538).
FT                                {ECO:0000269|PubMed:12955727}.
FT                                /FTId=VAR_017562.
FT   VARIANT     471    471       T -> N (in CPS1D).
FT                                {ECO:0000269|PubMed:20578160}.
FT                                /FTId=VAR_064063.
FT   VARIANT     498    498       A -> P (in CPS1D).
FT                                {ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_066192.
FT   VARIANT     530    530       G -> V (found in a patient with VACTERL
FT                                syndrome and postsurgical PHN; variant of
FT                                unknown pathological significance;
FT                                dbSNP:rs1250316045).
FT                                {ECO:0000269|PubMed:21767969}.
FT                                /FTId=VAR_070211.
FT   VARIANT     531    531       V -> E (in CPS1D).
FT                                {ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_066193.
FT   VARIANT     531    531       V -> G (in CPS1D).
FT                                {ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_066194.
FT   VARIANT     544    544       T -> M (in CPS1D; almost complete loss of
FT                                enzyme activity; approximately 60-fold
FT                                increase in the apparent Km for
FT                                bicarbonate and approximately 4-fold
FT                                respective decrease and increase in the
FT                                apparent Vmax and Km for ammonia;
FT                                dbSNP:rs121912592).
FT                                {ECO:0000269|PubMed:21120950,
FT                                ECO:0000269|PubMed:23649895,
FT                                ECO:0000269|PubMed:9711878}.
FT                                /FTId=VAR_006835.
FT   VARIANT     587    587       R -> C (in CPS1D; dbSNP:rs1242028775).
FT                                {ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_066195.
FT   VARIANT     587    587       R -> H (in CPS1D).
FT                                {ECO:0000269|PubMed:17310273,
FT                                ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_063564.
FT   VARIANT     587    587       R -> L (in CPS1D).
FT                                {ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_066196.
FT   VARIANT     589    589       A -> T (in CPS1D; dbSNP:rs777233486).
FT                                {ECO:0000269|PubMed:16737834}.
FT                                /FTId=VAR_066142.
FT   VARIANT     593    593       G -> R (in CPS1D; dbSNP:rs1048119191).
FT                                {ECO:0000269|PubMed:17310273}.
FT                                /FTId=VAR_063565.
FT   VARIANT     597    597       S -> L (in CPS1D).
FT                                {ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_066197.
FT   VARIANT     622    622       V -> M (in CPS1D).
FT                                {ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_066198.
FT   VARIANT     628    628       G -> D (in CPS1D; dbSNP:rs1275599086).
FT                                {ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_066199.
FT   VARIANT     632    632       I -> R (in CPS1D).
FT                                {ECO:0000269|PubMed:21120950,
FT                                ECO:0000269|PubMed:24813853}.
FT                                /FTId=VAR_066200.
FT   VARIANT     638    638       R -> P (in CPS1D; dbSNP:rs757205958).
FT                                {ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_066201.
FT   VARIANT     640    640       A -> S (in CPS1D; dbSNP:rs142693704).
FT                                {ECO:0000269|PubMed:16737834}.
FT                                /FTId=VAR_066143.
FT   VARIANT     648    648       C -> Y (in CPS1D).
FT                                {ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_066202.
FT   VARIANT     651    651       E -> K (in CPS1D).
FT                                {ECO:0000269|PubMed:17310273}.
FT                                /FTId=VAR_063566.
FT   VARIANT     654    654       D -> V (in CPS1D).
FT                                {ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_066203.
FT   VARIANT     661    661       G -> R (in CPS1D).
FT                                {ECO:0000269|PubMed:22173106}.
FT                                /FTId=VAR_075807.
FT   VARIANT     674    674       N -> I (in CPS1D).
FT                                {ECO:0000269|PubMed:17310273}.
FT                                /FTId=VAR_063567.
FT   VARIANT     674    674       N -> K (in CPS1D; dbSNP:rs1248368809).
FT                                {ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_066204.
FT   VARIANT     678    678       Q -> P (in CPS1D; results in a poor
FT                                enzyme expression and solubility; hampers
FT                                correct enzyme folding).
FT                                {ECO:0000269|PubMed:20578160}.
FT                                /FTId=VAR_064064.
FT   VARIANT     698    698       N -> S (in CPS1D).
FT                                {ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_066205.
FT   VARIANT     716    716       N -> K (in CPS1D; dbSNP:rs369061090).
FT                                {ECO:0000269|PubMed:16737834}.
FT                                /FTId=VAR_066144.
FT   VARIANT     718    718       R -> K (in CPS1D).
FT                                {ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_066107.
FT   VARIANT     721    721       R -> Q (in CPS1D; dbSNP:rs752339705).
FT                                {ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_066108.
FT   VARIANT     724    724       A -> P (in CPS1D).
FT                                {ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_066109.
FT   VARIANT     726    726       A -> T (in CPS1D).
