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Database: UniProt
Entry: P11498
LinkDB: P11498
Original site: P11498 
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   29-OCT-2014, entry version 172.
DE   RecName: Full=Pyruvate carboxylase, mitochondrial;
DE            EC=6.4.1.1;
DE   AltName: Full=Pyruvic carboxylase;
DE            Short=PCB;
DE   Flags: Precursor;
GN   Name=PC;
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 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.,
RA   Yang B.-S., Liu T.-C., Kwon M., Patel M.S., Kerr D.S.;
RT   "Primary amino acid sequence and structure of human pyruvate
RT   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.,
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   [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.,
RA   Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA   FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA   Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA   Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA   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
RT   project: 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-
RT   CoA 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
RP   AT LYS-1144.
RX   PubMed=6548474;
RA   Freytag S.O., Collier K.J.;
RT   "Molecular cloning of a cDNA for human pyruvate carboxylase.
RT   Structural relationship to other biotin-containing carboxylases and
RT   regulation of mRNA 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
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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   [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.,
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   [11]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 481-1178 IN COMPLEX WITH
RP   PYRUVATE; MANGANESE AND BIOTIN ANALOG, CARBAMYLATION AT LYS-741,
RP   MUTAGENESIS OF 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
RT   carboxylase and molecular insights into the carboxyltransfer
RT   reaction.";
RL   Nat. Struct. Mol. Biol. 15:295-302(2008).
RN   [12]
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.,
RA   Seargeant L., Robinson B.H.;
RT   "Amerindian pyruvate carboxylase deficiency is associated with two
RT   distinct missense mutations.";
RL   Am. J. Hum. Genet. 62:1312-1319(1998).
RN   [13]
RP   VARIANTS PC DEFICIENCY ALA-145 AND CYS-451.
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   [14]
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,
CC       involving the ATP-dependent carboxylation of the covalently
CC       attached biotin in the first step and the transfer of the carboxyl
CC       group to pyruvate in the second. Catalyzes in a tissue specific
CC       manner, the initial reactions of glucose (liver, kidney) and lipid
CC       (adipose tissue, liver, brain) synthesis from pyruvate.
CC   -!- CATALYTIC ACTIVITY: ATP + pyruvate + HCO(3)(-) = ADP + phosphate +
CC       oxaloacetate.
CC   -!- COFACTOR: Biotin.
CC   -!- COFACTOR: Binds 1 manganese ion per subunit.
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:18297087}.
CC   -!- INTERACTION:
CC       Q03463:- (xeno); NbExp=7; IntAct=EBI-2211322, EBI-8803426;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
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         Note=No experimental confirmation available.;
CC   -!- DISEASE: Pyruvate carboxylase deficiency (PC deficiency)
CC       [MIM:266150]: Leads to lactic acidosis, mental retardation and
CC       death. It occurs in three forms: mild or type A, severe neonatal
CC       or type B, and a very mild lacticacidemia. Note=The disease is
CC       caused by mutations affecting the gene represented in this entry.
CC   -!- SIMILARITY: Contains 1 ATP-grasp domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00409}.
CC   -!- SIMILARITY: Contains 1 biotin carboxylation domain. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 biotinyl-binding domain. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 carboxyltransferase domain. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=Pyruvate carboxylase entry;
CC       URL="http://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.
DR   RefSeq; NP_001035806.1; NM_001040716.1.
DR   RefSeq; NP_071504.2; NM_022172.2.
DR   RefSeq; XP_005274088.1; XM_005274031.2.
DR   RefSeq; XP_005274089.1; XM_005274032.2.
DR   RefSeq; XP_006718640.1; XM_006718577.1.
DR   RefSeq; XP_006718641.1; XM_006718578.1.
DR   UniGene; Hs.89890; -.
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   PDBsum; 3BG3; -.
DR   PDBsum; 3BG9; -.
DR   ProteinModelPortal; P11498; -.
DR   SMR; P11498; 37-488, 494-1178.
DR   BioGrid; 111124; 28.
DR   DIP; DIP-46372N; -.
DR   IntAct; P11498; 4.
DR   MINT; MINT-3007737; -.
DR   STRING; 9606.ENSP00000377527; -.
DR   DrugBank; DB00121; Biotin.
DR   DrugBank; DB00119; Pyruvic acid.
DR   PhosphoSite; P11498; -.
DR   DMDM; 1709947; -.
