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Database: UniProt
Entry: Q5SWU9
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Original site: Q5SWU9 
ID   ACACA_MOUSE             Reviewed;        2345 AA.
AC   Q5SWU9; A2A6H4; Q5SWU6; Q5SWU7; Q5SWU8; Q6JIZ1; Q6PHL9; Q705X8;
AC   Q705X9; Q91VC8; Q925C4; Q925C5;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   10-APR-2019, entry version 148.
DE   RecName: Full=Acetyl-CoA carboxylase 1;
DE            Short=ACC1;
DE            EC=6.4.1.2 {ECO:0000269|PubMed:20952656};
DE   AltName: Full=ACC-alpha;
DE   AltName: Full=Acetyl-CoA carboxylase 265;
DE   Includes:
DE     RecName: Full=Biotin carboxylase;
DE              EC=6.3.4.14 {ECO:0000269|PubMed:20952656};
GN   Name=Acaca {ECO:0000312|MGI:MGI:108451};
GN   Synonyms=Acac {ECO:0000312|EMBL:AAS13685.1}, Gm738;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1] {ECO:0000312|EMBL:AAS13685.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J {ECO:0000312|EMBL:AAS13685.1};
RC   TISSUE=Liver {ECO:0000312|EMBL:AAS13685.1};
RA   Mao J., Wakil S.J.;
RT   "Characterization of the mouse acetyl-CoA carboxylase 1 (ACC1) gene
RT   and identification of an intronless pseudogene.";
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1-119 (ISOFORM 2).
RC   STRAIN=SWR/J; TISSUE=Brain;
RX   PubMed=15607423; DOI=10.1016/j.ygeno.2004.10.001;
RA   Travers M.T., Cambot M., Kennedy H.T., Lenoir G.M., Barber M.C.,
RA   Joulin V.;
RT   "Asymmetric expression of transcripts derived from the shared promoter
RT   between the divergently oriented ACACA and TADA2L genes.";
RL   Genomics 85:71-84(2005).
RN   [4] {ECO:0000305, ECO:0000312|EMBL:AAK57392.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-38; 1221-1348 AND 1681-1891.
RC   STRAIN=C57BL/6J {ECO:0000312|EMBL:AAK57392.1};
RX   PubMed=12668174; DOI=10.1016/S1388-1981(03)00041-6;
RA   Salles J., Sargueil F., Knoll-Gellida A., Witters L.A., Cassagne C.,
RA   Garbay B.;
RT   "Acetyl-CoA carboxylase and SREBP expression during peripheral nervous
RT   system myelination.";
RL   Biochim. Biophys. Acta 1631:229-238(2003).
RN   [5] {ECO:0000305, ECO:0000312|EMBL:AAH56500.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1501-2345.
RC   STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH56500.1};
RC   TISSUE=Brain {ECO:0000312|EMBL:AAH56500.1};
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 298-306 AND 2267-2275, INTERACTION WITH BRCA1, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=12360400; DOI=10.1038/sj.onc.1205915;
RA   Magnard C., Bachelier R., Vincent A., Jaquinod M., Kieffer S.,
RA   Lenoir G.M., Venezia N.D.;
RT   "BRCA1 interacts with acetyl-CoA carboxylase through its tandem of
RT   BRCT domains.";
RL   Oncogene 21:6729-6739(2002).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17208939; DOI=10.1074/mcp.M600218-MCP200;
RA   Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
RT   "Mitochondrial phosphoproteome revealed by an improved IMAC method and
RT   MS/MS/MS.";
RL   Mol. Cell. Proteomics 6:669-676(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25 AND SER-29, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29 AND SER-79, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-25; SER-29;
RP   SER-47; THR-57; SER-79; THR-609; SER-1215; SER-1217; THR-1226;
RP   SER-1258 AND SER-1262, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP   SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
RN   [12]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, ACTIVITY REGULATION,
RP   INTERACTION WITH MID1IP1, PHOSPHORYLATION AT SER-79, AND SUBCELLULAR
RP   LOCATION.
