ID PYR1_HUMAN Reviewed; 2225 AA.
AC P27708; D6W552; Q6P0Q0;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 3.
DT 01-MAY-2013, entry version 156.
DE RecName: Full=CAD protein;
DE Includes:
DE RecName: Full=Glutamine-dependent carbamoyl-phosphate synthase;
DE EC=6.3.5.5;
DE Includes:
DE RecName: Full=Aspartate carbamoyltransferase;
DE EC=2.1.3.2;
DE Includes:
DE RecName: Full=Dihydroorotase;
DE EC=3.5.2.3;
GN Name=CAD;
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].
RC TISSUE=Fetal lung fibroblast;
RX PubMed=8619816; DOI=10.1006/bbrc.1996.0213;
RA Iwahana H., Fujimura M., Ii S., Kondo M., Moritani M., Takahashi Y.,
RA Yamaoka T., Yoshimoto K., Itakura M.;
RT "Molecular cloning of a human cDNA encoding a trifunctional enzyme of
RT carbamoyl-phosphate synthetase-aspartate transcarbamoylase-
RT dihydroorotase in de Novo pyrimidine synthesis.";
RL Biochem. Biophys. Res. Commun. 219:249-255(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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 [4]
RP PROTEIN SEQUENCE OF 2-13; 157-165; 169-177; 359-371; 501-516; 548-555;
RP 599-606; 697-719; 761-778; 843-854; 932-944; 1034-1048; 1067-1075;
RP 1110-1127; 1229-1240; 1263-1270; 1313-1323; 1326-1333; 1658-1667;
RP 1723-1731; 1840-1848; 1976-1986; 2025-2036; 2103-2110; 2179-2187 AND
RP 2215-2225, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND
RP MASS SPECTROMETRY.
RC TISSUE=Colon adenocarcinoma, and Hepatoma;
RA Bienvenut W.V., Dhillon A.S., Matallanas D., Murray L., Brunton V.G.,
RA Cooper W.N., Boldt K., von Kriegsheim A.F., Kolch W., Frame M.C.;
RL Submitted (FEB-2008) to UniProtKB.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1752-2225.
RX PubMed=1979741; DOI=10.1089/dna.1990.9.667;
RA Davidson J.N., Rao G.N., Niswander L., Andreano C., Tamer C.,
RA Chen K.C.;
RT "Organization and nucleotide sequence of the 3' end of the human CAD
RT gene.";
RL DNA Cell Biol. 9:667-676(1990).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1859, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1859, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1859 AND THR-1884, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1884, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-747 AND LYS-1411, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1859; SER-1900 AND
RP THR-1906, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1406 AND SER-1859, AND
RP MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [15]
RP VARIANTS [LARGE SCALE ANALYSIS] GLN-177 AND CYS-735.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: This protein is a "fusion" protein encoding four
CC enzymatic activities of the pyrimidine pathway (GATase, CPSase,
CC ATCase and DHOase).
CC -!- CATALYTIC ACTIVITY: 2 ATP + L-glutamine + HCO(3)(-) + H(2)O = 2
CC ADP + phosphate + L-glutamate + carbamoyl phosphate.
CC -!- CATALYTIC ACTIVITY: Carbamoyl phosphate + L-aspartate = phosphate
CC + N-carbamoyl-L-aspartate.
CC -!- CATALYTIC ACTIVITY: (S)-dihydroorotate + H(2)O = N-carbamoyl-L-
CC aspartate.
CC -!- COFACTOR: Binds 1 zinc ion per subunit (for dihydroorotase
CC activity) (Potential).
CC -!- ENZYME REGULATION: Allosterically regulated and controlled by
CC phosphorylation. 5-phosphoribose 1-diphosphate is an activator
CC while UMP is an inhibitor of the CPSase reaction.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC pathway; (S)-dihydroorotate from bicarbonate: step 1/3.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC pathway; (S)-dihydroorotate from bicarbonate: step 2/3.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC pathway; (S)-dihydroorotate from bicarbonate: step 3/3.
