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Entry: O00763
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ID   ACACB_HUMAN             Reviewed;        2458 AA.
AC   O00763; A6NK36; Q16852; Q1HEC1; Q6KE87; Q6KE89; Q6TY48;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 3.
DT   03-SEP-2014, entry version 145.
DE   RecName: Full=Acetyl-CoA carboxylase 2;
DE            EC=6.4.1.2;
DE   AltName: Full=ACC-beta;
DE   Includes:
DE     RecName: Full=Biotin carboxylase;
DE              EC=6.3.4.14;
GN   Name=ACACB; Synonyms=ACC2, ACCB;
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] (ISOFORMS LONG AND SHORT), AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Liver;
RX   PubMed=9099716; DOI=10.1074/jbc.272.16.10669;
RA   Abu-Elheiga L., Almarza-Ortega D.B., Baldini A., Wakil S.J.;
RT   "Human acetyl-CoA carboxylase 2. Molecular cloning, characterization,
RT   chromosomal mapping, and evidence for two isoforms.";
RL   J. Biol. Chem. 272:10669-10677(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), COFACTOR,
RP   BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, AND VARIANT
RP   ILE-2141.
RX   PubMed=16854592; DOI=10.1016/j.pep.2006.06.005;
RA   Cheng D., Chu C.-H., Chen L., Feder J.N., Mintier G.A., Wu Y.,
RA   Cook J.W., Harpel M.R., Locke G.A., An Y., Tamura J.K.;
RT   "Expression, purification, and characterization of human and rat
RT   acetyl coenzyme A carboxylase (ACC) isozymes.";
RL   Protein Expr. Purif. 51:11-21(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), AND VARIANT ILE-2141.
RC   TISSUE=Heart;
RA   Peng X.R., Lindgren K., Corneliussen B.;
RT   "Corrected sequence for human acetyl-CoA carboxylase 2 obtained by
RT   alignment to human genomic DNA and PCR cloning from human skeletal
RT   muscle and heart cDNA.";
RL   Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
RC   TISSUE=Heart;
RA   Mao J., Wakil S.J.;
RT   "Alternative splicing in the human acetyl-CoA carboxylase 2 (ACC2)
RT   gene.";
RL   Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16541075; DOI=10.1038/nature04569;
RA   Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA   Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA   Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
RA   Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA   Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA   Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA   Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA   Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA   Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA   Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA   Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA   Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA   Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA   Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA   Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA   Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA   Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA   Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
RA   Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA   Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA   Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA   Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA   Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA   Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA   Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA   Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA   Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA   Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA   Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA   Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA   Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA   Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA   Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA   Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA   Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA   Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
RA   Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA   Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA   Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA   Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA   Kucherlapati R., Weinstock G., Gibbs R.A.;
RT   "The finished DNA sequence of human chromosome 12.";
RL   Nature 440:346-351(2006).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1324-2109.
RC   TISSUE=Adipose tissue;
RX   PubMed=8670171;
RA   Widmer J., Fassihi K.S., Schlichter S.C., Wheeler K.S., Crute B.E.,
RA   King N., Nutile-Mcmenemy N., Noll W.W., Daniel S., Ha J., Kim K.-H.,
RA   Witters L.A.;
RT   "Identification of a second human acetyl-CoA carboxylase gene.";
RL   Biochem. J. 316:915-922(1996).
RN   [7]
RP   PHOSPHORYLATION AT SER-222 BY AMPK.
RX   PubMed=12488245; DOI=10.1152/ajpendo.00436.2002;
RA   Wojtaszewski J.F., MacDonald C., Nielsen J.N., Hellsten Y.,
RA   Hardie D.G., Kemp B.E., Kiens B., Richter E.A.;
RT   "Regulation of 5'AMP-activated protein kinase activity and substrate
RT   utilization in exercising human skeletal muscle.";
RL   Am. J. Physiol. 284:E813-E822(2003).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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   [9]
RP   CATALYTIC ACTIVITY, SUBUNIT, ENZYME REGULATION, AND INTERACTION WITH
RP   MID1IP1.
RX   PubMed=20952656; DOI=10.1073/pnas.1012736107;
RA   Colbert C.L., Kim C.W., Moon Y.A., Henry L., Palnitkar M.,
RA   McKean W.B., Fitzgerald K., Deisenhofer J., Horton J.D., Kwon H.J.;
RT   "Crystal structure of Spot 14, a modulator of fatty acid synthesis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:18820-18825(2010).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 217-775.
