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Database: UniProt
Entry: PYC_HUMAN
LinkDB: PYC_HUMAN
Original site: PYC_HUMAN 
ID   PYC_HUMAN               Reviewed;        1178 AA.
AC   P11498; B4DN00; Q16705;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   24-JAN-2024, entry version 241.
DE   RecName: Full=Pyruvate carboxylase, mitochondrial {ECO:0000305};
DE            EC=6.4.1.1 {ECO:0000269|PubMed:9585002};
DE   AltName: Full=Pyruvic carboxylase;
DE            Short=PCB;
DE   Flags: Precursor;
GN   Name=PC {ECO:0000312|HGNC:HGNC:8636};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND BIOTINYLATION AT LYS-1144.
RC   TISSUE=Kidney, and Liver;
RX   PubMed=7918683; DOI=10.1016/0925-4439(94)90105-8;
RA   Wexler I.D., Du Y., Lisgaris M.V., Mandal S.K., Freytag S.O., Yang B.-S.,
RA   Liu T.-C., Kwon M., Patel M.S., Kerr D.S.;
RT   "Primary amino acid sequence and structure of human pyruvate carboxylase.";
RL   Biochim. Biophys. Acta 1227:46-52(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Kidney;
RX   PubMed=8048912; DOI=10.1006/bbrc.1994.2029;
RA   Mackay N., Rigat B., Douglas C., Chen H.S., Robinson B.H.;
RT   "cDNA cloning of human kidney pyruvate carboxylase.";
RL   Biochem. Biophys. Res. Commun. 202:1009-1014(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Kidney, and Liver;
RA   Walker M.E., Jitrapakdee S., Val D.L., Wallace J.C.;
RL   Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Lung;
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., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., 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., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16554811; DOI=10.1038/nature04632;
RA   Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA   Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA   Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA   Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA   Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA   Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT   "Human chromosome 11 DNA sequence and analysis including novel gene
RT   identification.";
RL   Nature 440:497-500(2006).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Lung;
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 project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1083-1178 (ISOFORM 1).
RX   PubMed=3555348; DOI=10.1016/0003-9861(87)90146-9;
RA   Lamhonwah A.-M., Quan F., Gravel R.A.;
RT   "Sequence homology around the biotin-binding site of human propionyl-CoA
RT   carboxylase and pyruvate carboxylase.";
RL   Arch. Biochem. Biophys. 254:631-636(1987).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1135-1178 (ISOFORM 1), AND BIOTINYLATION AT
RP   LYS-1144.
RX   PubMed=6548474; DOI=10.1016/s0021-9258(18)90822-7;
RA   Freytag S.O., Collier K.J.;
RT   "Molecular cloning of a cDNA for human pyruvate carboxylase. Structural
RT   relationship to other biotin-containing carboxylases and regulation of mRNA
RT   content in differentiating preadipocytes.";
RL   J. Biol. Chem. 259:12831-12837(1984).
RN   [9]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1090, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   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   [10]
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., Buerckstuemmer T.,
RA   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   [11]
RP   INTERACTION WITH SIRT4.
RX   PubMed=23438705; DOI=10.1016/j.mito.2013.02.002;
RA   Wirth M., Karaca S., Wenzel D., Ho L., Tishkoff D., Lombard D.B.,
RA   Verdin E., Urlaub H., Jedrusik-Bode M., Fischle W.;
RT   "Mitochondrial SIRT4-type proteins in Caenorhabditis elegans and mammals
RT   interact with pyruvate carboxylase and other acetylated biotin-dependent
RT   carboxylases.";
RL   Mitochondrion 13:705-720(2013).
RN   [12]
RP   IDENTIFICATION BY MASS 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., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [13]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 481-1178 IN COMPLEX WITH PYRUVATE;
RP   MANGANESE AND BIOTIN ANALOG, CARBOXYLATION AT LYS-741, MUTAGENESIS OF
RP   PHE-1077, AND SUBUNIT.
RX   PubMed=18297087; DOI=10.1038/nsmb.1393;
RA   Xiang S., Tong L.;
RT   "Crystal structures of human and Staphylococcus aureus pyruvate carboxylase
RT   and molecular insights into the carboxyltransfer reaction.";
RL   Nat. Struct. Mol. Biol. 15:295-302(2008).
RN   [15]
RP   VARIANTS PC DEFICIENCY THR-610 AND ILE-743.
RX   PubMed=9585612; DOI=10.1086/301884;
RA   Carbone M.A., MacKay N., Ling M., Cole D.E.C., Douglas C., Rigat B.,
RA   Feigenbaum A., Clarke J.T.R., Haworth J.C., Greenberg C.R., Seargeant L.,
RA   Robinson B.H.;
RT   "Amerindian pyruvate carboxylase deficiency is associated with two distinct
RT   missense mutations.";
RL   Am. J. Hum. Genet. 62:1312-1319(1998).