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   [13]
RP   INDUCTION BY ENDOCANNABINOID ANANDAMIDE.
RX   PubMed=21987372; DOI=10.1002/hep.24733;
RA   Jourdan T., Demizieux L., Gresti J., Djaouti L., Gaba L., Verges B.,
RA   Degrace P.;
RT   "Antagonism of peripheral hepatic cannabinoid receptor-1 improves
RT   liver lipid metabolism in mice: evidence from cultured explants.";
RL   Hepatology 55:790-799(2012).
CC   -!- FUNCTION: Catalyzes the rate-limiting reaction in the biogenesis
CC       of long-chain fatty acids. Carries out three functions: biotin
CC       carboxyl carrier protein, biotin carboxylase and
CC       carboxyltransferase. {ECO:0000250|UniProtKB:Q13085,
CC       ECO:0000269|PubMed:20952656}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) +
CC         malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384,
CC         ChEBI:CHEBI:456216; EC=6.4.1.2;
CC         Evidence={ECO:0000269|PubMed:20952656};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein]
CC         = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505,
CC         Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144,
CC         ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14;
CC         Evidence={ECO:0000269|PubMed:20952656};
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000250|UniProtKB:O00763};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 2 manganese ions per subunit. {ECO:0000250};
CC   -!- ACTIVITY REGULATION: By phosphorylation (By similarity). Activity
CC       is increased by oligomerization. Citrate and MID1IP1 promote
CC       oligomerization. {ECO:0000250, ECO:0000269|PubMed:20952656}.
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 in its inactive phosphorylated
CC       form with the BRCT domains of BRCA1 which prevents ACACA
CC       dephosphorylation and inhibits lipid synthesis. Interacts with
CC       MID1IP1; interaction with MID1IP1 promotes oligomerization and
CC       increases its activity. {ECO:0000269|PubMed:12360400,
CC       ECO:0000269|PubMed:20952656}.
CC   -!- INTERACTION:
CC       Q9CQ20:Mid1ip1; NbExp=2; IntAct=EBI-773043, EBI-473024;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12360400,
CC       ECO:0000269|PubMed:20952656}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative promoter usage; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q5SWU9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5SWU9-2; Sequence=VSP_026101;
CC   -!- INDUCTION: Up-regulated by endocannabinoid anandamide/AEA.
CC       {ECO:0000269|PubMed:21987372}.
CC   -!- PTM: Phosphorylation on Ser-1262 is required for interaction with
CC       BRCA1. {ECO:0000250|UniProtKB:Q13085}.
DR   EMBL; AY451393; AAS13685.1; -; mRNA.
DR   EMBL; AL596252; CAI24019.1; -; Genomic_DNA.
DR   EMBL; AL596447; CAI24019.1; JOINED; Genomic_DNA.
DR   EMBL; AL596447; CAI25271.1; -; Genomic_DNA.
DR   EMBL; AL596252; CAI25271.1; JOINED; Genomic_DNA.
DR   EMBL; AL596447; CAI25272.1; -; Genomic_DNA.
DR   EMBL; AL596447; CAI25273.1; -; Genomic_DNA.
DR   EMBL; AL596447; CAI25274.1; -; Genomic_DNA.
DR   EMBL; AL596447; CAM21560.1; -; Genomic_DNA.
DR   EMBL; AJ619664; CAF02251.1; -; mRNA.
DR   EMBL; AJ619665; CAF02252.1; -; Genomic_DNA.
DR   EMBL; AF374167; AAK57389.1; -; mRNA.
DR   EMBL; AF374168; AAK57390.1; -; mRNA.
DR   EMBL; AF374169; AAK57391.1; -; mRNA.
DR   EMBL; AF374170; AAK57392.1; -; mRNA.
DR   EMBL; BC056500; AAH56500.1; -; mRNA.