RX   PubMed=17876819; DOI=10.1002/prot.21611;
RA   Cho Y.S., Lee J.I., Shin D., Kim H.T., Cheon Y.H., Seo C.I., Kim Y.E.,
RA   Hyun Y.L., Lee Y.S., Sugiyama K., Park S.Y., Ro S., Cho J.M.,
RA   Lee T.G., Heo Y.S.;
RT   "Crystal structure of the biotin carboxylase domain of human acetyl-
RT   CoA carboxylase 2.";
RL   Proteins 70:268-272(2008).
RN   [11]
RP   STRUCTURE BY NMR OF 885-971.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of RSGI RUH-053, an apo-biotin carboxy carrier
RT   protein from human transcarboxylase.";
RL   Submitted (OCT-2006) to the PDB data bank.
RN   [12]
RP   VARIANT [LARGE SCALE ANALYSIS] LEU-193.
RX   PubMed=18772397; DOI=10.1126/science.1164368;
RA   Jones S., Zhang X., Parsons D.W., Lin J.C., Leary R.J., Angenendt P.,
RA   Mankoo P., Carter H., Kamiyama H., Jimeno A., Hong S.M., Fu B.,
RA   Lin M.T., Calhoun E.S., Kamiyama M., Walter K., Nikolskaya T.,
RA   Nikolsky Y., Hartigan J., Smith D.R., Hidalgo M., Leach S.D.,
RA   Klein A.P., Jaffee E.M., Goggins M., Maitra A., Iacobuzio-Donahue C.,
RA   Eshleman J.R., Kern S.E., Hruban R.H., Karchin R., Papadopoulos N.,
RA   Parmigiani G., Vogelstein B., Velculescu V.E., Kinzler K.W.;
RT   "Core signaling pathways in human pancreatic cancers revealed by
RT   global genomic analyses.";
RL   Science 321:1801-1806(2008).
CC   -!- FUNCTION: ACC-beta may be involved in the provision of malonyl-CoA
CC       or in the regulation of fatty acid oxidation, rather than fatty
CC       acid biosynthesis. Carries out three functions: biotin carboxyl
CC       carrier protein, biotin carboxylase and carboxyltransferase.
CC   -!- CATALYTIC ACTIVITY: ATP + acetyl-CoA + HCO(3)(-) = ADP + phosphate
CC       + malonyl-CoA.
CC   -!- CATALYTIC ACTIVITY: ATP + biotin-[carboxyl-carrier-protein] +
CC       CO(2) = ADP + phosphate + carboxy-biotin-[carboxyl-carrier-
CC       protein].
CC   -!- COFACTOR: Biotin (By similarity).
CC   -!- COFACTOR: Binds 2 manganese ions per subunit (By similarity).
CC   -!- ENZYME REGULATION: Activity is increased by oligomerization.
CC       Activated by citrate. Citrate and MID1IP1 promote oligomerization.
CC       Inhibited by malonyl-CoA.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=120 uM for ATP;
CC         KM=58 uM for Acetyl-CoA;
CC         KM=3.0 mM for NaHCO(3);
CC   -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA
CC       from acetyl-CoA: step 1/1.
CC   -!- SUBUNIT: Monomer, homodimer, and homotetramer. Can form
CC       filamentous polymers. Interacts with MID1IP1; interaction with
CC       MID1IP1 promotes oligomerization and increases its activity.
CC   -!- INTERACTION:
CC       P50747:HLCS; NbExp=4; IntAct=EBI-2211739, EBI-3915568;
CC   -!- SUBCELLULAR LOCATION: Endomembrane system. Note=May associate with
CC       membranes.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Long;
CC         IsoId=O00763-1; Sequence=Displayed;
CC       Name=Short;
CC         IsoId=O00763-2; Sequence=VSP_000547;
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in the heart, skeletal
CC       muscles and liver.
CC   -!- PTM: Phosphorylated by AMPK, leading to inactivate the enzyme.
CC   -!- SIMILARITY: Contains 1 ATP-grasp domain.