RN   [16]
RP   VARIANTS PC DEFICIENCY ALA-145 AND CYS-451, FUNCTION, CATALYTIC ACTIVITY,
RP   SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANTS PC DEFICIENCY ALA-145
RP   AND CYS-451, AND COFACTOR.
RX   PubMed=9585002; DOI=10.1203/00006450-199805000-00004;
RA   Wexler I.D., Kerr D.S., Du Y., Kaung M.M., Stephenson W., Lusk M.M.,
RA   Wappner R.S., Higgins J.J.;
RT   "Molecular characterization of pyruvate carboxylase deficiency in two
RT   consanguineous families.";
RL   Pediatr. Res. 43:579-584(1998).
RN   [17]
RP   VARIANTS PC DEFICIENCY ALA-145; GLN-156; TRP-270; CYS-304; CYS-451;
RP   LEU-583; THR-610; GLN-631; ILE-743 AND 1131-VAL--LYS-1133 DEL.
RX   PubMed=19306334; DOI=10.1002/humu.20908;
RA   Monnot S., Serre V., Chadefaux-Vekemans B., Aupetit J., Romano S.,
RA   De Lonlay P., Rival J.-M., Munnich A., Steffann J., Bonnefont J.-P.;
RT   "Structural insights on pathogenic effects of novel mutations causing
RT   pyruvate carboxylase deficiency.";
RL   Hum. Mutat. 30:734-740(2009).
CC   -!- FUNCTION: Pyruvate carboxylase catalyzes a 2-step reaction, involving
CC       the ATP-dependent carboxylation of the covalently attached biotin in
CC       the first step and the transfer of the carboxyl group to pyruvate in
CC       the second. Catalyzes in a tissue specific manner, the initial
CC       reactions of glucose (liver, kidney) and lipid (adipose tissue, liver,
CC       brain) synthesis from pyruvate. {ECO:0000269|PubMed:9585002}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + hydrogencarbonate + pyruvate = ADP + H(+) + oxaloacetate
CC         + phosphate; Xref=Rhea:RHEA:20844, ChEBI:CHEBI:15361,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16452, ChEBI:CHEBI:17544,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=6.4.1.1;
CC         Evidence={ECO:0000269|PubMed:9585002};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20845;
CC         Evidence={ECO:0000269|PubMed:9585002};
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000269|PubMed:18297087};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC       Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000269|PubMed:18297087};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC       {ECO:0000305|PubMed:9585002}.
CC   -!- SUBUNIT: Homotetramer (PubMed:18297087). Interacts (via the biotin
CC       carboxylation domain) with SIRT4 (PubMed:23438705).
CC       {ECO:0000269|PubMed:18297087, ECO:0000269|PubMed:23438705}.
CC   -!- INTERACTION:
CC       P11498; P48163: ME1; NbExp=14; IntAct=EBI-2211322, EBI-11958484;
CC       P11498; P11498: PC; NbExp=4; IntAct=EBI-2211322, EBI-2211322;
CC       P11498; PRO_0000278740 [Q03463]; Xeno; NbExp=7; IntAct=EBI-2211322, EBI-8803426;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000269|PubMed:9585002}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P11498-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P11498-2; Sequence=VSP_056358, VSP_056359;
CC   -!- PTM: Acetylation of Lys-748 might play a role in catalytic activity
CC       regulation. {ECO:0000250|UniProtKB:Q05920}.
CC   -!- DISEASE: Pyruvate carboxylase deficiency (PC deficiency) [MIM:266150]:
CC       Leads to lactic acidosis, intellectual disability and death. It occurs
CC       in three forms: mild or type A, severe neonatal or type B, and a very
CC       mild lacticacidemia. {ECO:0000269|PubMed:19306334,
CC       ECO:0000269|PubMed:9585002, ECO:0000269|PubMed:9585612}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=Pyruvate carboxylase entry;
CC       URL="https://en.wikipedia.org/wiki/Pyruvate_carboxylase";
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DR   EMBL; U04641; AAA99537.1; -; mRNA.
DR   EMBL; S72370; AAB31500.1; -; mRNA.
DR   EMBL; U30891; AAA82937.1; -; mRNA.
DR   EMBL; AK297705; BAG60062.1; -; mRNA.
DR   EMBL; AP000485; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AP003176; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC011617; AAH11617.1; -; mRNA.
DR   EMBL; M26122; AAA36423.1; -; mRNA.
DR   EMBL; K02282; AAA60033.1; -; mRNA.
DR   CCDS; CCDS8152.1; -. [P11498-1]
DR   PIR; G01933; JC2460.