FT                                {ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_066110.
FT   VARIANT     767    767       D -> V (in CPS1D).
FT                                {ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_066111.
FT   VARIANT     774    774       P -> L (in CPS1D; the enzyme is
FT                                inactive). {ECO:0000269|PubMed:20578160}.
FT                                /FTId=VAR_064065.
FT   VARIANT     780    780       R -> H (in CPS1D; dbSNP:rs758724746).
FT                                {ECO:0000269|PubMed:17310273,
FT                                ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_063568.
FT   VARIANT     792    792       M -> I (in CPS1D).
FT                                {ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_066112.
FT   VARIANT     803    803       R -> C (in CPS1D; dbSNP:rs201716417).
FT                                {ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_066145.
FT   VARIANT     803    803       R -> G (in CPS1D; dbSNP:rs201716417).
FT                                {ECO:0000269|PubMed:21120950,
FT                                ECO:0000269|PubMed:26440671}.
FT                                /FTId=VAR_066146.
FT   VARIANT     803    803       R -> S (in CPS1D; dbSNP:rs201716417).
FT                                {ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_066147.
FT   VARIANT     805    805       F -> L (in CPS1D).
FT                                {ECO:0000269|PubMed:16737834}.
FT                                /FTId=VAR_066148.
FT   VARIANT     805    805       F -> S (in CPS1D).
FT                                {ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_066149.
FT   VARIANT     810    810       Q -> R (in CPS1D).
FT                                {ECO:0000269|PubMed:12955727}.
FT                                /FTId=VAR_017563.
FT   VARIANT     814    814       R -> W (in CPS1D; dbSNP:rs772782772).
FT                                {ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_066150.
FT   VARIANT     816    816       C -> R (in CPS1D).
FT                                {ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_066151.
FT   VARIANT     843    843       L -> S (in CPS1D; associated in cis with
FT                                E-875; causes 70% decrease of enzyme
FT                                activity; significant decrease in protein
FT                                yield). {ECO:0000269|PubMed:12655559,
FT                                ECO:0000269|PubMed:15164414,
FT                                ECO:0000269|PubMed:24813853}.
FT                                /FTId=VAR_017564.
FT   VARIANT     850    850       R -> C (in CPS1D; moderate decrease in
FT                                protein yield and partial loss of enzyme
FT                                activity; dbSNP:rs1015051007).
FT                                {ECO:0000269|PubMed:17310273,
FT                                ECO:0000269|PubMed:24813853}.
FT                                /FTId=VAR_063569.
FT   VARIANT     850    850       R -> H (in CPS1D; partial loss of enzyme
FT                                activity; dbSNP:rs767694281).
FT                                {ECO:0000269|PubMed:15617192,
FT                                ECO:0000269|PubMed:21120950,
FT                                ECO:0000269|PubMed:24813853,
FT                                ECO:0000269|PubMed:26440671}.
FT                                /FTId=VAR_030675.
FT   VARIANT     871    871       T -> P (in CPS1D; significant decrease in
FT                                protein yield and enzyme activity).
FT                                {ECO:0000269|PubMed:24813853}.
FT                                /FTId=VAR_075407.
FT   VARIANT     875    875       K -> E (polymorphism; associated in cis
FT                                with S-843 in a patient with carbamoyl-
FT                                phosphate synthase deficiency; does not
FT                                affect enzyme activity; significant
FT                                decrease in protein yield and thermal
FT                                stability; dbSNP:rs147062907).
FT                                {ECO:0000269|PubMed:12655559,
FT                                ECO:0000269|PubMed:15164414,
FT                                ECO:0000269|PubMed:24813853,
FT                                ECO:0000269|PubMed:27535533}.
FT                                /FTId=VAR_017565.
FT   VARIANT     911    911       G -> E (in CPS1D; significant decrease in
FT                                protein yield and enzyme activity;
FT                                dbSNP:rs1388955593).
FT                                {ECO:0000269|PubMed:21120950,
FT                                ECO:0000269|PubMed:24813853}.
FT                                /FTId=VAR_066152.
FT   VARIANT     911    911       G -> V (in CPS1D; significant decrease in
FT                                protein yield and enzyme activity).
FT                                {ECO:0000269|PubMed:16737834,
FT                                ECO:0000269|PubMed:24813853}.
FT                                /FTId=VAR_066153.
FT   VARIANT     913    913       S -> L (in CPS1D; significant decrease in
FT                                protein yield and partial loss of enzyme
FT                                activity; dbSNP:rs754706559).
FT                                {ECO:0000269|PubMed:21120950,
FT                                ECO:0000269|PubMed:24813853}.
FT                                /FTId=VAR_066154.
FT   VARIANT     914    914       D -> G (in CPS1D; significant decrease in
FT                                protein yield and enzyme activity).