DR   MaxQB; P11498; -.
DR   PaxDb; P11498; -.
DR   PeptideAtlas; P11498; -.
DR   PRIDE; P11498; -.
DR   Ensembl; ENST00000393955; ENSP00000377527; ENSG00000173599. [P11498-1]
DR   Ensembl; ENST00000393958; ENSP00000377530; ENSG00000173599. [P11498-1]
DR   Ensembl; ENST00000393960; ENSP00000377532; ENSG00000173599. [P11498-1]
DR   GeneID; 5091; -.
DR   KEGG; hsa:5091; -.
DR   UCSC; uc001ojn.1; human. [P11498-1]
DR   CTD; 5091; -.
DR   GeneCards; GC11M066615; -.
DR   GeneReviews; PC; -.
DR   HGNC; HGNC:8636; PC.
DR   HPA; CAB033742; -.
DR   HPA; HPA043922; -.
DR   MIM; 266150; phenotype.
DR   MIM; 608786; gene.
DR   neXtProt; NX_P11498; -.
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   eggNOG; COG1038; -.
DR   GeneTree; ENSGT00550000074986; -.
DR   HOGENOM; HOG000282801; -.
DR   HOVERGEN; HBG008340; -.
DR   InParanoid; P11498; -.
DR   KO; K01958; -.
DR   OMA; HSMENIT; -.
DR   OrthoDB; EOG7WT40F; -.
DR   PhylomeDB; P11498; -.
DR   TreeFam; TF300535; -.
DR   BioCyc; MetaCyc:HS10697-MONOMER; -.
DR   BRENDA; 6.4.1.1; 2681.
DR   Reactome; REACT_11153; Biotin transport and metabolism.
DR   Reactome; REACT_1520; Gluconeogenesis.
DR   Reactome; REACT_169312; Defective HLCS causes multiple carboxylase deficiency.
DR   SABIO-RK; P11498; -.
DR   UniPathway; UPA00138; -.
DR   ChiTaRS; PC; human.
DR   EvolutionaryTrace; P11498; -.
DR   GenomeRNAi; 5091; -.
DR   NextBio; 19632; -.
DR   PRO; PR:P11498; -.
DR   Bgee; P11498; -.
DR   CleanEx; HS_PC; -.
DR   ExpressionAtlas; P11498; baseline and differential.
DR   Genevestigator; P11498; -.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:Ensembl.
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:0004075; F:biotin carboxylase activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004736; F:pyruvate carboxylase activity; TAS:Reactome.
DR   GO; GO:0006768; P:biotin metabolic process; TAS:Reactome.
DR   GO; GO:0005975; P:carbohydrate metabolic process; TAS:Reactome.
DR   GO; GO:0006094; P:gluconeogenesis; TAS:Reactome.
DR   GO; GO:0006006; P:glucose metabolic process; TAS:Reactome.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006107; P:oxaloacetate metabolic process; IEA:Ensembl.
DR   GO; GO:0006090; P:pyruvate metabolic process; IEA:Ensembl.
DR   GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR   GO; GO:0006766; P:vitamin metabolic process; TAS:Reactome.
DR   GO; GO:0006767; P:water-soluble vitamin metabolic process; TAS:Reactome.
DR   Gene3D; 1.10.10.60; -; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   Gene3D; 3.30.470.20; -; 1.
DR   Gene3D; 3.40.50.20; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR013816; ATP_grasp_subdomain_2.
DR   InterPro; IPR001882; Biotin_BS.
DR   InterPro; IPR011764; Biotin_carboxylation_dom.
DR   InterPro; IPR005482; Biotin_COase_C.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR005481; CarbamoylP_synth_lsu_N.
DR   InterPro; IPR003379; Carboxylase_cons_dom.
DR   InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR009057; Homeodomain-like.
DR   InterPro; IPR016185; PreATP-grasp_dom.
DR   InterPro; IPR000891; PYR_CT.
DR   InterPro; IPR005930; Pyruv_COase.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   Pfam; PF02785; Biotin_carb_C; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF00289; CPSase_L_chain; 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; SSF51230; SSF51230; 1.
DR   SUPFAM; SSF51246; SSF51246; 1.
DR   SUPFAM; SSF52440; SSF52440; 1.