CC   -!- SIMILARITY: Contains 1 biotin carboxylation domain.
CC   -!- SIMILARITY: Contains 1 biotinyl-binding domain.
CC   -!- SIMILARITY: Contains 1 carboxyltransferase domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB58382.1; Type=Miscellaneous discrepancy; Note=Many Frameshifts and conflicts;
CC       Sequence=CAE01470.2; Type=Erroneous translation; Note=Wrong choice of CDS;
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DR   EMBL; U89344; AAB58382.1; ALT_SEQ; mRNA.
DR   EMBL; DQ493870; ABF48723.1; -; mRNA.
DR   EMBL; AJ575431; CAE01470.2; ALT_SEQ; mRNA.
DR   EMBL; AJ575592; CAE01471.3; -; mRNA.
DR   EMBL; AY382667; AAR37018.1; -; mRNA.
DR   EMBL; AC007637; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; U34591; AAC50571.1; -; mRNA.
DR   CCDS; CCDS31898.1; -. [O00763-1]
DR   PIR; S71091; S71091.
DR   RefSeq; NP_001084.3; NM_001093.3. [O00763-1]
DR   RefSeq; XP_005253933.1; XM_005253876.2. [O00763-1]
DR   RefSeq; XP_006719428.1; XM_006719365.1. [O00763-1]
DR   UniGene; Hs.234898; -.
DR   PDB; 2DN8; NMR; -; A=885-971.
DR   PDB; 2HJW; X-ray; 2.50 A; A=217-775.
DR   PDB; 2KCC; NMR; -; A=891-965.
DR   PDB; 3FF6; X-ray; 3.19 A; A/B/C/D=1693-2450.
DR   PDB; 3GID; X-ray; 2.30 A; A/B=238-760.
DR   PDB; 3GLK; X-ray; 2.10 A; A=238-760.
DR   PDB; 3JRW; X-ray; 2.60 A; A=217-775.
DR   PDB; 3JRX; X-ray; 2.50 A; A=217-775.
DR   PDB; 3TDC; X-ray; 2.41 A; A=1690-2445.
DR   PDB; 4HQ6; X-ray; 2.70 A; A=217-776.
DR   PDBsum; 2DN8; -.
DR   PDBsum; 2HJW; -.
DR   PDBsum; 2KCC; -.
DR   PDBsum; 3FF6; -.
DR   PDBsum; 3GID; -.
DR   PDBsum; 3GLK; -.
DR   PDBsum; 3JRW; -.
DR   PDBsum; 3JRX; -.
DR   PDBsum; 3TDC; -.
DR   PDBsum; 4HQ6; -.
DR   ProteinModelPortal; O00763; -.
DR   SMR; O00763; 237-758, 891-960, 1695-2449.
DR   BioGrid; 106550; 5.
DR   DIP; DIP-51617N; -.
DR   IntAct; O00763; 5.
DR   MINT; MINT-6800190; -.
DR   STRING; 9606.ENSP00000367079; -.
DR   BindingDB; O00763; -.
DR   ChEMBL; CHEMBL4829; -.
DR   DrugBank; DB00121; Biotin.
DR   GuidetoPHARMACOLOGY; 1264; -.
DR   PhosphoSite; O00763; -.
DR   MaxQB; O00763; -.
DR   PaxDb; O00763; -.
DR   PRIDE; O00763; -.
DR   DNASU; 32; -.
DR   Ensembl; ENST00000338432; ENSP00000341044; ENSG00000076555. [O00763-1]
DR   Ensembl; ENST00000377848; ENSP00000367079; ENSG00000076555. [O00763-1]
DR   GeneID; 32; -.
DR   KEGG; hsa:32; -.
DR   UCSC; uc001tob.3; human. [O00763-1]
DR   CTD; 32; -.
DR   GeneCards; GC12P109577; -.
DR   H-InvDB; HIX0036741; -.
DR   HGNC; HGNC:85; ACACB.
DR   HPA; HPA006554; -.
DR   MIM; 601557; gene.
DR   neXtProt; NX_O00763; -.
DR   PharmGKB; PA24422; -.
DR   eggNOG; COG0511; -.
DR   HOVERGEN; HBG005371; -.