FT                                {ECO:0000269|PubMed:21120950,
FT                                ECO:0000269|PubMed:24813853}.
FT                                /FTId=VAR_066155.
FT   VARIANT     914    914       D -> H (in CPS1D; significant decrease in
FT                                protein yield and enzyme activity;
FT                                dbSNP:rs765484849).
FT                                {ECO:0000269|PubMed:21120950,
FT                                ECO:0000269|PubMed:24813853}.
FT                                /FTId=VAR_066156.
FT   VARIANT     918    918       S -> P (in CPS1D; significant decrease in
FT                                protein yield and enzyme activity).
FT                                {ECO:0000269|PubMed:15617192,
FT                                ECO:0000269|PubMed:24813853}.
FT                                /FTId=VAR_030676.
FT   VARIANT     932    932       R -> T (in CPS1D; significant decrease in
FT                                protein yield and partial loss of enzyme
FT                                activity). {ECO:0000269|PubMed:21120950,
FT                                ECO:0000269|PubMed:24813853}.
FT                                /FTId=VAR_066157.
FT   VARIANT     937    937       I -> N (in CPS1D; associated with R-401;
FT                                significant decrease in protein yield and
FT                                enzyme activity; dbSNP:rs760714614).
FT                                {ECO:0000269|PubMed:24813853}.
FT                                /FTId=VAR_075408.
FT   VARIANT     949    949       A -> T (in CPS1D; partial loss of enzyme
FT                                activity and significant decrease in
FT                                thermal stability; dbSNP:rs537170841).
FT                                {ECO:0000269|PubMed:21120950,
FT                                ECO:0000269|PubMed:24813853}.
FT                                /FTId=VAR_066158.
FT   VARIANT     958    958       L -> P (in CPS1D; significant decrease in
FT                                protein yield and enzyme activity).
FT                                {ECO:0000269|PubMed:16737834,
FT                                ECO:0000269|PubMed:24813853}.
FT                                /FTId=VAR_066159.
FT   VARIANT     959    959       Y -> C (in CPS1D; significant decrease in
FT                                protein yield and thermal stability;
FT                                partial loss of enzyme activity;
FT                                dbSNP:rs1191587211).
FT                                {ECO:0000269|PubMed:21120950,
FT                                ECO:0000269|PubMed:24813853}.
FT                                /FTId=VAR_066160.
FT   VARIANT     962    962       Y -> C (in CPS1D; significant decrease in
FT                                protein yield and partial loss of enzyme
FT                                activity; dbSNP:rs955666400).
FT                                {ECO:0000269|PubMed:21120950,
FT                                ECO:0000269|PubMed:24813853}.
FT                                /FTId=VAR_066161.
FT   VARIANT     964    964       G -> D (in CPS1D; significant decrease in
FT                                protein yield and enzyme activity;
FT                                dbSNP:rs534815243).
FT                                {ECO:0000269|PubMed:22173106,
FT                                ECO:0000269|PubMed:24813853}.
FT                                /FTId=VAR_075409.
FT   VARIANT     978    978       V -> E (in CPS1D).
FT                                {ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_066113.
FT   VARIANT     982    982       G -> D (in CPS1D; dbSNP:rs121912595).
FT                                {ECO:0000269|PubMed:17310273}.
FT                                /FTId=VAR_063570.
FT   VARIANT     982    982       G -> S (in CPS1D; dbSNP:rs757059355).
FT                                {ECO:0000269|PubMed:16737834}.
FT                                /FTId=VAR_066162.
FT   VARIANT     982    982       G -> V (in CPS1D; dbSNP:rs121912595).
FT                                {ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_066114.
FT   VARIANT     984    984       Y -> H (in CPS1D).
FT                                {ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_066115.
FT   VARIANT     986    986       I -> T (in CPS1D; associated with V-304).
FT                                {ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_066116.
FT   VARIANT     987    987       G -> C (in CPS1D; may affect splicing).
FT                                {ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_066117.
FT   VARIANT     992    992       F -> S (in CPS1D; dbSNP:rs990390709).
FT                                {ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_066118.
FT   VARIANT     998    998       S -> F (in CPS1D; dbSNP:rs1404696893).
FT                                {ECO:0000269|PubMed:16737834}.
FT                                /FTId=VAR_066163.
FT   VARIANT    1016   1016       N -> S (in CPS1D; dbSNP:rs749238466).
FT                                {ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_066119.
FT   VARIANT    1017   1017       P -> L (in CPS1D).
FT                                {ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_066120.
FT   VARIANT    1022   1022       T -> I (in CPS1D; dbSNP:rs1437651658).
FT                                {ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_066121.
FT   VARIANT    1034   1034       E -> G (in CPS1D).
FT                                {ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_066122.
FT   VARIANT    1045   1045       H -> R (in CPS1D; dbSNP:rs1241423400).
FT                                {ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_066123.