DR   RefSeq; NP_000911.2; NM_000920.3. [P11498-1]
DR   RefSeq; NP_001035806.1; NM_001040716.1. [P11498-1]
DR   RefSeq; NP_071504.2; NM_022172.2. [P11498-1]
DR   RefSeq; XP_005274088.1; XM_005274031.4. [P11498-1]
DR   RefSeq; XP_005274089.1; XM_005274032.4. [P11498-1]
DR   RefSeq; XP_006718641.1; XM_006718578.3. [P11498-1]
DR   RefSeq; XP_011543388.1; XM_011545086.2. [P11498-1]
DR   RefSeq; XP_016873357.1; XM_017017868.1. [P11498-1]
DR   RefSeq; XP_016873358.1; XM_017017869.1. [P11498-1]
DR   RefSeq; XP_016873359.1; XM_017017870.1. [P11498-1]
DR   RefSeq; XP_016873360.1; XM_017017871.1. [P11498-1]
DR   RefSeq; XP_016873361.1; XM_017017872.1. [P11498-1]
DR   PDB; 3BG3; X-ray; 2.80 A; A/B/C/D=482-1178.
DR   PDB; 3BG9; X-ray; 3.00 A; A/B/C/D=482-1178.
DR   PDB; 7WTA; EM; 3.90 A; A/B/C/D=1-1178.
DR   PDB; 7WTB; EM; 3.70 A; A/B/C/D=1-1178.
DR   PDB; 7WTC; EM; 4.00 A; A/B/C/D=1-1178.
DR   PDB; 7WTD; EM; 3.90 A; A/B/C/D=1-1178.
DR   PDB; 7WTE; EM; 3.30 A; A/B/C/D=1-1178.
DR   PDBsum; 3BG3; -.
DR   PDBsum; 3BG9; -.
DR   PDBsum; 7WTA; -.
DR   PDBsum; 7WTB; -.
DR   PDBsum; 7WTC; -.
DR   PDBsum; 7WTD; -.
DR   PDBsum; 7WTE; -.
DR   AlphaFoldDB; P11498; -.
DR   EMDB; EMD-32773; -.
DR   EMDB; EMD-32774; -.
DR   EMDB; EMD-32775; -.
DR   EMDB; EMD-32776; -.
DR   EMDB; EMD-32777; -.
DR   EMDB; EMD-32778; -.
DR   EMDB; EMD-32779; -.
DR   EMDB; EMD-32780; -.
DR   EMDB; EMD-32781; -.
DR   EMDB; EMD-32782; -.
DR   SMR; P11498; -.
DR   BioGRID; 111124; 190.
DR   ComplexPortal; CPX-7142; Hydride transfer complex.
DR   DIP; DIP-46372N; -.
DR   IntAct; P11498; 47.
DR   MINT; P11498; -.
DR   STRING; 9606.ENSP00000498994; -.
DR   DrugBank; DB07497; 5-(hexahydro-2-oxo-1H-thieno[3,4-D]imidazol-6-yl)pentanal.
DR   DrugBank; DB00121; Biotin.
DR   DrugBank; DB00119; Pyruvic acid.
DR   GlyGen; P11498; 2 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; P11498; -.
DR   PhosphoSitePlus; P11498; -.
DR   SwissPalm; P11498; -.
DR   BioMuta; PC; -.
DR   DMDM; 1709947; -.
DR   EPD; P11498; -.
DR   jPOST; P11498; -.
DR   MassIVE; P11498; -.
DR   MaxQB; P11498; -.
DR   PaxDb; 9606-ENSP00000377532; -.
DR   PeptideAtlas; P11498; -.
DR   ProteomicsDB; 4659; -.
DR   ProteomicsDB; 52785; -. [P11498-1]
DR   Pumba; P11498; -.
DR   Antibodypedia; 30264; 409 antibodies from 37 providers.
DR   DNASU; 5091; -.
DR   Ensembl; ENST00000393955.6; ENSP00000377527.2; ENSG00000173599.15. [P11498-1]
DR   Ensembl; ENST00000393958.7; ENSP00000377530.2; ENSG00000173599.15. [P11498-1]
DR   Ensembl; ENST00000393960.7; ENSP00000377532.1; ENSG00000173599.15. [P11498-1]
DR   Ensembl; ENST00000524491.6; ENSP00000434192.2; ENSG00000173599.15. [P11498-2]
DR   Ensembl; ENST00000529047.6; ENSP00000435905.2; ENSG00000173599.15. [P11498-1]
DR   Ensembl; ENST00000651036.1; ENSP00000498406.1; ENSG00000173599.15. [P11498-1]
DR   Ensembl; ENST00000651854.1; ENSP00000498994.1; ENSG00000173599.15. [P11498-1]
DR   Ensembl; ENST00000652125.1; ENSP00000498302.1; ENSG00000173599.15. [P11498-1]
DR   GeneID; 5091; -.
DR   KEGG; hsa:5091; -.
DR   MANE-Select; ENST00000393960.7; ENSP00000377532.1; NM_001040716.2; NP_001035806.1.
DR   UCSC; uc001ojn.2; human. [P11498-1]
DR   AGR; HGNC:8636; -.