DR   CCDS; CCDS25185.1; -. [Q5SWU9-1]
DR   RefSeq; NP_579938.2; NM_133360.2. [Q5SWU9-1]
DR   RefSeq; XP_006532016.1; XM_006531953.1. [Q5SWU9-2]
DR   RefSeq; XP_006532017.1; XM_006531954.2. [Q5SWU9-1]
DR   RefSeq; XP_006532018.1; XM_006531955.1. [Q5SWU9-1]
DR   RefSeq; XP_006532019.1; XM_006531956.2. [Q5SWU9-1]
DR   RefSeq; XP_006532020.1; XM_006531957.3. [Q5SWU9-1]
DR   RefSeq; XP_011246969.1; XM_011248667.1. [Q5SWU9-1]
DR   UniGene; Mm.31374; -.
DR   ProteinModelPortal; Q5SWU9; -.
DR   SMR; Q5SWU9; -.
DR   BioGrid; 223322; 6.
DR   DIP; DIP-32276N; -.
DR   IntAct; Q5SWU9; 12.
DR   MINT; Q5SWU9; -.
DR   STRING; 10090.ENSMUSP00000099490; -.
DR   BindingDB; Q5SWU9; -.
DR   ChEMBL; CHEMBL3086; -.
DR   iPTMnet; Q5SWU9; -.
DR   PhosphoSitePlus; Q5SWU9; -.
DR   SwissPalm; Q5SWU9; -.
DR   EPD; Q5SWU9; -.
DR   jPOST; Q5SWU9; -.
DR   PaxDb; Q5SWU9; -.
DR   PeptideAtlas; Q5SWU9; -.
DR   PRIDE; Q5SWU9; -.
DR   Ensembl; ENSMUST00000020843; ENSMUSP00000020843; ENSMUSG00000020532. [Q5SWU9-1]
DR   Ensembl; ENSMUST00000103201; ENSMUSP00000099490; ENSMUSG00000020532. [Q5SWU9-1]
DR   GeneID; 107476; -.
DR   KEGG; mmu:107476; -.
DR   UCSC; uc007kql.1; mouse. [Q5SWU9-1]
DR   CTD; 31; -.
DR   MGI; MGI:108451; Acaca.
DR   eggNOG; KOG0368; Eukaryota.
DR   eggNOG; COG0439; LUCA.
DR   eggNOG; COG0511; LUCA.
DR   eggNOG; COG4799; LUCA.
DR   GeneTree; ENSGT00940000156706; -.
DR   HOVERGEN; HBG005371; -.
DR   InParanoid; Q5SWU9; -.
DR   KO; K11262; -.
DR   OMA; LPYGEWN; -.
DR   OrthoDB; 156081at2759; -.
DR   PhylomeDB; Q5SWU9; -.
DR   TreeFam; TF300061; -.
DR   BRENDA; 6.4.1.2; 3474.
DR   Reactome; R-MMU-163765; ChREBP activates metabolic gene expression.
DR   Reactome; R-MMU-196780; Biotin transport and metabolism.
DR   Reactome; R-MMU-200425; Import of palmitoyl-CoA into the mitochondrial matrix.
DR   Reactome; R-MMU-75105; Fatty acyl-CoA biosynthesis.
DR   UniPathway; UPA00655; UER00711.
DR   PRO; PR:Q5SWU9; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   Bgee; ENSMUSG00000020532; Expressed in 280 organ(s), highest expression level in mesenteric lymph node.
DR   ExpressionAtlas; Q5SWU9; baseline and differential.
DR   Genevisible; Q5SWU9; MM.
DR   GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR   GO; GO:0005739; C:mitochondrion; HDA:MGI.
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; ISO:MGI.
DR   GO; GO:0004075; F:biotin carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0019900; F:kinase binding; ISO:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006084; P:acetyl-CoA metabolic process; IDA:UniProtKB.
DR   GO; GO:0071380; P:cellular response to prostaglandin E stimulus; IDA:MGI.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0055088; P:lipid homeostasis; IMP:MGI.
DR   GO; GO:0006629; P:lipid metabolic process; IMP:MGI.