DR   KO; K11262; -.
DR   OMA; WRLRVAQ; -.
DR   OrthoDB; EOG7HXCPW; -.
DR   PhylomeDB; O00763; -.
DR   TreeFam; TF300061; -.
DR   BioCyc; MetaCyc:HS01211-MONOMER; -.
DR   BRENDA; 6.4.1.2; 2681.
DR   Reactome; REACT_11082; Import of palmitoyl-CoA into the mitochondrial matrix.
DR   Reactome; REACT_11153; Biotin transport and metabolism.
DR   Reactome; REACT_147904; Activation of gene expression by SREBF (SREBP).
DR   Reactome; REACT_169312; Defective HLCS causes multiple carboxylase deficiency.
DR   Reactome; REACT_2122; ChREBP activates metabolic gene expression.
DR   SABIO-RK; O00763; -.
DR   UniPathway; UPA00655; UER00711.
DR   EvolutionaryTrace; O00763; -.
DR   GeneWiki; ACACB; -.
DR   GenomeRNAi; 32; -.
DR   NextBio; 123; -.
DR   PRO; PR:O00763; -.
DR   ArrayExpress; O00763; -.
DR   Bgee; O00763; -.
DR   CleanEx; HS_ACACB; -.
DR   Genevestigator; O00763; -.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR   GO; GO:0005741; C:mitochondrial outer membrane; TAS:Reactome.
DR   GO; GO:0003989; F:acetyl-CoA carboxylase activity; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0009374; F:biotin binding; IEA:Ensembl.
DR   GO; GO:0004075; F:biotin carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0006084; P:acetyl-CoA metabolic process; IDA:UniProtKB.
DR   GO; GO:0006768; P:biotin metabolic process; TAS:Reactome.
DR   GO; GO:0006853; P:carnitine shuttle; TAS:Reactome.
DR   GO; GO:0044255; P:cellular lipid metabolic process; TAS:Reactome.
DR   GO; GO:0006112; P:energy reserve metabolic process; TAS:Reactome.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0031325; P:positive regulation of cellular metabolic process; TAS:Reactome.
DR   GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
DR   GO; GO:0042493; P:response to drug; IEA:Ensembl.
DR   GO; GO:0014070; P:response to organic cyclic compound; 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; 3.30.1490.20; -; 1.
DR   Gene3D; 3.30.470.20; -; 1.
DR   Gene3D; 3.40.50.20; -; 1.
DR   Gene3D; 3.90.226.10; -; 3.
DR   InterPro; IPR013537; AcCoA_COase_cen.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR013816; ATP_grasp_subdomain_2.
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; IPR000022; Carboxyl_trans.
DR   InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom.
DR   InterPro; IPR011763; COA_CT_C.
DR   InterPro; IPR011762; COA_CT_N.
DR   InterPro; IPR016185; PreATP-grasp_dom.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   Pfam; PF08326; ACC_central; 1.
DR   Pfam; PF02785; Biotin_carb_C; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF01039; Carboxyl_trans; 1.
DR   Pfam; PF00289; CPSase_L_chain; 1.
DR   Pfam; PF02786; CPSase_L_D2; 1.
DR   SMART; SM00878; Biotin_carb_C; 1.
DR   SUPFAM; SSF51230; SSF51230; 1.
DR   SUPFAM; SSF51246; SSF51246; 1.
DR   SUPFAM; SSF52096; SSF52096; 2.
DR   SUPFAM; SSF52440; SSF52440; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS50979; BC; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS50989; COA_CT_CTER; 1.
DR   PROSITE; PS50980; COA_CT_NTER; 1.
DR   PROSITE; PS00866; CPSASE_1; 1.
DR   PROSITE; PS00867; CPSASE_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Allosteric enzyme; Alternative splicing; ATP-binding;
KW   Biotin; Complete proteome; Fatty acid biosynthesis;
KW   Fatty acid metabolism; Ligase; Lipid biosynthesis; Lipid metabolism;
KW   Manganese; Membrane; Metal-binding; Multifunctional enzyme;
KW   Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome.
FT   CHAIN         1   2458       Acetyl-CoA carboxylase 2.
FT                                /FTId=PRO_0000146767.