DR   CTD; 5091; -.
DR   DisGeNET; 5091; -.
DR   GeneCards; PC; -.
DR   GeneReviews; PC; -.
DR   HGNC; HGNC:8636; PC.
DR   HPA; ENSG00000173599; Tissue enhanced (adipose tissue, liver).
DR   MalaCards; PC; -.
DR   MIM; 266150; phenotype.
DR   MIM; 608786; gene.
DR   neXtProt; NX_P11498; -.
DR   OpenTargets; ENSG00000173599; -.
DR   Orphanet; 353320; Pyruvate carboxylase deficiency, benign type.
DR   Orphanet; 353308; Pyruvate carboxylase deficiency, infantile type.
DR   Orphanet; 353314; Pyruvate carboxylase deficiency, severe neonatal type.
DR   PharmGKB; PA32975; -.
DR   VEuPathDB; HostDB:ENSG00000173599; -.
DR   eggNOG; KOG0369; Eukaryota.
DR   GeneTree; ENSGT00900000141164; -.
DR   HOGENOM; CLU_000395_0_1_1; -.
DR   InParanoid; P11498; -.
DR   OMA; KGDAWSI; -.
DR   OrthoDB; 1129179at2759; -.
DR   PhylomeDB; P11498; -.
DR   TreeFam; TF300535; -.
DR   BioCyc; MetaCyc:HS10697-MONOMER; -.
DR   BRENDA; 6.4.1.1; 2681.
DR   PathwayCommons; P11498; -.
DR   Reactome; R-HSA-196780; Biotin transport and metabolism.
DR   Reactome; R-HSA-3371599; Defective HLCS causes multiple carboxylase deficiency.
DR   Reactome; R-HSA-70263; Gluconeogenesis.
DR   SABIO-RK; P11498; -.
DR   SignaLink; P11498; -.
DR   SIGNOR; P11498; -.
DR   UniPathway; UPA00138; -.
DR   BioGRID-ORCS; 5091; 264 hits in 1160 CRISPR screens.
DR   ChiTaRS; PC; human.
DR   EvolutionaryTrace; P11498; -.
DR   GenomeRNAi; 5091; -.
DR   Pharos; P11498; Tbio.
DR   PRO; PR:P11498; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; P11498; Protein.
DR   Bgee; ENSG00000173599; Expressed in right lobe of liver and 132 other cell types or tissues.
DR   ExpressionAtlas; P11498; baseline and differential.
DR   Genevisible; P11498; HS.
DR   GO; GO:0005737; C:cytoplasm; IDA:AgBase.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR   GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR   GO; GO:0005524; F:ATP binding; TAS:ProtInc.
DR   GO; GO:0009374; F:biotin binding; TAS:ProtInc.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004736; F:pyruvate carboxylase activity; IMP:UniProtKB.
DR   GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006734; P:NADH metabolic process; IDA:ComplexPortal.
DR   GO; GO:0006739; P:NADP metabolic process; IDA:ComplexPortal.
DR   GO; GO:0010629; P:negative regulation of gene expression; IMP:AgBase.
DR   GO; GO:0044794; P:positive regulation by host of viral process; IMP:AgBase.
DR   GO; GO:0006090; P:pyruvate metabolic process; IBA:GO_Central.
DR   GO; GO:0019076; P:viral release from host cell; IMP:AgBase.
DR   GO; GO:0019074; P:viral RNA genome packaging; IMP:AgBase.
DR   CDD; cd06850; biotinyl_domain; 1.
DR   CDD; cd07937; DRE_TIM_PC_TC_5S; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   Gene3D; 3.10.600.10; pyruvate carboxylase f1077a mutant domain; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR005481; BC-like_N.
DR   InterPro; IPR001882; Biotin_BS.
DR   InterPro; IPR011764; Biotin_carboxylation_dom.
DR   InterPro; IPR005482; Biotin_COase_C.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR003379; Carboxylase_cons_dom.
DR   InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR000891; PYR_CT.
DR   InterPro; IPR005930; Pyruv_COase.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   NCBIfam; TIGR01235; pyruv_carbox; 1.
DR   PANTHER; PTHR43778; PYRUVATE CARBOXYLASE; 1.
DR   PANTHER; PTHR43778:SF2; PYRUVATE CARBOXYLASE, MITOCHONDRIAL; 1.
DR   Pfam; PF02785; Biotin_carb_C; 1.
DR   Pfam; PF00289; Biotin_carb_N; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF02786; CPSase_L_D2; 1.
DR   Pfam; PF00682; HMGL-like; 1.
DR   Pfam; PF02436; PYC_OADA; 1.
DR   PIRSF; PIRSF001594; Pyruv_carbox; 1.
DR   SMART; SM00878; Biotin_carb_C; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF89000; post-HMGL domain-like; 1.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR   SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR   SUPFAM; SSF51230; Single hybrid motif; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS50979; BC; 1.