DR   GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
DR   GO; GO:0019538; P:protein metabolic process; IMP:MGI.
DR   GO; GO:0014070; P:response to organic cyclic compound; ISO:MGI.
DR   GO; GO:0001894; P:tissue homeostasis; IMP:MGI.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   InterPro; IPR034733; AcCoA_carboxyl.
DR   InterPro; IPR013537; AcCoA_COase_cen.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
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; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR011763; COA_CT_C.
DR   InterPro; IPR011762; COA_CT_N.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
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; PF00289; Biotin_carb_N; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF01039; Carboxyl_trans; 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; PS00188; BIOTIN; 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   Acetylation; Allosteric enzyme; Alternative promoter usage;
KW   ATP-binding; Biotin; Complete proteome; Cytoplasm;
KW   Direct protein sequencing; Fatty acid biosynthesis;
KW   Fatty acid metabolism; Ligase; Lipid biosynthesis; Lipid metabolism;
KW   Manganese; Metal-binding; Multifunctional enzyme; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN         1   2345       Acetyl-CoA carboxylase 1.
FT                                /FTId=PRO_0000258040.
FT   DOMAIN      116    617       Biotin carboxylation. {ECO:0000255}.
FT   DOMAIN      274    465       ATP-grasp. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   DOMAIN      744    818       Biotinyl-binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01066}.
FT   DOMAIN     1575   1913       CoA carboxyltransferase N-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01136}.
FT   DOMAIN     1917   2233       CoA carboxyltransferase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01137}.
FT   NP_BIND     300    357       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   REGION     1575   2233       Carboxyltransferase.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01138}.
FT   ACT_SITE    440    440       {ECO:0000255}.
FT   METAL       423    423       Manganese 1. {ECO:0000255}.
FT   METAL       436    436       Manganese 1. {ECO:0000255}.
FT   METAL       436    436       Manganese 2. {ECO:0000255}.
FT   METAL       438    438       Manganese 2. {ECO:0000255}.
FT   BINDING    1822   1822       Coenzyme A.
FT                                {ECO:0000250|UniProtKB:Q00955}.
FT   BINDING    2126   2126       Coenzyme A.
FT                                {ECO:0000250|UniProtKB:Q00955}.
FT   BINDING    2128   2128       Coenzyme A.
FT                                {ECO:0000250|UniProtKB:Q00955}.
FT   MOD_RES       1      1       N-acetylmethionine.
FT                                {ECO:0000250|UniProtKB:Q13085}.
FT   MOD_RES       5      5       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q13085}.
FT   MOD_RES      23     23       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES      25     25       Phosphoserine.
FT                                {ECO:0000244|PubMed:17242355,
FT                                ECO:0000244|PubMed:21183079}.
FT   MOD_RES      29     29       Phosphoserine.
FT                                {ECO:0000244|PubMed:17242355,
FT                                ECO:0000244|PubMed:18630941,
FT                                ECO:0000244|PubMed:21183079}.
FT   MOD_RES      34     34       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P11497}.
FT   MOD_RES      47     47       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES      49     49       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P11497}.
FT   MOD_RES      52     52       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q13085}.
FT   MOD_RES      57     57       Phosphothreonine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES      77     77       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P11497}.
FT   MOD_RES      79     79       Phosphoserine.
FT                                {ECO:0000244|PubMed:17208939,
FT                                ECO:0000244|PubMed:18630941,
FT                                ECO:0000244|PubMed:19131326,
FT                                ECO:0000244|PubMed:21183079,
FT                                ECO:0000269|PubMed:20952656}.
FT   MOD_RES      79     79       Phosphoserine; by AMPK.
FT                                {ECO:0000244|PubMed:17208939,
FT                                ECO:0000244|PubMed:18630941,
FT                                ECO:0000244|PubMed:19131326,
FT                                ECO:0000244|PubMed:21183079,
FT                                ECO:0000305|PubMed:20952656}.