FT   VARIANT    1054   1054       I -> R (in CPS1D).
FT                                {ECO:0000269|PubMed:11388595}.
FT                                /FTId=VAR_066164.
FT   VARIANT    1059   1059       Q -> R (in CPS1D).
FT                                {ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_066124.
FT   VARIANT    1065   1065       A -> E (in CPS1D; dbSNP:rs770471782).
FT                                {ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_066125.
FT   VARIANT    1089   1089       R -> C (in CPS1D; dbSNP:rs1392559810).
FT                                {ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_066126.
FT   VARIANT    1089   1089       R -> L (in CPS1D; dbSNP:rs1280211937).
FT                                {ECO:0000269|PubMed:16737834}.
FT                                /FTId=VAR_066165.
FT   VARIANT    1103   1103       Q -> R (in CPS1D).
FT                                {ECO:0000269|PubMed:17310273}.
FT                                /FTId=VAR_063571.
FT   VARIANT    1141   1141       V -> G (in CPS1D).
FT                                {ECO:0000269|PubMed:17310273}.
FT                                /FTId=VAR_063572.
FT   VARIANT    1155   1155       A -> E (in CPS1D).
FT                                {ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_066127.
FT   VARIANT    1155   1155       A -> V (in CPS1D; dbSNP:rs766125631).
FT                                {ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_066128.
FT   VARIANT    1167   1167       T -> R (in CPS1D).
FT                                {ECO:0000269|PubMed:22173106}.
FT                                /FTId=VAR_075808.
FT   VARIANT    1194   1194       E -> D (in CPS1D).
FT                                {ECO:0000269|PubMed:24813853}.
FT                                /FTId=VAR_075410.
FT   VARIANT    1195   1195       H -> P (in CPS1D).
FT                                {ECO:0000269|PubMed:17310273}.
FT                                /FTId=VAR_063573.
FT   VARIANT    1203   1203       S -> L (in CPS1D; dbSNP:rs149518280).
FT                                {ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_066129.
FT   VARIANT    1203   1203       S -> P (in CPS1D; dbSNP:rs1319489001).
FT                                {ECO:0000269|PubMed:16737834}.
FT                                /FTId=VAR_066166.
FT   VARIANT    1205   1205       D -> N (in CPS1D).
FT                                {ECO:0000269|PubMed:16737834}.
FT                                /FTId=VAR_066167.
FT   VARIANT    1215   1215       I -> V (in CPS1D; dbSNP:rs141373204).
FT                                {ECO:0000269|PubMed:17310273}.
FT                                /FTId=VAR_063574.
FT   VARIANT    1228   1228       R -> Q (in CPS1D; dbSNP:rs778117194).
FT                                {ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_066130.
FT   VARIANT    1241   1241       N -> K (in CPS1D).
FT                                {ECO:0000269|PubMed:17310273}.
FT                                /FTId=VAR_063575.
FT   VARIANT    1254   1254       I -> F (in CPS1D; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:26440671}.
FT                                /FTId=VAR_075411.
FT   VARIANT    1255   1255       E -> D (in CPS1D).
FT                                {ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_066131.
FT   VARIANT    1262   1262       R -> P (in CPS1D).
FT                                {ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_066132.
FT   VARIANT    1262   1262       R -> Q (in CPS1D; dbSNP:rs750670270).
FT                                {ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_066133.
FT   VARIANT    1266   1266       F -> S (in dbSNP:rs1047886).
FT                                {ECO:0000269|PubMed:1840546}.
FT                                /FTId=VAR_017566.
FT   VARIANT    1274   1274       D -> H (in CPS1D).
FT                                {ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_066134.
FT   VARIANT    1283   1283       M -> L (in dbSNP:rs1047887).
FT                                {ECO:0000269|PubMed:1840546}.
FT                                /FTId=VAR_017567.
FT   VARIANT    1327   1327       C -> R (in CPS1D).
FT                                {ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_066135.
FT   VARIANT    1331   1331       S -> P (in CPS1D).
FT                                {ECO:0000269|PubMed:16737834}.
FT                                /FTId=VAR_066168.
FT   VARIANT    1333   1333       G -> E (in CPS1D; dbSNP:rs372645328).
FT                                {ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_066136.
FT   VARIANT    1363   1366       Missing (in CPS1D; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:26440671}.
FT                                /FTId=VAR_075412.
FT   VARIANT    1371   1371       R -> L (in CPS1D).
FT                                {ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_066137.
FT   VARIANT    1376   1376       G -> S (polymorphism; no functional
FT                                consequences; no negative effect on
FT                                protein stability, enzyme activity and
FT                                thermal stability; dbSNP:rs140578009).
FT                                {ECO:0000269|PubMed:12853138,
FT                                ECO:0000269|PubMed:20578160,
FT                                ECO:0000269|PubMed:23649895}.
FT                                /FTId=VAR_017568.