DR   PROSITE; PS00188; BIOTIN; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS50991; PYR_CT; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; ATP-binding; Biotin;
KW   Disease variant; Gluconeogenesis; Ligase; Lipid biosynthesis;
KW   Lipid metabolism; Manganese; Metal-binding; Mitochondrion;
KW   Multifunctional enzyme; Nucleotide-binding; Phosphoprotein; Pyruvate;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..20
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..1178
FT                   /note="Pyruvate carboxylase, mitochondrial"
FT                   /id="PRO_0000002840"
FT   DOMAIN          36..486
FT                   /note="Biotin carboxylation"
FT   DOMAIN          156..353
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   DOMAIN          563..832
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
FT   DOMAIN          1109..1178
FT                   /note="Biotinyl-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT   ACT_SITE        328
FT                   /evidence="ECO:0000250"
FT   BINDING         152
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         236
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         271
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         571..575
FT                   /ligand="substrate"
FT   BINDING         572
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000269|PubMed:18297087"
FT   BINDING         644
FT                   /ligand="substrate"
FT   BINDING         741
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /note="via carbamate group"
FT                   /evidence="ECO:0000269|PubMed:18297087"
FT   BINDING         771
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000269|PubMed:18297087"
FT   BINDING         773
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000269|PubMed:18297087"
FT   BINDING         908
FT                   /ligand="substrate"
FT   MOD_RES         35
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q05920"
FT   MOD_RES         39
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q05920"
FT   MOD_RES         79
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q05920"
FT   MOD_RES         79
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q05920"
FT   MOD_RES         148
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q05920"
FT   MOD_RES         152
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q05920"
FT   MOD_RES         241
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q05920"
FT   MOD_RES         297
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q05920"
FT   MOD_RES         319
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q05920"
FT   MOD_RES         434
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q05920"
FT   MOD_RES         442
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q05920"
FT   MOD_RES         589
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q05920"
FT   MOD_RES         661
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q05920"
FT   MOD_RES         717
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q05920"
FT   MOD_RES         741
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000269|PubMed:18297087"
FT   MOD_RES         748
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q05920"
FT   MOD_RES         892
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q05920"
FT   MOD_RES         969
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q05920"
FT   MOD_RES         992
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q05920"
FT   MOD_RES         1003
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P52873"
FT   MOD_RES         1061
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q05920"
FT   MOD_RES         1090
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         1124
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q05920"
FT   MOD_RES         1144
FT                   /note="N6-biotinyllysine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01066,
FT                   ECO:0000269|PubMed:6548474, ECO:0000269|PubMed:7918683"
FT   VAR_SEQ         457..529
FT                   /note="TNIAFLQNVLNNQQFLAGTVDTQFIDENPELFQLRPAQNRAQKLLHYLGHVM
FT                   VNGPTTPIPVKASPSPTDPVV -> VRRHQAQPLAAALGRPCGQEARRPQAAVTAPTGP
FT                   GSPTLVRVPPAARVLSSRLGGPSQTTPETSTEVSPTILL (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_056358"
FT   VAR_SEQ         530..1178
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_056359"
FT   VARIANT         76
FT                   /note="H -> L (in dbSNP:rs7104156)"
FT                   /id="VAR_048416"
FT   VARIANT         145
FT                   /note="V -> A (in PC deficiency; mild; strongly reduced
FT                   pyruvate carboxylase activity; dbSNP:rs28940591)"
FT                   /evidence="ECO:0000269|PubMed:19306334,
FT                   ECO:0000269|PubMed:9585002"
FT                   /id="VAR_015199"
FT   VARIANT         156
FT                   /note="R -> Q (in PC deficiency; dbSNP:rs119103241)"
FT                   /evidence="ECO:0000269|PubMed:19306334"
FT                   /id="VAR_058957"
FT   VARIANT         270
FT                   /note="R -> W (in PC deficiency; dbSNP:rs1258494752)"
FT                   /evidence="ECO:0000269|PubMed:19306334"
FT                   /id="VAR_058958"
FT   VARIANT         304
FT                   /note="Y -> C (in PC deficiency)"
FT                   /evidence="ECO:0000269|PubMed:19306334"
FT                   /id="VAR_058959"
FT   VARIANT         451
FT                   /note="R -> C (in PC deficiency; mild; strongly reduced
FT                   pyruvate carboxylase activity; dbSNP:rs113994143)"
FT                   /evidence="ECO:0000269|PubMed:19306334,
FT                   ECO:0000269|PubMed:9585002"
FT                   /id="VAR_015200"
FT   VARIANT         583
FT                   /note="R -> L (in PC deficiency; dbSNP:rs119103242)"
FT                   /evidence="ECO:0000269|PubMed:19306334"
FT                   /id="VAR_058960"
FT   VARIANT         610
FT                   /note="A -> T (in PC deficiency; mild; dbSNP:rs28940589)"
FT                   /evidence="ECO:0000269|PubMed:19306334,
FT                   ECO:0000269|PubMed:9585612"
FT                   /id="VAR_008095"
FT   VARIANT         631
FT                   /note="R -> Q (in PC deficiency; dbSNP:rs113994145)"
FT                   /evidence="ECO:0000269|PubMed:19306334"
FT                   /id="VAR_058961"
FT   VARIANT         743
FT                   /note="M -> I (in PC deficiency; mild; dbSNP:rs28940590)"
FT                   /evidence="ECO:0000269|PubMed:19306334,
FT                   ECO:0000269|PubMed:9585612"
FT                   /id="VAR_008096"
FT   VARIANT         1131..1133
FT                   /note="Missing (in PC deficiency)"
FT                   /evidence="ECO:0000269|PubMed:19306334"
FT                   /id="VAR_058962"
FT   MUTAGEN         1077
FT                   /note="F->A,E: Loss of tetramerization and enzyme activity,
FT                   resulting in an inactive homodimer."