FT   MOD_RES     609    609       Phosphothreonine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     785    785       N6-biotinyllysine. {ECO:0000250,
FT                                ECO:0000255|PROSITE-ProRule:PRU01066}.
FT   MOD_RES     834    834       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q13085}.
FT   MOD_RES    1200   1200       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P11497}.
FT   MOD_RES    1215   1215       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES    1217   1217       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES    1226   1226       Phosphothreonine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES    1258   1258       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES    1262   1262       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES    1272   1272       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q13085}.
FT   MOD_RES    1333   1333       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q13085}.
FT   MOD_RES    2152   2152       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q13085}.
FT   VAR_SEQ       1      1       M -> MMWWSTLMSLLRASSFWRRISAETIRIIRALRAYFE
FT                                RIM (in isoform 2).
FT                                {ECO:0000303|PubMed:15607423}.
FT                                /FTId=VSP_026101.
FT   CONFLICT    623    623       E -> G (in Ref. 1; AAS13685).
FT                                {ECO:0000305}.
FT   CONFLICT    906    906       S -> P (in Ref. 1; AAS13685).
FT                                {ECO:0000305}.
FT   CONFLICT    933    933       C -> Y (in Ref. 1; AAS13685).
FT                                {ECO:0000305}.
FT   CONFLICT   1456   1456       L -> S (in Ref. 1; AAS13685).
FT                                {ECO:0000305}.
FT   CONFLICT   1995   1995       S -> G (in Ref. 1; AAS13685).
FT                                {ECO:0000305}.
FT   CONFLICT   2077   2077       V -> I (in Ref. 1; AAS13685).
FT                                {ECO:0000305}.
FT   CONFLICT   2169   2169       E -> K (in Ref. 1; AAS13685).
FT                                {ECO:0000305}.
FT   CONFLICT   2251   2251       F -> S (in Ref. 1; AAS13685).
FT                                {ECO:0000305}.
FT   CONFLICT   2257   2257       T -> A (in Ref. 1; AAS13685).
FT                                {ECO:0000305}.
SQ   SEQUENCE   2345 AA;  265257 MW;  6995C534B054FE02 CRC64;
     MDEPSPLAKT LELNQHSRFI IGSVSEDNSE DEISNLVKLD LEEKEGSLSP ASVSSDTLSD
     LGISGLQDGL AFHMRSSMSG LHLVKQGRDR KKIDSQRDFT VASPAEFVTR FGGNKVIEKV
     LIANNGIAAV KCMRSIRRWS YEMFRNERAI RFVVMVTPED LKANAEYIKM ADHYVPVPGG