FT   VARIANT    1378   1378       A -> T (in CPS1D; significant reduction
FT                                in thermal stability;
FT                                dbSNP:rs1245373037).
FT                                {ECO:0000269|PubMed:16737834,
FT                                ECO:0000269|PubMed:23649895}.
FT                                /FTId=VAR_066169.
FT   VARIANT    1381   1381       L -> S (in CPS1D; significant loss of
FT                                protein stability).
FT                                {ECO:0000269|PubMed:23649895}.
FT                                /FTId=VAR_075413.
FT   VARIANT    1391   1391       T -> M (in CPS1D; dbSNP:rs1392934477).
FT                                {ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_066138.
FT   VARIANT    1398   1398       L -> V (in CPS1D).
FT                                {ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_066139.
FT   VARIANT    1406   1406       T -> N (polymorphism; associated with
FT                                susceptibility to neonatal pulmonary
FT                                hypertension; also highly associated with
FT                                hepatocellular carcinoma progression;
FT                                dbSNP:rs1047891).
FT                                {ECO:0000269|PubMed:11407344,
FT                                ECO:0000269|PubMed:12853138,
FT                                ECO:0000269|PubMed:12955727,
FT                                ECO:0000269|PubMed:1840546,
FT                                ECO:0000269|PubMed:20520828,
FT                                ECO:0000269|PubMed:21767969,
FT                                ECO:0000269|PubMed:24237036}.
FT                                /FTId=VAR_017569.
FT   VARIANT    1411   1411       P -> L (in CPS1D; modestly decreases
FT                                enzyme activity; dbSNP:rs1202306773).
FT                                {ECO:0000269|PubMed:16737834,
FT                                ECO:0000269|PubMed:20578160}.
FT                                /FTId=VAR_064066.
FT   VARIANT    1439   1439       P -> L (in CPS1D).
FT                                {ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_066140.
FT   VARIANT    1443   1443       T -> A (in CPS1D; almost complete loss of
FT                                enzyme activity; approximately 10-fold
FT                                decrease in the apparent Vmax for
FT                                bicarbonate, ammonia and ATP; decreased
FT                                affinity for NAG).
FT                                {ECO:0000269|PubMed:16737834,
FT                                ECO:0000269|PubMed:23649895}.
FT                                /FTId=VAR_066170.
FT   VARIANT    1453   1453       R -> Q (in CPS1D; the enzyme is
FT                                inactive). {ECO:0000269|PubMed:20578160}.
FT                                /FTId=VAR_064067.
FT   VARIANT    1453   1453       R -> W (in CPS1D; the enzyme is inactive;
FT                                dbSNP:rs933813349).
FT                                {ECO:0000269|PubMed:20578160,
FT                                ECO:0000269|PubMed:21120950}.
FT                                /FTId=VAR_064068.
FT   VARIANT    1462   1462       P -> R (in CPS1D).
FT                                {ECO:0000269|PubMed:21120950,
FT                                ECO:0000269|PubMed:24813853}.
FT                                /FTId=VAR_066141.
FT   VARIANT    1491   1491       Y -> H (in CPS1D; triggers a large
FT                                decrease in the apparent affinity for N-
FT                                acetyl-L-glutamate (NAG)).
FT                                {ECO:0000269|PubMed:20578160}.
FT                                /FTId=VAR_064069.
FT   CONFLICT    111    111       A -> S (in Ref. 1; BAA14328).
FT                                {ECO:0000305}.
FT   CONFLICT    279    279       R -> Q (in Ref. 1; BAA14328).
FT                                {ECO:0000305}.
FT   CONFLICT    338    338       G -> C (in Ref. 1; BAA14328).
FT                                {ECO:0000305}.
FT   CONFLICT    718    722       RLSRS -> KMSPN (in Ref. 1; BAA14328).
FT                                {ECO:0000305}.
FT   CONFLICT    729    729       A -> T (in Ref. 1; BAA14328).
FT                                {ECO:0000305}.
FT   CONFLICT    749    749       E -> G (in Ref. 1; BAA14328).
FT                                {ECO:0000305}.
FT   CONFLICT    912    912       F -> L (in Ref. 6; CAE45707).
FT                                {ECO:0000305}.
FT   CONFLICT   1161   1162       EH -> AT (in Ref. 1; BAA14328).
FT                                {ECO:0000305}.
FT   CONFLICT   1204   1205       GD -> EN (in Ref. 1; BAA14328).
FT                                {ECO:0000305}.
FT   CONFLICT   1254   1254       I -> N (in Ref. 1; BAA14328).
FT                                {ECO:0000305}.
FT   CONFLICT   1303   1303       A -> V (in Ref. 1; BAA14328).
FT                                {ECO:0000305}.
FT   STRAND       45     50       {ECO:0000244|PDB:5DOT}.