FT   DOMAIN      259    761       Biotin carboxylation.
FT   DOMAIN      414    609       ATP-grasp.
FT   DOMAIN      895    961       Biotinyl-binding.
FT   DOMAIN     1809   2305       Carboxyltransferase.
FT   NP_BIND     458    463       ATP (Potential).
FT   ACT_SITE    584    584       By similarity.
FT   METAL       567    567       Manganese 1 (By similarity).
FT   METAL       580    580       Manganese 1 (By similarity).
FT   METAL       580    580       Manganese 2 (By similarity).
FT   METAL       582    582       Manganese 2 (By similarity).
FT   BINDING    1934   1934       Coenzyme A (By similarity).
FT   BINDING    2238   2238       Coenzyme A (By similarity).
FT   BINDING    2240   2240       Coenzyme A (By similarity).
FT   MOD_RES     222    222       Phosphoserine; by AMPK.
FT   MOD_RES     929    929       N6-biotinyllysine (By similarity).
FT   VAR_SEQ    1118   1187       Missing (in isoform Short).
FT                                /FTId=VSP_000547.
FT   VARIANT     193    193       R -> L (in a pancreatic ductal
FT                                adenocarcinoma sample; somatic mutation).
FT                                /FTId=VAR_062667.
FT   VARIANT     552    552       I -> V (in dbSNP:rs16940029).
FT                                /FTId=VAR_031255.
FT   VARIANT     651    651       A -> T (in dbSNP:rs2300455).
FT                                /FTId=VAR_031256.
FT   VARIANT    2141   2141       V -> I (in dbSNP:rs2075260).
FT                                /FTId=VAR_031257.
FT   CONFLICT      9      9       C -> R (in Ref. 2; ABF48723).
FT   CONFLICT    120    120       T -> I (in Ref. 4; AAR37018).
FT   CONFLICT    422    422       I -> T (in Ref. 4; AAR37018).
FT   CONFLICT   1340   1340       S -> N (in Ref. 6; AAC50571).
FT   CONFLICT   1383   1383       D -> G (in Ref. 6; AAC50571).
FT   CONFLICT   1425   1425       V -> M (in Ref. 6; AAC50571).
FT   CONFLICT   1819   1821       AEG -> PEA (in Ref. 6; AAC50571).
FT   CONFLICT   1892   1893       MI -> IM (in Ref. 6; AAC50571).
FT   HELIX       247    253
FT   STRAND      262    265
FT   HELIX       269    287
FT   STRAND      292    299
FT   HELIX       301    305
FT   HELIX       309    313
FT   STRAND      314    319
FT   HELIX       325    327
FT   TURN        328    330
FT   HELIX       332    341
FT   STRAND      345    348
FT   HELIX       353    356
FT   HELIX       359    366
FT   STRAND      370    373
FT   HELIX       376    379
FT   HELIX       385    394
FT   TURN        403    406
FT   HELIX       426    431
FT   HELIX       437    447
FT   STRAND      449    455
FT   STRAND      464    467
FT   TURN        470    472
FT   HELIX       473    483
FT   STRAND      489    493
FT   STRAND      496    507
FT   STRAND      509    511
FT   STRAND      513    523
FT   STRAND      524    527