FT                   /evidence="ECO:0000269|PubMed:18297087"
FT   CONFLICT        225..226
FT                   /note="LA -> WP (in Ref. 2; AAB31500)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        352
FT                   /note="A -> S (in Ref. 3; AAA82937)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        385..386
FT                   /note="RS -> PT (in Ref. 2; AAB31500)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        486..487
FT                   /note="EL -> DV (in Ref. 2; AAB31500)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        638
FT                   /note="P -> R (in Ref. 2; AAB31500)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        729
FT                   /note="E -> A (in Ref. 2; AAB31500)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        774..775
FT                   /note="DT -> AP (in Ref. 2; AAB31500)"
FT                   /evidence="ECO:0000305"
FT   STRAND          39..42
FT                   /evidence="ECO:0007829|PDB:7WTE"
FT   HELIX           47..58
FT                   /evidence="ECO:0007829|PDB:7WTE"
FT   STRAND          62..67
FT                   /evidence="ECO:0007829|PDB:7WTE"
FT   STRAND          75..77
FT                   /evidence="ECO:0007829|PDB:7WTE"
FT   STRAND          80..85
FT                   /evidence="ECO:0007829|PDB:7WTE"
FT   TURN            92..94
FT                   /evidence="ECO:0007829|PDB:7WTE"
FT   HELIX           95..97
FT                   /evidence="ECO:0007829|PDB:7WTE"
FT   HELIX           99..108
FT                   /evidence="ECO:0007829|PDB:7WTE"
FT   STRAND          113..115
FT                   /evidence="ECO:0007829|PDB:7WTE"
FT   TURN            117..119
FT                   /evidence="ECO:0007829|PDB:7WTE"
FT   HELIX           125..133
FT                   /evidence="ECO:0007829|PDB:7WTE"
FT   STRAND          137..141
FT                   /evidence="ECO:0007829|PDB:7WTE"
FT   HELIX           143..148
FT                   /evidence="ECO:0007829|PDB:7WTE"
FT   STRAND          149..151
FT                   /evidence="ECO:0007829|PDB:7WTE"
FT   HELIX           152..161
FT                   /evidence="ECO:0007829|PDB:7WTE"
FT   HELIX           177..186
FT                   /evidence="ECO:0007829|PDB:7WTE"
FT   STRAND          191..200
FT                   /evidence="ECO:0007829|PDB:7WTE"
FT   HELIX           211..226
FT                   /evidence="ECO:0007829|PDB:7WTE"
FT   STRAND          233..237
FT                   /evidence="ECO:0007829|PDB:7WTE"
FT   STRAND          245..251
FT                   /evidence="ECO:0007829|PDB:7WTE"
FT   STRAND          257..279
FT                   /evidence="ECO:0007829|PDB:7WTE"
FT   HELIX           285..302
FT                   /evidence="ECO:0007829|PDB:7WTE"
FT   STRAND          306..311
FT                   /evidence="ECO:0007829|PDB:7WTE"
FT   HELIX           333..340
FT                   /evidence="ECO:0007829|PDB:7WTE"
FT   HELIX           344..353
FT                   /evidence="ECO:0007829|PDB:7WTE"
FT   HELIX           357..360
FT                   /evidence="ECO:0007829|PDB:7WTE"
FT   TURN            364..366
FT                   /evidence="ECO:0007829|PDB:7WTE"
FT   STRAND          371..379
FT                   /evidence="ECO:0007829|PDB:7WTE"
FT   TURN            383..386
FT                   /evidence="ECO:0007829|PDB:7WTE"
FT   STRAND          387..389
FT                   /evidence="ECO:0007829|PDB:7WTE"
FT   STRAND          396..398
FT                   /evidence="ECO:0007829|PDB:7WTE"
FT   STRAND          405..411
FT                   /evidence="ECO:0007829|PDB:7WTE"