FT   STRAND       55     60       {ECO:0000244|PDB:5DOT}.
FT   STRAND       67     74       {ECO:0000244|PDB:5DOT}.
FT   HELIX        80     83       {ECO:0000244|PDB:5DOT}.
FT   HELIX        87     89       {ECO:0000244|PDB:5DOT}.
FT   STRAND       92    101       {ECO:0000244|PDB:5DOT}.
FT   STRAND      116    125       {ECO:0000244|PDB:5DOT}.
FT   STRAND      129    132       {ECO:0000244|PDB:5DOT}.
FT   STRAND      134    136       {ECO:0000244|PDB:5DOT}.
FT   HELIX       149    155       {ECO:0000244|PDB:5DOT}.
FT   STRAND      160    163       {ECO:0000244|PDB:5DOT}.
FT   HELIX       166    173       {ECO:0000244|PDB:5DOT}.
FT   STRAND      179    185       {ECO:0000244|PDB:5DOT}.
FT   HELIX       195    197       {ECO:0000244|PDB:5DOT}.
FT   HELIX       200    204       {ECO:0000244|PDB:5DOT}.
FT   STRAND      210    213       {ECO:0000244|PDB:5DOT}.
FT   STRAND      217    226       {ECO:0000244|PDB:5DOT}.
FT   HELIX       229    237       {ECO:0000244|PDB:5DOT}.
FT   STRAND      240    246       {ECO:0000244|PDB:5DOT}.
FT   STRAND      257    263       {ECO:0000244|PDB:5DOT}.
FT   HELIX       268    270       {ECO:0000244|PDB:5DOT}.
FT   HELIX       272    283       {ECO:0000244|PDB:5DOT}.
FT   STRAND      290    294       {ECO:0000244|PDB:5DOT}.
FT   HELIX       295    304       {ECO:0000244|PDB:5DOT}.
FT   STRAND      308    324       {ECO:0000244|PDB:5DOT}.
FT   TURN        325    327       {ECO:0000244|PDB:5DOT}.
FT   STRAND      330    341       {ECO:0000244|PDB:5DOT}.
FT   STRAND      349    355       {ECO:0000244|PDB:5DOT}.
FT   TURN        356    358       {ECO:0000244|PDB:5DOT}.
FT   STRAND      361    376       {ECO:0000244|PDB:5DOT}.
FT   STRAND      381    383       {ECO:0000244|PDB:5DOT}.
FT   HELIX       389    400       {ECO:0000244|PDB:5DOT}.
FT   HELIX       407    409       {ECO:0000244|PDB:5DOT}.
FT   STRAND      423    428       {ECO:0000244|PDB:5DOT}.
FT   STRAND      435    437       {ECO:0000244|PDB:5DOT}.
FT   HELIX       445    454       {ECO:0000244|PDB:5DOT}.
FT   STRAND      458    462       {ECO:0000244|PDB:5DOT}.
FT   HELIX       469    471       {ECO:0000244|PDB:5DOT}.
FT   STRAND      473    475       {ECO:0000244|PDB:5DOU}.
FT   STRAND      480    483       {ECO:0000244|PDB:5DOT}.
FT   HELIX       489    499       {ECO:0000244|PDB:5DOT}.
FT   STRAND      502    505       {ECO:0000244|PDB:5DOT}.
FT   STRAND      507    509       {ECO:0000244|PDB:5DOT}.
FT   HELIX       510    522       {ECO:0000244|PDB:5DOT}.
FT   HELIX       527    530       {ECO:0000244|PDB:4UTV}.
FT   HELIX       538    545       {ECO:0000244|PDB:5DOT}.
FT   HELIX       547    555       {ECO:0000244|PDB:5DOT}.
FT   TURN        556    558       {ECO:0000244|PDB:5DOT}.
FT   STRAND      563    569       {ECO:0000244|PDB:5DOU}.
FT   HELIX       570    580       {ECO:0000244|PDB:5DOU}.
FT   STRAND      582    590       {ECO:0000244|PDB:5DOU}.
FT   TURN        593    596       {ECO:0000244|PDB:5DOU}.
FT   STRAND      598    602       {ECO:0000244|PDB:5DOU}.
FT   HELIX       603    614       {ECO:0000244|PDB:5DOU}.
FT   STRAND      620    624       {ECO:0000244|PDB:5DOU}.
FT   STRAND      629    638       {ECO:0000244|PDB:5DOT}.
FT   STRAND      644    653       {ECO:0000244|PDB:5DOT}.
FT   HELIX       660    662       {ECO:0000244|PDB:5DOU}.
FT   STRAND      665    668       {ECO:0000244|PDB:5DOT}.
FT   HELIX       674    690       {ECO:0000244|PDB:5DOT}.
FT   STRAND      695    703       {ECO:0000244|PDB:5DOT}.