DR   TIGRFAMs; TIGR01235; pyruv_carbox; 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   Complete proteome; Disease mutation; Gluconeogenesis; Ligase;
KW   Lipid biosynthesis; Lipid metabolism; Manganese; Metal-binding;
KW   Mitochondrion; Multifunctional enzyme; Nucleotide-binding;
KW   Polymorphism; Pyruvate; Reference proteome; Transit peptide.
FT   TRANSIT       1     20       Mitochondrion. {ECO:0000255}.
FT   CHAIN        21   1178       Pyruvate carboxylase, mitochondrial.
FT                                /FTId=PRO_0000002840.
FT   DOMAIN       36    486       Biotin carboxylation.
FT   DOMAIN      156    353       ATP-grasp. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   DOMAIN      563    832       Carboxyltransferase.
FT   DOMAIN     1110   1177       Biotinyl-binding.
FT   REGION      571    575       Substrate binding.
FT   ACT_SITE    328    328       {ECO:0000250}.
FT   METAL       572    572       Manganese. {ECO:0000269|PubMed:18297087}.
FT   METAL       741    741       Manganese; via carbamate group.
FT                                {ECO:0000269|PubMed:18297087}.
FT   METAL       771    771       Manganese; via tele nitrogen.
FT                                {ECO:0000269|PubMed:18297087}.
FT   METAL       773    773       Manganese; via tele nitrogen.
FT                                {ECO:0000269|PubMed:18297087}.
FT   BINDING     152    152       ATP. {ECO:0000250}.
FT   BINDING     236    236       ATP. {ECO:0000250}.
FT   BINDING     271    271       ATP. {ECO:0000250}.
FT   BINDING     644    644       Substrate.
FT   BINDING     908    908       Substrate.
FT   MOD_RES      79     79       N6-acetyllysine; alternate.
FT                                {ECO:0000250}.
FT   MOD_RES      79     79       N6-succinyllysine; alternate.
FT                                {ECO:0000250}.
FT   MOD_RES     297    297       N6-acetyllysine. {ECO:0000250}.
FT   MOD_RES     319    319       N6-acetyllysine. {ECO:0000250}.
FT   MOD_RES     434    434       N6-acetyllysine. {ECO:0000250}.
FT   MOD_RES     442    442       N6-succinyllysine. {ECO:0000250}.
FT   MOD_RES     661    661       N6-acetyllysine. {ECO:0000250}.
FT   MOD_RES     741    741       N6-carboxylysine.
FT                                {ECO:0000269|PubMed:18297087}.
FT   MOD_RES     748    748       N6-acetyllysine. {ECO:0000250}.
FT   MOD_RES     992    992       N6-acetyllysine. {ECO:0000250}.
FT   MOD_RES    1061   1061       N6-acetyllysine. {ECO:0000250}.
FT   MOD_RES    1090   1090       N6-acetyllysine.
FT                                {ECO:0000269|PubMed:19608861}.
FT   MOD_RES    1124   1124       N6-acetyllysine. {ECO:0000250}.
FT   MOD_RES    1144   1144       N6-biotinyllysine.
FT                                {ECO:0000269|PubMed:6548474,
FT                                ECO:0000269|PubMed:7918683}.
FT   VAR_SEQ     457    529       TNIAFLQNVLNNQQFLAGTVDTQFIDENPELFQLRPAQNRA
FT                                QKLLHYLGHVMVNGPTTPIPVKASPSPTDPVV -> VRRHQ
FT                                AQPLAAALGRPCGQEARRPQAAVTAPTGPGSPTLVRVPPAA
FT                                RVLSSRLGGPSQTTPETSTEVSPTILL (in isoform
FT                                2). {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_056358.
FT   VAR_SEQ     530   1178       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_056359.
FT   VARIANT      76     76       H -> L (in dbSNP:rs7104156).
FT                                /FTId=VAR_048416.
FT   VARIANT     145    145       V -> A (in PC deficiency; mild;
FT                                dbSNP:rs28940591).
FT                                {ECO:0000269|PubMed:19306334,
FT                                ECO:0000269|PubMed:9585002}.
FT                                /FTId=VAR_015199.
FT   VARIANT     156    156       R -> Q (in PC deficiency).
FT                                {ECO:0000269|PubMed:19306334}.
FT                                /FTId=VAR_058957.
FT   VARIANT     270    270       R -> W (in PC deficiency).
FT                                {ECO:0000269|PubMed:19306334}.
FT                                /FTId=VAR_058958.