CC -!- SUBUNIT: Homohexamer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- MISCELLANEOUS: GATase (glutamine amidotransferase) and CPSase
CC (carbamoyl phosphate synthase) form together the glutamine-
CC dependent CPSase (GD-CPSase) (EC 6.3.5.5).
CC -!- SIMILARITY: In the central section; belongs to the DHOase family.
CC -!- SIMILARITY: Contains 2 ATP-grasp domains.
CC -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Aspartate carbamoyltransferase
CC entry;
CC URL="http://en.wikipedia.org/wiki/Aspartate_carbamoyltransferase";
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DR EMBL; D78586; BAA11423.1; -; mRNA.
DR EMBL; CH471053; EAX00612.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00613.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00614.1; -; Genomic_DNA.
DR EMBL; BC065510; AAH65510.1; -; mRNA.
DR EMBL; M38561; AAA51907.1; -; Genomic_DNA.
DR IPI; IPI00301263; -.
DR PIR; A36240; A36240.
DR RefSeq; NP_004332.2; NM_004341.3.
DR UniGene; Hs.377010; -.
DR ProteinModelPortal; P27708; -.
DR DIP; DIP-39484N; -.
DR IntAct; P27708; 16.
DR MINT; MINT-5000537; -.
DR STRING; 9606.ENSP00000264705; -.
DR MEROPS; C26.952; -.
DR PhosphoSite; P27708; -.
DR DMDM; 50403731; -.
DR PaxDb; P27708; -.
DR PeptideAtlas; P27708; -.
DR PRIDE; P27708; -.
DR Ensembl; ENST00000264705; ENSP00000264705; ENSG00000084774.
DR GeneID; 790; -.
DR KEGG; hsa:790; -.
DR UCSC; uc002rji.3; human.
DR CTD; 790; -.
DR GeneCards; GC02P027440; -.
DR HGNC; HGNC:1424; CAD.
DR HPA; CAB007781; -.
DR MIM; 114010; gene.
DR neXtProt; NX_P27708; -.
DR PharmGKB; PA26023; -.
DR eggNOG; COG0458; -.
DR HOGENOM; HOG000234584; -.
DR HOVERGEN; HBG000279; -.
DR InParanoid; P27708; -.
DR KO; K11540; -.
DR OrthoDB; EOG46WZ7G; -.
DR PhylomeDB; P27708; -.
DR BioCyc; MetaCyc:ENSG00000084774-MONOMER; -.
DR BRENDA; 3.5.2.3; 2681.
DR Reactome; REACT_111217; Metabolism.
DR UniPathway; UPA00070; UER00115.
DR UniPathway; UPA00070; UER00116.
DR UniPathway; UPA00070; UER00117.
DR BindingDB; P27708; -.
DR ChEMBL; CHEMBL3093; -.
DR ChiTaRS; cad; human.
DR DrugBank; DB00128; L-Aspartic Acid.
DR DrugBank; DB00130; L-Glutamine.
DR GenomeRNAi; 790; -.
DR NextBio; 3214; -.
DR PMAP-CutDB; P27708; -.
DR ArrayExpress; P27708; -.
DR Bgee; P27708; -.
DR CleanEx; HS_CAD; -.
DR Genevestigator; P27708; -.
DR GermOnline; ENSG00000084774; Homo sapiens.
DR GO; GO:0005829; C:cytosol; IDA:BHF-UCL.
DR GO; GO:0043025; C:neuronal cell body; ISS:BHF-UCL.
DR GO; GO:0016363; C:nuclear matrix; IDA:BHF-UCL.
DR GO; GO:0043234; C:protein complex; IEA:Compara.
DR GO; GO:0043195; C:terminal bouton; ISS:BHF-UCL.
DR GO; GO:0070335; F:aspartate binding; ISS:BHF-UCL.
DR GO; GO:0004070; F:aspartate carbamoyltransferase activity; ISS:BHF-UCL.
DR GO; GO:0005524; F:ATP binding; ISS:BHF-UCL.
DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; ISS:BHF-UCL.
DR GO; GO:0004151; F:dihydroorotase activity; ISS:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; ISS:BHF-UCL.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; ISS:BHF-UCL.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; ISS:BHF-UCL.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0070409; P:carbamoyl phosphate biosynthetic process; IEA:InterPro.