FT   STRAND      710    716       {ECO:0000244|PDB:5DOT}.
FT   HELIX       721    730       {ECO:0000244|PDB:5DOT}.
FT   HELIX       734    742       {ECO:0000244|PDB:5DOT}.
FT   HELIX       747    749       {ECO:0000244|PDB:5DOT}.
FT   TURN        753    755       {ECO:0000244|PDB:5DOT}.
FT   STRAND      756    760       {ECO:0000244|PDB:5DOT}.
FT   STRAND      767    775       {ECO:0000244|PDB:5DOT}.
FT   STRAND      796    804       {ECO:0000244|PDB:5DOT}.
FT   HELIX       805    816       {ECO:0000244|PDB:5DOT}.
FT   HELIX       828    830       {ECO:0000244|PDB:5DOT}.
FT   HELIX       839    844       {ECO:0000244|PDB:5DOT}.
FT   HELIX       850    859       {ECO:0000244|PDB:5DOT}.
FT   HELIX       864    871       {ECO:0000244|PDB:5DOT}.
FT   HELIX       875    892       {ECO:0000244|PDB:5DOT}.
FT   TURN        896    898       {ECO:0000244|PDB:5DOT}.
FT   HELIX       901    909       {ECO:0000244|PDB:5DOT}.
FT   HELIX       914    921       {ECO:0000244|PDB:5DOT}.
FT   HELIX       925    934       {ECO:0000244|PDB:5DOT}.
FT   STRAND      940    943       {ECO:0000244|PDB:5DOT}.
FT   STRAND      957    963       {ECO:0000244|PDB:5DOT}.
FT   STRAND      976    979       {ECO:0000244|PDB:5DOT}.
FT   HELIX       991   1005       {ECO:0000244|PDB:5DOT}.
FT   STRAND     1010   1014       {ECO:0000244|PDB:5DOT}.
FT   TURN       1024   1026       {ECO:0000244|PDB:5DOT}.
FT   STRAND     1027   1032       {ECO:0000244|PDB:5DOT}.
FT   HELIX      1037   1047       {ECO:0000244|PDB:5DOT}.
FT   STRAND     1050   1053       {ECO:0000244|PDB:5DOT}.
FT   STRAND     1055   1057       {ECO:0000244|PDB:5DOU}.
FT   HELIX      1059   1063       {ECO:0000244|PDB:5DOT}.
FT   HELIX      1065   1070       {ECO:0000244|PDB:5DOT}.
FT   HELIX      1080   1087       {ECO:0000244|PDB:5DOT}.
FT   HELIX      1089   1098       {ECO:0000244|PDB:5DOT}.
FT   STRAND     1106   1109       {ECO:0000244|PDB:5DOT}.
FT   HELIX      1112   1122       {ECO:0000244|PDB:5DOT}.
FT   STRAND     1126   1129       {ECO:0000244|PDB:5DOT}.
FT   STRAND     1140   1142       {ECO:0000244|PDB:5DOT}.
FT   HELIX      1145   1151       {ECO:0000244|PDB:5DOT}.
FT   STRAND     1164   1167       {ECO:0000244|PDB:5DOT}.
FT   STRAND     1174   1183       {ECO:0000244|PDB:5DOT}.
FT   STRAND     1186   1197       {ECO:0000244|PDB:5DOT}.
FT   HELIX      1203   1205       {ECO:0000244|PDB:5DOU}.
FT   STRAND     1208   1211       {ECO:0000244|PDB:5DOT}.
FT   HELIX      1217   1233       {ECO:0000244|PDB:5DOT}.
FT   STRAND     1238   1247       {ECO:0000244|PDB:5DOT}.
FT   STRAND     1250   1259       {ECO:0000244|PDB:5DOT}.
FT   HELIX      1264   1271       {ECO:0000244|PDB:5DOT}.
FT   HELIX      1275   1283       {ECO:0000244|PDB:5DOT}.
FT   STRAND     1296   1298       {ECO:0000244|PDB:5DOT}.
FT   STRAND     1306   1310       {ECO:0000244|PDB:5DOT}.
FT   STRAND     1312   1318       {ECO:0000244|PDB:5DOT}.
FT   STRAND     1322   1324       {ECO:0000244|PDB:5DOT}.
FT   STRAND     1327   1332       {ECO:0000244|PDB:5DOT}.
FT   STRAND     1335   1341       {ECO:0000244|PDB:5DOT}.
FT   HELIX      1344   1350       {ECO:0000244|PDB:2YVQ}.
FT   STRAND     1360   1365       {ECO:0000244|PDB:2YVQ}.
FT   HELIX      1368   1370       {ECO:0000244|PDB:2YVQ}.
FT   HELIX      1371   1382       {ECO:0000244|PDB:2YVQ}.
FT   TURN       1383   1385       {ECO:0000244|PDB:2YVQ}.