FT   STRAND          420..422
FT                   /evidence="ECO:0007829|PDB:7WTE"
FT   STRAND          425..435
FT                   /evidence="ECO:0007829|PDB:7WTE"
FT   HELIX           436..449
FT                   /evidence="ECO:0007829|PDB:7WTE"
FT   STRAND          451..455
FT                   /evidence="ECO:0007829|PDB:7WTE"
FT   HELIX           459..467
FT                   /evidence="ECO:0007829|PDB:7WTE"
FT   HELIX           469..473
FT                   /evidence="ECO:0007829|PDB:7WTE"
FT   HELIX           478..480
FT                   /evidence="ECO:0007829|PDB:7WTE"
FT   TURN            481..483
FT                   /evidence="ECO:0007829|PDB:7WTE"
FT   TURN            485..489
FT                   /evidence="ECO:0007829|PDB:7WTE"
FT   HELIX           495..510
FT                   /evidence="ECO:0007829|PDB:3BG3"
FT   HELIX           541..559
FT                   /evidence="ECO:0007829|PDB:3BG3"
FT   STRAND          564..567
FT                   /evidence="ECO:0007829|PDB:3BG3"
FT   TURN            569..571
FT                   /evidence="ECO:0007829|PDB:3BG3"
FT   HELIX           572..577
FT                   /evidence="ECO:0007829|PDB:3BG3"
FT   HELIX           584..597
FT                   /evidence="ECO:0007829|PDB:3BG3"
FT   STRAND          602..608
FT                   /evidence="ECO:0007829|PDB:3BG3"
FT   HELIX           611..617
FT                   /evidence="ECO:0007829|PDB:3BG3"
FT   HELIX           623..633
FT                   /evidence="ECO:0007829|PDB:3BG3"
FT   STRAND          635..637
FT                   /evidence="ECO:0007829|PDB:3BG3"
FT   STRAND          639..643
FT                   /evidence="ECO:0007829|PDB:3BG3"
FT   HELIX           645..647
FT                   /evidence="ECO:0007829|PDB:3BG3"
FT   STRAND          650..652
FT                   /evidence="ECO:0007829|PDB:3BG3"
FT   HELIX           656..669
FT                   /evidence="ECO:0007829|PDB:3BG3"
FT   STRAND          673..677
FT                   /evidence="ECO:0007829|PDB:3BG3"
FT   HELIX           683..694
FT                   /evidence="ECO:0007829|PDB:3BG3"
FT   TURN            695..697
FT                   /evidence="ECO:0007829|PDB:3BG3"
FT   STRAND          698..705
FT                   /evidence="ECO:0007829|PDB:3BG3"
FT   HELIX           720..733
FT                   /evidence="ECO:0007829|PDB:3BG3"
FT   STRAND          736..741
FT                   /evidence="ECO:0007829|PDB:3BG3"
FT   HELIX           749..762
FT                   /evidence="ECO:0007829|PDB:3BG3"
FT   STRAND          768..771
FT                   /evidence="ECO:0007829|PDB:3BG3"
FT   HELIX           779..788
FT                   /evidence="ECO:0007829|PDB:3BG3"
FT   STRAND          792..797
FT                   /evidence="ECO:0007829|PDB:3BG3"
FT   HELIX           799..801
FT                   /evidence="ECO:0007829|PDB:3BG3"
FT   HELIX           810..817
FT                   /evidence="ECO:0007829|PDB:3BG3"
FT   HELIX           828..844
FT                   /evidence="ECO:0007829|PDB:3BG3"
FT   HELIX           845..848
FT                   /evidence="ECO:0007829|PDB:3BG3"
FT   HELIX           850..852
FT                   /evidence="ECO:0007829|PDB:3BG3"
FT   HELIX           861..864
FT                   /evidence="ECO:0007829|PDB:3BG3"
FT   HELIX           868..875
FT                   /evidence="ECO:0007829|PDB:3BG3"
FT   HELIX           876..878
FT                   /evidence="ECO:0007829|PDB:3BG3"
FT   TURN            879..881
FT                   /evidence="ECO:0007829|PDB:3BG3"
FT   HELIX           886..900
FT                   /evidence="ECO:0007829|PDB:3BG3"
FT   HELIX           910..923