FT   VARIANT     304    304       Y -> C (in PC deficiency).
FT                                {ECO:0000269|PubMed:19306334}.
FT                                /FTId=VAR_058959.
FT   VARIANT     451    451       R -> C (in PC deficiency; mild).
FT                                {ECO:0000269|PubMed:19306334,
FT                                ECO:0000269|PubMed:9585002}.
FT                                /FTId=VAR_015200.
FT   VARIANT     583    583       R -> L (in PC deficiency).
FT                                {ECO:0000269|PubMed:19306334}.
FT                                /FTId=VAR_058960.
FT   VARIANT     610    610       A -> T (in PC deficiency; mild;
FT                                dbSNP:rs28940589).
FT                                {ECO:0000269|PubMed:19306334,
FT                                ECO:0000269|PubMed:9585612}.
FT                                /FTId=VAR_008095.
FT   VARIANT     631    631       R -> Q (in PC deficiency).
FT                                {ECO:0000269|PubMed:19306334}.
FT                                /FTId=VAR_058961.
FT   VARIANT     743    743       M -> I (in PC deficiency; mild;
FT                                dbSNP:rs28940590).
FT                                {ECO:0000269|PubMed:19306334,
FT                                ECO:0000269|PubMed:9585612}.
FT                                /FTId=VAR_008096.
FT   VARIANT    1131   1133       Missing (in PC deficiency).
FT                                {ECO:0000269|PubMed:19306334}.
FT                                /FTId=VAR_058962.
FT   MUTAGEN    1077   1077       F->A,E: Loss of tetramerization and
FT                                enzyme activity, resulting in an inactive
FT                                homodimer. {ECO:0000269|PubMed:18297087}.
FT   CONFLICT    225    226       LA -> WP (in Ref. 2; AAB31500).
FT                                {ECO:0000305}.
FT   CONFLICT    352    352       A -> S (in Ref. 3; AAA82937).
FT                                {ECO:0000305}.
FT   CONFLICT    385    386       RS -> PT (in Ref. 2; AAB31500).
FT                                {ECO:0000305}.
FT   CONFLICT    486    487       EL -> DV (in Ref. 2; AAB31500).
FT                                {ECO:0000305}.
FT   CONFLICT    638    638       P -> R (in Ref. 2; AAB31500).
FT                                {ECO:0000305}.
FT   CONFLICT    729    729       E -> A (in Ref. 2; AAB31500).
FT                                {ECO:0000305}.
FT   CONFLICT    774    775       DT -> AP (in Ref. 2; AAB31500).
FT                                {ECO:0000305}.
FT   HELIX       495    510
FT   HELIX       541    559
FT   STRAND      564    567
FT   TURN        569    571
FT   HELIX       572    577
FT   HELIX       584    597
FT   STRAND      602    608
FT   HELIX       611    617
FT   HELIX       623    633
FT   STRAND      635    637
FT   STRAND      639    643
FT   HELIX       645    647
FT   STRAND      650    652
FT   HELIX       656    669
FT   STRAND      673    677
FT   HELIX       683    694
FT   TURN        695    697
FT   STRAND      698    705
FT   HELIX       720    733
FT   STRAND      736    741
FT   HELIX       749    762
FT   STRAND      768    771
FT   HELIX       779    788
FT   STRAND      792    797
FT   HELIX       799    801
FT   HELIX       810    817
FT   HELIX       828    844
FT   HELIX       845    848
FT   HELIX       850    852
FT   HELIX       861    864
FT   HELIX       868    875
FT   HELIX       876    878
FT   TURN        879    881
FT   HELIX       886    900
FT   HELIX       910    923
FT   HELIX       928    934
FT   TURN        935    937
FT   HELIX       942    947
FT   TURN        948    950
FT   HELIX       961    968
FT   STRAND      969    971
FT   HELIX       978    981
FT   HELIX       989    997
FT   HELIX      1004   1012
FT   HELIX      1014   1026
FT   HELIX      1035   1040
FT   STRAND     1047   1051
FT   TURN       1053   1055
FT   STRAND     1057   1068
FT   STRAND     1072   1090
FT   HELIX      1092   1094
FT   STRAND     1108   1110
FT   STRAND     1118   1123
FT   STRAND     1138   1144
FT   STRAND     1146   1149
FT   STRAND     1164   1168
FT   STRAND     1173   1175
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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