FT   STRAND     1387   1391       {ECO:0000244|PDB:2YVQ}.
FT   HELIX      1392   1400       {ECO:0000244|PDB:2YVQ}.
FT   STRAND     1406   1408       {ECO:0000244|PDB:2YVQ}.
FT   HELIX      1411   1413       {ECO:0000244|PDB:2YVQ}.
FT   STRAND     1418   1421       {ECO:0000244|PDB:5DOT}.
FT   HELIX      1423   1428       {ECO:0000244|PDB:2YVQ}.
FT   STRAND     1434   1437       {ECO:0000244|PDB:2YVQ}.
FT   HELIX      1443   1445       {ECO:0000244|PDB:2YVQ}.
FT   HELIX      1446   1458       {ECO:0000244|PDB:2YVQ}.
FT   HELIX      1467   1475       {ECO:0000244|PDB:2YVQ}.
FT   TURN       1486   1491       {ECO:0000244|PDB:5DOT}.
SQ   SEQUENCE   1500 AA;  164939 MW;  E53A22D77563961D CRC64;
     MTRILTAFKV VRTLKTGFGF TNVTAHQKWK FSRPGIRLLS VKAQTAHIVL EDGTKMKGYS
     FGHPSSVAGE VVFNTGLGGY PEAITDPAYK GQILTMANPI IGNGGAPDTT ALDELGLSKY
     LESNGIKVSG LLVLDYSKDY NHWLATKSLG QWLQEEKVPA IYGVDTRMLT KIIRDKGTML
     GKIEFEGQPV DFVDPNKQNL IAEVSTKDVK VYGKGNPTKV VAVDCGIKNN VIRLLVKRGA
     EVHLVPWNHD FTKMEYDGIL IAGGPGNPAL AEPLIQNVRK ILESDRKEPL FGISTGNLIT
     GLAAGAKTYK MSMANRGQNQ PVLNITNKQA FITAQNHGYA LDNTLPAGWK PLFVNVNDQT
     NEGIMHESKP FFAVQFHPEV TPGPIDTEYL FDSFFSLIKK GKATTITSVL PKPALVASRV
     EVSKVLILGS GGLSIGQAGE FDYSGSQAVK AMKEENVKTV LMNPNIASVQ TNEVGLKQAD
     TVYFLPITPQ FVTEVIKAEQ PDGLILGMGG QTALNCGVEL FKRGVLKEYG VKVLGTSVES
     IMATEDRQLF SDKLNEINEK IAPSFAVESI EDALKAADTI GYPVMIRSAY ALGGLGSGIC
     PNRETLMDLS TKAFAMTNQI LVEKSVTGWK EIEYEVVRDA DDNCVTVCNM ENVDAMGVHT
     GDSVVVAPAQ TLSNAEFQML RRTSINVVRH LGIVGECNIQ FALHPTSMEY CIIEVNARLS
     RSSALASKAT GYPLAFIAAK IALGIPLPEI KNVVSGKTSA CFEPSLDYMV TKIPRWDLDR
     FHGTSSRIGS SMKSVGEVMA IGRTFEESFQ KALRMCHPSI EGFTPRLPMN KEWPSNLDLR
     KELSEPSSTR IYAIAKAIDD NMSLDEIEKL TYIDKWFLYK MRDILNMEKT LKGLNSESMT
     EETLKRAKEI GFSDKQISKC LGLTEAQTRE LRLKKNIHPW VKQIDTLAAE YPSVTNYLYV
     TYNGQEHDVN FDDHGMMVLG CGPYHIGSSV EFDWCAVSSI RTLRQLGKKT VVVNCNPETV
     STDFDECDKL YFEELSLERI LDIYHQEACG GCIISVGGQI PNNLAVPLYK NGVKIMGTSP
     LQIDRAEDRS IFSAVLDELK VAQAPWKAVN TLNEALEFAK SVDYPCLLRP SYVLSGSAMN
     VVFSEDEMKK FLEEATRVSQ EHPVVLTKFV EGAREVEMDA VGKDGRVISH AISEHVEDAG
     VHSGDATLML PTQTISQGAI EKVKDATRKI AKAFAISGPF NVQFLVKGND VLVIECNLRA
     SRSFPFVSKT LGVDFIDVAT KVMIGENVDE KHLPTLDHPI IPADYVAIKA PMFSWPRLRD
     ADPILRCEMA STGEVACFGE GIHTAFLKAM LSTGFKIPQK GILIGIQQSF RPRFLGVAEQ
     LHNEGFKLFA TEATSDWLNA NNVPATPVAW PSQEGQNPSL SSIRKLIRDG SIDLVINLPN
     NNTKFVHDNY VIRRTAVDSG IPLLTNFQVT KLFAEAVQKS RKVDSKSLFH YRQYSAGKAA
//
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