     PNNNNYANVE LILDIAKRIP VQAVWAGWGH ASENPKLPEL LLKNGIAFMG PPSQAMWALG
     DKIASSIVAQ TAGIPTLPWS GSGLRVDWQE NDFSKRILNV PQDLYEKGYV KDVDDGLKAA
     EEVGYPVMIK ASEGGGGKGI RKVNNADDFP NLFRQVQAEV PGSPIFVMRL AKQSRHLEVQ
     ILADQYGNAI SLFGRDCSVQ RRHQKIIEEA PAAIATPAVF EHMEQCAVKL AKMVGYVSAG
     TVEYLYSQDG SFYFLELNPR LQVEHPCTEM VADVNLPAAQ LQIAMGIPLF RIKDIRMMYG
     VSPWGDAPID FENSAHVPCP RGHVIAARIT SENPDEGFKP SSGTVQELNF RSNKNVWGYF
     SVAAAGGLHE FADSQFGHCF SWGENREEAI SNMVVALKEL SIRGDFRTTV EYLIKLLETE
     SFQLNRIDTG WLDRLIAEKV QAERPDTMLG VVCGALHVAD VSLRNSISNF LHSLERGQVL
     PAHTLLNTVD VELIYEGIKY VLKVTRQSPN SYVVIMNGSC VEVDVHRLSD GGLLLSYDGS
     SYTTYMKEEV DRYRITIGNK TCVFEKENDP SVMRSPSAGK LIQYIVEDGG HVFAGQCYAE
     IEVMKMVMTL TAVESGCIHY VKRPGAALDP GCVIAKMQLD NPSKVQQAEL HTGSLPQIQS
     TALRGEKLHR VFHYVLDNLV NVMNGYCLPD PFFSSRVKDW VERLMKTLRD PSLPLLELQD
     IMTSVSGRIP LNVEKSIKKE MAQYASNITS VLCQFPSQQI ANILDSHAAT LNRKSEREVF
     FMNTQSIVQL VQRYRSGIRG HMKAVVMDLL RQYLRVETQF QNGHYDKCVF ALREENKSDM
     NTVLNYIFSH AQVTKKNLLV TMLIDQLCGR DPTLTDELLN ILTELTQLSK TTNAKVALRA
     RQVLIASHLP SYELRHNQVE SIFLSAIDMY GHQFCIENLQ KLILSETSIF DVLPNFFYHS
     NQVVRMAALE VYVRRAYIAY ELNSVQHRQL KDNTCVVEFQ FMLPTSHPNR GNIPTLNRMS
     FASNLNHYGM THVASVSDVL LDNAFTPPCQ RMGGMVSFRT FEDFVRIFDE IMGCFCDSPP
     QSPTFPESGH TSLYDEDKVP RDEPIHILNV AIKTDGDIED DRLAAMFREF TQQNKATLVE
     HGIRRLTFLV AQKDFRKQVN CEVDQRFHRE FPKFFTFRAR DKFEEDRIYR HLEPALAFQL
     ELNRMRNFDL TAIPCANHKM HLYLGAAKVE VGTEVTDYRF FVRAIIRHSD LVTKEASFEY
     LQNEGERLLL EAMDELEVAF NNTNVRTDCN HIFLNFVPTV IMDPSKIEES VRSMVMRYGS
     RLWKLRVLQA ELKINIRLTT TGKAIPIRLF LTNESGYYLD ISLYKEVTDS RTAQIMFQAY
     GDKQGPLHGM LINTPYVTKD LLQSKRFQAQ SLGTTYIYDI PEMFRQSLIK LWESMSTQAF
     LPSPPLPSDI LTYTELVLDD QGQLVHMNRL PGGNEIGMVA WKMSLKSPEY PDGRDIIVIG
     NDITYRIGSF GPQEDLLFLR ASELARAEGI PRIYVAANSG ARIGLAEEIR HMFHVAWVDP
     EDPYKGYKYL YLTPQDYKRV SALNSVHCEH VEDEGESRYK ITDIIGKEEG LGAENLRGSG
     MIAGESSLAY DEVITISLVT CRAIGIGAYL VRLGQRTIQV ENSHLILTGA GALNKVLGRE
     VYTSNNQLGG IQIMHNNGVT HSTVCDDFEG VFTVLHWLSY MPKSVHSSVP LLNSKDPIDR
     IIEFVPTKAP YDPRWMLAGR PHPTQKGQWL SGFFDYGSFS EIMQPWAQTV VVGRARLGGI
     PVGVVAVETR TVELSIPADP ANLDSEAKII QQAGQVWFPD SAFKTYQAIK DFNREGLPLM
     VFANWRGFSG GMKDMYDQVL KFGAYIVDGL RECSQPVMVY IPPQAELRGG SWVVIDPTIN
     PRHMEMYADR ESRGSVLEPE GTVEIKFRKK DLVKTMRRVD PVYIRLAERL GTPELSPTER
     KELESKLKER EEFLIPIYHQ VAVQFADLHD TPGRMQEKGV INDILDWKTS RTFFYWRLRR
     LLLEDLVKKK IHNANPELTD GQIQAMLRRW FVEVEGTVKA YVWDNNKDLV EWLEKQLTEE
     DGVRSVIEEN IKYISRDYVL KQIRSLVQAN PEVAMDSIVH MTQHISPTQR AEVVRILSTM
     DSPST
//
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