FT   STRAND      530    535
FT   HELIX       541    558
FT   STRAND      562    571
FT   STRAND      572    574
FT   STRAND      576    582
FT   HELIX       589    596
FT   HELIX       600    608
FT   HELIX       613    615
FT   HELIX       617    622
FT   STRAND      635    637
FT   STRAND      646    653
FT   STRAND      669    671
FT   STRAND      679    685
FT   STRAND      700    709
FT   HELIX       710    724
FT   HELIX       728    730
FT   HELIX       732    742
FT   HELIX       744    748
FT   HELIX       754    756
FT   STRAND      896    898
FT   STRAND      900    902
FT   STRAND      903    910
FT   STRAND      914    916
FT   STRAND      921    927
FT   STRAND      930    935
FT   STRAND      937    944
FT   STRAND      957    961
FT   TURN       1698   1700
FT   HELIX      1703   1711
FT   HELIX      1717   1719
FT   HELIX      1720   1732
FT   STRAND     1742   1750
FT   STRAND     1756   1759
FT   STRAND     1767   1777
FT   STRAND     1786   1793
FT   HELIX      1798   1800
FT   HELIX      1804   1820
FT   STRAND     1824   1828
FT   HELIX      1839   1842
FT   STRAND     1846   1850
FT   HELIX      1855   1857
FT   STRAND     1859   1864
FT   HELIX      1866   1872
FT   TURN       1873   1876
FT   STRAND     1878   1885
FT   STRAND     1888   1896
FT   STRAND     1899   1901
FT   HELIX      1905   1924
FT   STRAND     1927   1931
FT   STRAND     1933   1936
FT   HELIX      1938   1946
FT   STRAND     1948   1952
FT   STRAND     1956   1960
FT   HELIX      1962   1969
FT   HELIX      1977   1981
FT   HELIX      1983   1986
FT   TURN       1987   1990
FT   STRAND     1993   1998
FT   HELIX      1999   2010
FT   HELIX      2045   2050
FT   STRAND     2055   2057
FT   STRAND     2072   2075
FT   STRAND     2082   2089
FT   STRAND     2092   2099
FT   STRAND     2104   2108
FT   STRAND     2120   2124
FT   HELIX      2131   2147
FT   STRAND     2151   2154
FT   HELIX      2164   2168
FT   HELIX      2171   2183
FT   STRAND     2189   2193
FT   STRAND     2198   2200
FT   HELIX      2201   2205
FT   HELIX      2209   2211
FT   TURN       2213   2215
FT   STRAND     2216   2221
FT   STRAND     2225   2229
FT   HELIX      2231   2238
FT   HELIX      2241   2251
FT   HELIX      2253   2261
FT   HELIX      2269   2299
FT   HELIX      2300   2302
FT   HELIX      2304   2309
FT   STRAND     2312   2317
FT   HELIX      2319   2321
FT   HELIX      2322   2344
FT   HELIX      2345   2348
FT   HELIX      2352   2365
FT   HELIX      2369   2376
FT   HELIX      2378   2388
FT   HELIX      2404   2420
FT   TURN       2423   2425
FT   HELIX      2426   2435
FT   HELIX      2439   2448
SQ   SEQUENCE   2458 AA;  276541 MW;  ED12674A1A8A0706 CRC64;
     MVLLLCLSCL IFSCLTFSWL KIWGKMTDSK PITKSKSEAN LIPSQEPFPA SDNSGETPQR
     NGEGHTLPKT PSQAEPASHK GPKDAGRRRN SLPPSHQKPP RNPLSSSDAA PSPELQANGT