DR GO; GO:0035690; P:cellular response to drug; IEA:Compara.
DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IEA:Compara.
DR GO; GO:0017144; P:drug metabolic process; ISS:BHF-UCL.
DR GO; GO:0009790; P:embryo development; IEA:Compara.
DR GO; GO:0007565; P:female pregnancy; IEA:Compara.
DR GO; GO:0006543; P:glutamine catabolic process; IEA:InterPro.
DR GO; GO:0006541; P:glutamine metabolic process; ISS:BHF-UCL.
DR GO; GO:0007595; P:lactation; IEA:Compara.
DR GO; GO:0031100; P:organ regeneration; IEA:Compara.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; ISS:BHF-UCL.
DR GO; GO:0046777; P:protein autophosphorylation; ISS:BHF-UCL.
DR GO; GO:0046134; P:pyrimidine nucleoside biosynthetic process; TAS:Reactome.
DR GO; GO:0014075; P:response to amine stimulus; IEA:Compara.
DR GO; GO:0031000; P:response to caffeine; IEA:Compara.
DR GO; GO:0051414; P:response to cortisol stimulus; IEA:Compara.
DR GO; GO:0033574; P:response to testosterone stimulus; IEA:Compara.
DR GO; GO:0006228; P:UTP biosynthetic process; IEA:Compara.
DR Gene3D; 1.10.1030.10; -; 1.
DR Gene3D; 3.30.1490.20; -; 1.
DR Gene3D; 3.30.470.20; -; 2.
DR Gene3D; 3.40.50.1380; -; 1.
DR Gene3D; 3.40.50.20; -; 2.
DR Gene3D; 3.50.30.20; -; 1.
DR InterPro; IPR006132; Asp/Orn_carbamoyltranf_P-bd.
DR InterPro; IPR006130; Asp/Orn_carbamoylTrfase.
DR InterPro; IPR002082; Asp_carbamoyltransf.
DR InterPro; IPR006131; Asp_carbamoyltransf_Asp/Orn-bd.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR013816; ATP_grasp_subdomain_2.
DR InterPro; IPR006275; CarbamoylP_synth_lsu.
DR InterPro; IPR005481; CarbamoylP_synth_lsu_N.
DR InterPro; IPR005480; CarbamoylP_synth_lsu_oligo.
DR InterPro; IPR006274; CarbamoylP_synth_ssu.
DR InterPro; IPR002474; CarbamoylP_synth_ssu_N.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR005483; CbamoylP_synth_lsu_CPSase_dom.
DR InterPro; IPR002195; Dihydroorotase_CS.
DR InterPro; IPR017926; GATASE_1.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR011607; MGS-like_dom.
DR InterPro; IPR016185; PreATP-grasp_dom.
DR Pfam; PF00289; CPSase_L_chain; 2.
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 Pfam; PF00185; OTCace; 1.
DR Pfam; PF02729; OTCace_N; 1.
DR PRINTS; PR00100; AOTCASE.
DR PRINTS; PR00101; ATCASE.
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; SSF53671; Asp/Orn_carbamoyltranf; 1.
DR SUPFAM; SSF48108; CarbamoylP_synth_lsu_oligo; 1.
DR SUPFAM; SSF52021; CP_synthsmall; 1.
DR SUPFAM; SSF51338; Metalo_hydrolase; 1.
DR SUPFAM; SSF52335; MGS-like_dom; 1.
DR SUPFAM; SSF52440; PreATP-grasp-like; 2.
DR TIGRFAMs; TIGR00670; asp_carb_tr; 1.
DR TIGRFAMs; TIGR01369; CPSaseII_lrg; 1.
DR TIGRFAMs; TIGR01368; CPSaseIIsmall; 1.
DR PROSITE; PS50975; ATP_GRASP; 2.
DR PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1.
DR PROSITE; PS00866; CPSASE_1; 2.
DR PROSITE; PS00867; CPSASE_2; 2.
DR PROSITE; PS00482; DIHYDROOROTASE_1; 1.