FT                   /evidence="ECO:0007829|PDB:3BG3"
FT   HELIX           928..934
FT                   /evidence="ECO:0007829|PDB:3BG3"
FT   TURN            935..937
FT                   /evidence="ECO:0007829|PDB:3BG3"
FT   HELIX           942..947
FT                   /evidence="ECO:0007829|PDB:3BG3"
FT   TURN            948..950
FT                   /evidence="ECO:0007829|PDB:3BG3"
FT   HELIX           961..968
FT                   /evidence="ECO:0007829|PDB:3BG3"
FT   STRAND          969..971
FT                   /evidence="ECO:0007829|PDB:3BG3"
FT   HELIX           978..981
FT                   /evidence="ECO:0007829|PDB:3BG3"
FT   HELIX           989..997
FT                   /evidence="ECO:0007829|PDB:3BG3"
FT   HELIX           1004..1012
FT                   /evidence="ECO:0007829|PDB:3BG3"
FT   HELIX           1014..1026
FT                   /evidence="ECO:0007829|PDB:3BG3"
FT   STRAND          1031..1033
FT                   /evidence="ECO:0007829|PDB:7WTE"
FT   HELIX           1035..1040
FT                   /evidence="ECO:0007829|PDB:3BG3"
FT   STRAND          1047..1051
FT                   /evidence="ECO:0007829|PDB:3BG3"
FT   TURN            1053..1055
FT                   /evidence="ECO:0007829|PDB:3BG9"
FT   STRAND          1057..1068
FT                   /evidence="ECO:0007829|PDB:3BG3"
FT   STRAND          1072..1090
FT                   /evidence="ECO:0007829|PDB:3BG3"
FT   HELIX           1092..1094
FT                   /evidence="ECO:0007829|PDB:3BG3"
FT   STRAND          1108..1110
FT                   /evidence="ECO:0007829|PDB:3BG3"
FT   STRAND          1118..1123
FT                   /evidence="ECO:0007829|PDB:3BG3"
FT   STRAND          1138..1144
FT                   /evidence="ECO:0007829|PDB:3BG3"
FT   STRAND          1146..1149
FT                   /evidence="ECO:0007829|PDB:3BG3"
FT   STRAND          1164..1168
FT                   /evidence="ECO:0007829|PDB:3BG3"
FT   STRAND          1170..1172
FT                   /evidence="ECO:0007829|PDB:7WTE"
FT   STRAND          1173..1175
FT                   /evidence="ECO:0007829|PDB:3BG3"
SQ   SEQUENCE   1178 AA;  129634 MW;  381F527553A20095 CRC64;
     MLKFRTVHGG LRLLGIRRTS TAPAASPNVR RLEYKPIKKV MVANRGEIAI RVFRACTELG
     IRTVAIYSEQ DTGQMHRQKA DEAYLIGRGL APVQAYLHIP DIIKVAKENN VDAVHPGYGF
     LSERADFAQA CQDAGVRFIG PSPEVVRKMG DKVEARAIAI AAGVPVVPGT DAPITSLHEA
     HEFSNTYGFP IIFKAAYGGG GRGMRVVHSY EELEENYTRA YSEALAAFGN GALFVEKFIE
     KPRHIEVQIL GDQYGNILHL YERDCSIQRR HQKVVEIAPA AHLDPQLRTR LTSDSVKLAK
     QVGYENAGTV EFLVDRHGKH YFIEVNSRLQ VEHTVTEEIT DVDLVHAQIH VAEGRSLPDL
     GLRQENIRIN GCAIQCRVTT EDPARSFQPD TGRIEVFRSG EGMGIRLDNA SAFQGAVISP
     HYDSLLVKVI AHGKDHPTAA TKMSRALAEF RVRGVKTNIA FLQNVLNNQQ FLAGTVDTQF
     IDENPELFQL RPAQNRAQKL LHYLGHVMVN GPTTPIPVKA SPSPTDPVVP AVPIGPPPAG
     FRDILLREGP EGFARAVRNH PGLLLMDTTF RDAHQSLLAT RVRTHDLKKI APYVAHNFSK
     LFSMENWGGA TFDVAMRFLY ECPWRRLQEL RELIPNIPFQ MLLRGANAVG YTNYPDNVVF
     KFCEVAKENG MDVFRVFDSL NYLPNMLLGM EAAGSAGGVV EAAISYTGDV ADPSRTKYSL
     QYYMGLAEEL VRAGTHILCI KDMAGLLKPT ACTMLVSSLR DRFPDLPLHI HTHDTSGAGV
     AAMLACAQAG ADVVDVAADS MSGMTSQPSM GALVACTRGT PLDTEVPMER VFDYSEYWEG
     ARGLYAAFDC TATMKSGNSD VYENEIPGGQ YTNLHFQAHS MGLGSKFKEV KKAYVEANQM
     LGDLIKVTPS SKIVGDLAQF MVQNGLSRAE AEAQAEELSF PRSVVEFLQG YIGVPHGGFP
     EPFRSKVLKD LPRVEGRPGA SLPPLDLQAL EKELVDRHGE EVTPEDVLSA AMYPDVFAHF
     KDFTATFGPL DSLNTRLFLQ GPKIAEEFEV ELERGKTLHI KALAVSDLNR AGQRQVFFEL
     NGQLRSILVK DTQAMKEMHF HPKALKDVKG QIGAPMPGKV IDIKVVAGAK VAKGQPLCVL
     SAMKMETVVT SPMEGTVRKV HVTKDMTLEG DDLILEIE
//
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