     GTQGLEATDT NGLSSSARPQ GQQAGSPSKE DKKQANIKRQ LMTNFILGSF DDYSSDEDSV
     AGSSRESTRK GSRASLGALS LEAYLTTGEA ETRVPTMRPS MSGLHLVKRG REHKKLDLHR
     DFTVASPAEF VTRFGGDRVI EKVLIANNGI AAVKCMRSIR RWAYEMFRNE RAIRFVVMVT
     PEDLKANAEY IKMADHYVPV PGGPNNNNYA NVELIVDIAK RIPVQAVWAG WGHASENPKL
     PELLCKNGVA FLGPPSEAMW ALGDKIASTV VAQTLQVPTL PWSGSGLTVE WTEDDLQQGK
     RISVPEDVYD KGCVKDVDEG LEAAERIGFP LMIKASEGGG GKGIRKAESA EDFPILFRQV
     QSEIPGSPIF LMKLAQHARH LEVQILADQY GNAVSLFGRD CSIQRRHQKI VEEAPATIAP
     LAIFEFMEQC AIRLAKTVGY VSAGTVEYLY SQDGSFHFLE LNPRLQVEHP CTEMIADVNL
     PAAQLQIAMG VPLHRLKDIR LLYGESPWGV TPISFETPSN PPLARGHVIA ARITSENPDE
     GFKPSSGTVQ ELNFRSSKNV WGYFSVAATG GLHEFADSQF GHCFSWGENR EEAISNMVVA
     LKELSIRGDF RTTVEYLINL LETESFQNND IDTGWLDYLI AEKVQAEKPD IMLGVVCGAL
     NVADAMFRTC MTDFLHSLER GQVLPADSLL NLVDVELIYG GVKYILKVAR QSLTMFVLIM
     NGCHIEIDAH RLNDGGLLLS YNGNSYTTYM KEEVDSYRIT IGNKTCVFEK ENDPTVLRSP
     SAGKLTQYTV EDGGHVEAGS SYAEMEVMKM IMTLNVQERG RVKYIKRPGA VLEAGCVVAR
     LELDDPSKVH PAEPFTGELP AQQTLPILGE KLHQVFHSVL ENLTNVMSGF CLPEPVFSIK
     LKEWVQKLMM TLRHPSLPLL ELQEIMTSVA GRIPAPVEKS VRRVMAQYAS NITSVLCQFP
     SQQIATILDC HAATLQRKAD REVFFINTQS IVQLVQRYRS GIRGYMKTVV LDLLRRYLRV
     EHHFQQAHYD KCVINLREQF KPDMSQVLDC IFSHAQVAKK NQLVIMLIDE LCGPDPSLSD
     ELISILNELT QLSKSEHCKV ALRARQILIA SHLPSYELRH NQVESIFLSA IDMYGHQFCP
     ENLKKLILSE TTIFDVLPTF FYHANKVVCM ASLEVYVRRG YIAYELNSLQ HRQLPDGTCV
     VEFQFMLPSS HPNRMTVPIS ITNPDLLRHS TELFMDSGFS PLCQRMGAMV AFRRFEDFTR
     NFDEVISCFA NVPKDTPLFS EARTSLYSED DCKSLREEPI HILNVSIQCA DHLEDEALVP
     ILRTFVQSKK NILVDYGLRR ITFLIAQEKE FPKFFTFRAR DEFAEDRIYR HLEPALAFQL
     ELNRMRNFDL TAVPCANHKM HLYLGAAKVK EGVEVTDHRF FIRAIIRHSD LITKEASFEY
     LQNEGERLLL EAMDELEVAF NNTSVRTDCN HIFLNFVPTV IMDPFKIEES VRYMVMRYGS
     RLWKLRVLQA EVKINIRQTT TGSAVPIRLF ITNESGYYLD ISLYKEVTDS RSGNIMFHSF
     GNKQGPQHGM LINTPYVTKD LLQAKRFQAQ TLGTTYIYDF PEMFRQALFK LWGSPDKYPK
     DILTYTELVL DSQGQLVEMN RLPGGNEVGM VAFKMRFKTQ EYPEGRDVIV IGNDITFRIG
     SFGPGEDLLY LRASEMARAE GIPKIYVAAN SGARIGMAEE IKHMFHVAWV DPEDPHKGFK
     YLYLTPQDYT RISSLNSVHC KHIEEGGESR YMITDIIGKD DGLGVENLRG SGMIAGESSL
     AYEEIVTISL VTCRAIGIGA YLVRLGQRVI QVENSHIILT GASALNKVLG REVYTSNNQL
     GGVQIMHYNG VSHITVPDDF EGVYTILEWL SYMPKDNHSP VPIITPTDPI DREIEFLPSR
     APYDPRWMLA GRPHPTLKGT WQSGFFDHGS FKEIMAPWAQ TVVTGRARLG GIPVGVIAVE
     TRTVEVAVPA DPANLDSEAK IIQQAGQVWF PDSAYKTAQA VKDFNREKLP LMIFANWRGF
     SGGMKDMYDQ VLKFGAYIVD GLRQYKQPIL IYIPPYAELR GGSWVVIDAT INPLCIEMYA
     DKESRGGVLE PEGTVEIKFR KKDLIKSMRR IDPAYKKLME QLGEPDLSDK DRKDLEGRLK
     AREDLLLPIY HQVAVQFADF HDTPGRMLEK GVISDILEWK TARTFLYWRL RRLLLEDQVK
     QEILQASGEL SHVHIQSMLR RWFVETEGAV KAYLWDNNQV VVQWLEQHWQ AGDGPRSTIR
     ENITYLKHDS VLKTIRGLVE ENPEVAVDCV IYLSQHISPA ERAQVVHLLS TMDSPAST
//
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