DR PROSITE; PS00483; DIHYDROOROTASE_2; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Allosteric enzyme; ATP-binding; Complete proteome;
KW Cytoplasm; Direct protein sequencing; Hydrolase; Ligase;
KW Metal-binding; Multifunctional enzyme; Nucleotide-binding;
KW Phosphoprotein; Polymorphism; Pyrimidine biosynthesis;
KW Reference proteome; Repeat; Transferase; Zinc.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 2225 CAD protein.
FT /FTId=PRO_0000199506.
FT DOMAIN 177 363 Glutamine amidotransferase type-1.
FT DOMAIN 519 711 ATP-grasp 1.
FT DOMAIN 1052 1243 ATP-grasp 2.
FT REGION 2 365 GATase (Glutamine amidotransferase).
FT REGION 366 394 Linker.
FT REGION 395 1455 CPSase (Carbamoyl-phosphate synthase).
FT REGION 395 933 CPSase A.
FT REGION 934 1455 CPSase B.
FT REGION 1456 1788 DHOase (dihydroorotase).
FT REGION 1789 1917 Linker.
FT REGION 1918 2225 ATCase (Aspartate transcarbamylase).
FT ACT_SITE 252 252 For GATase activity (By similarity).
FT ACT_SITE 336 336 For GATase activity (By similarity).
FT ACT_SITE 338 338 For GATase activity (By similarity).
FT METAL 1471 1471 Zinc (Potential).
FT METAL 1473 1473 Zinc (Potential).
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 747 747 N6-acetyllysine.
FT MOD_RES 1406 1406 Phosphoserine.
FT MOD_RES 1411 1411 N6-acetyllysine.
FT MOD_RES 1859 1859 Phosphoserine.
FT MOD_RES 1884 1884 Phosphothreonine.
FT MOD_RES 1900 1900 Phosphoserine.
FT MOD_RES 1906 1906 Phosphothreonine.
FT VARIANT 177 177 R -> Q (in a colorectal cancer sample;
FT somatic mutation).
FT /FTId=VAR_035897.
FT VARIANT 735 735 Y -> C (in a colorectal cancer sample;
FT somatic mutation).
FT /FTId=VAR_035898.
FT CONFLICT 505 505 P -> T (in Ref. 1; BAA11423).
FT CONFLICT 535 535 A -> G (in Ref. 1; BAA11423).
FT CONFLICT 560 560 L -> V (in Ref. 1; BAA11423).
FT CONFLICT 1103 1103 T -> A (in Ref. 1; BAA11423).
FT CONFLICT 1513 1513 A -> G (in Ref. 1; BAA11423).
FT CONFLICT 1676 1676 N -> D (in Ref. 1; BAA11423).
SQ SEQUENCE 2225 AA; 242984 MW; 2AB8E8413E825A8F CRC64;
MAALVLEDGS VLRGQPFGAA VSTAGEVVFQ TGMVGYPEAL TDPSYKAQIL VLTYPLIGNY
GIPPDEMDEF GLCKWFESSG IHVAALVVGE CCPTPSHWSA TRTLHEWLQQ HGIPGLQGVD
TRELTKKLRE QGSLLGKLVQ NGTEPSSLPF LDPNARPLVP EVSIKTPRVF NTGGAPRILA
LDCGLKYNQI RCLCQRGAEV TVVPWDHALD SQEYEGLFLS NGPGDPASYP SVVSTLSRVL
SEPNPRPVFG ICLGHQLLAL AIGAKTYKMR YGNRGHNQPC LLVGSGRCFL TSQNHGFAVE
TDSLPADWAP LFTNANDGSN EGIVHNSLPF FSVQFHPEHQ AGPSDMELLF DIFLETVKEA
TAGNPGGQTV RERLTERLCP PGIPTPGSGL PPPRKVLILG SGGLSIGQAG EFDYSGSQAI
KALKEENIQT LLINPNIATV QTSQGLADKV YFLPITPHYV TQVIRNERPD GVLLTFGGQT
ALNCGVELTK AGVLARYGVR VLGTPVETIE LTEDRRAFAA RMAEIGEHVA PSEAANSLEQ
AQAAAERLGY PVLVRAAFAL GGLGSGFASN REELSALVAP AFAHTSQVLV DKSLKGWKEI
EYEVVRDAYG NCVTVCNMEN LDPLGIHTGE SIVVAPSQTL NDREYQLLRQ TAIKVTQHLG
IVGECNVQYA LNPESEQYYI IEVNARLSRS SALASKATGY PLAYVAAKLA LGIPLPELRN
SVTGGTAAFE PSVDYCVVKI PRWDLSKFLR VSTKIGSCMK SVGEVMGIGR SFEEAFQKAL
RMVDENCVGF DHTVKPVSDM ELETPTDKRI FVVAAALWAG YSVDRLYELT RIDRWFLHRM
KRIIAHAQLL EQHRGQPLPP DLLQQAKCLG FSDKQIALAV LSTELAVRKL RQELGICPAV
KQIDTVAAEW PAQTNYLYLT YWGTTHDLTF RTPHVLVLGS GVYRIGSSVE FDWCAVGCIQ
QLRKMGYKTI MVNYNPETVS TDYDMCDRLY FDEISFEVVM DIYELENPEG VILSMGGQLP
NNMAMALHRQ QCRVLGTSPE AIDSAENRFK FSRLLDTIGI SQPQWRELSD LESARQFCQT
VGYPCVVRPS YVLSGAAMNV AYTDGDLERF LSSAAAVSKE HPVVISKFIQ EAKEIDVDAV
ASDGVVAAIA ISEHVENAGV HSGDATLVTP PQDITAKTLE RIKAIVHAVG QELQVTGPFN
LQLIAKDDQL KVIECNVRVS RSFPFVSKTL GVDLVALATR VIMGEEVEPV GLMTGSGVVG
VKVPQFSFSR LAGADVVLGV EMTSTGEVAG FGESRCEAYL KAMLSTGFKI PKKNILLTIG
SYKNKSELLP TVRLLESLGY SLYASLGTAD FYTEHGVKVT AVDWHFEEAV DGECPPQRSI
LEQLAEKNFE LVINLSMRGA GGRRLSSFVT KGYRTRRLAA DFSVPLIIDI KCTKLFVEAL
GQIGPAPPLK VHVDCMTSQK LVRLPGLIDV HVHLREPGGT HKEDFASGTA AALAGGITMV
CAMPNTRPPI IDAPALALAQ KLAEAGARCD FALFLGASSE NAGTLGTVAG SAAGLKLYLN
ETFSELRLDS VVQWMEHFET WPSHLPIVAH AEQQTVAAVL MVAQLTQRSV HICHVARKEE
ILLIKAAKAR GLPVTCEVAP HHLFLSHDDL ERLGPGKGEV RPELGSRQDV EALWENMAVI
DCFASDHAPH TLEEKCGSRP PPGFPGLETM LPLLLTAVSE GRLSLDDLLQ RLHHNPRRIF
HLPPQEDTYV EVDLEHEWTI PSHMPFSKAH WTPFEGQKVK GTVRRVVLRG EVAYIDGQVL
VPPGYGQDVR KWPQGAVPQL PPSAPATSEM TTTPERPRRG IPGLPDGRFH LPPRIHRASD
PGLPAEEPKE KSSRKVAEPE LMGTPDGTCY PPPPVPRQAS PQNLGTPGLL HPQTSPLLHS
LVGQHILSVQ QFTKDQMSHL FNVAHTLRMM VQKERSLDIL KGKVMASMFY EVSTRTSSSF
AAAMARLGGA VLSFSEATSS VQKGESLADS VQTMSCYADV VVLRHPQPGA VELAAKHCRR
PVINAGDGVG EHPTQALLDI FTIREELGTV NGMTITMVGD LKHGRTVHSL ACLLTQYRVS
LRYVAPPSLR MPPTVRAFVA SRGTKQEEFE SIEEALPDTD VLYMTRIQKE RFGSTQEYEA
CFGQFILTPH IMTRAKKKMV VMHPMPRVNE ISVEVDSDPR AAYFRQAENG MYIRMALLAT
VLGRF
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