ID ACACA_RAT Reviewed; 2345 AA.
AC P11497; A1EC79; P97902;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 24-JAN-2024, entry version 194.
DE RecName: Full=Acetyl-CoA carboxylase 1 {ECO:0000305};
DE Short=ACC1;
DE EC=6.4.1.2 {ECO:0000250|UniProtKB:Q13085};
DE AltName: Full=ACC-alpha;
GN Name=Acaca {ECO:0000312|RGD:621248}; Synonyms=Acac;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=2901088; DOI=10.1073/pnas.85.16.5784;
RA Lopez-Casillas F., Bai D.-H., Luo X., Kong I.-S., Hermodson M.A.,
RA Kim K.-H.;
RT "Structure of the coding sequence and primary amino acid sequence of
RT acetyl-coenzyme A carboxylase.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:5784-5788(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2566999; DOI=10.1073/pnas.86.11.4042;
RA Luo X.N., Park K., Lopez-Casillas F., Kim K.-H.;
RT "Structural features of the acetyl-CoA carboxylase gene: mechanisms for the
RT generation of mRNAs with 5' end heterogeneity.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:4042-4046(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=Dahl salt-sensitive, and Lewis;
RX PubMed=17218081; DOI=10.1016/j.ygeno.2006.12.005;
RA Saad Y., Garrett M.R., Manickavasagam E., Yerga-Woolwine S., Farms P.,
RA Radecki T., Joe B.;
RT "Fine-mapping and comprehensive transcript analysis reveals nonsynonymous
RT variants within a novel 1.17 Mb blood pressure QTL region on rat chromosome
RT 10.";
RL Genomics 89:343-353(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-33.
RX PubMed=2565337; DOI=10.1016/s0021-9258(18)83218-5;
RA Lopez-Casillas F., Kim K.-H.;
RT "Heterogeneity at the 5' end of rat acetyl-coenzyme A carboxylase mRNA.
RT Lipogenic conditions enhance synthesis of a unique mRNA in liver.";
RL J. Biol. Chem. 264:7176-7184(1989).
RN [5]
RP PROTEIN SEQUENCE OF 76-85 AND 1198-1201, AND PHOSPHORYLATION AT SER-77;
RP SER-79 AND SER-1200.
RX PubMed=2900138; DOI=10.1111/j.1432-1033.1988.tb14201.x;
RA Munday M.R., Campbell D.G., Carling D., Hardie D.G.;
RT "Identification by amino acid sequencing of three major regulatory
RT phosphorylation sites on rat acetyl-CoA carboxylase.";
RL Eur. J. Biochem. 175:331-338(1988).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1167-1200 (ISOFORMS 1 AND 2), AND
RP PHOSPHORYLATION AT SER-1200.
RX PubMed=1974251; DOI=10.1016/s0021-9258(18)77405-x;
RA Kong I.-S., Lopez-Casillas F., Kim K.-H.;
RT "Acetyl-CoA carboxylase mRNA species with or without inhibitory coding
RT sequence for Ser-1200 phosphorylation.";
RL J. Biol. Chem. 265:13695-13701(1990).
RN [7]
RP PARTIAL PROTEIN SEQUENCE, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Wistar; TISSUE=Liver;
RX PubMed=7910165; DOI=10.1016/s0021-9258(17)36642-5;
RA Winz R., Hess D., Aebersold R., Brownsey R.W.;
RT "Unique structural features and differential phosphorylation of the 280-kDa
RT component (isozyme) of rat liver acetyl-CoA carboxylase.";
RL J. Biol. Chem. 269:14438-14445(1994).
RN [8]
RP BIOTINYLATION AT LYS-785, AND COFACTOR.
RX PubMed=2567668; DOI=10.1111/j.1432-1033.1989.tb14823.x;
RA Bai D.-H., Moon T.-W., Lopez-Casillas F., Andrews P.C., Kim K.-H.;
RT "Analysis of the biotin-binding site on acetyl-CoA carboxylase from rat.";
RL Eur. J. Biochem. 182:239-245(1989).
RN [9]
RP PHOSPHORYLATION AT SER-79; SER-1200 AND SER-1215.
RX PubMed=1346520; DOI=10.1111/j.1432-1033.1992.tb16591.x;
RA Davies S.P., Carling D., Munday M.R., Hardie D.G.;
RT "Diurnal rhythm of phosphorylation of rat liver acetyl-CoA carboxylase by
RT the AMP-activated protein kinase, demonstrated using freeze-clamping.
RT Effects of high fat diets.";
RL Eur. J. Biochem. 203:615-623(1992).
RN [10]
RP PHOSPHORYLATION BY AMPK.
RX PubMed=9029219; DOI=10.1152/jappl.1997.82.1.219;
RA Winder W.W., Wilson H.A., Hardie D.G., Rasmussen B.B., Hutber C.A.,
RA Call G.B., Clayton R.D., Conley L.M., Yoon S., Zhou B.;
RT "Phosphorylation of rat muscle acetyl-CoA carboxylase by AMP-activated
RT protein kinase and protein kinase A.";
RL J. Appl. Physiol. 82:219-225(1997).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16396499; DOI=10.1021/pr0503073;
RA Moser K., White F.M.;
RT "Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-
RT MS/MS.";
RL J. Proteome Res. 5:98-104(2006).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-25; SER-29; SER-34;
RP SER-47; SER-49; SER-79; THR-609 AND SER-1258, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Cytosolic enzyme that catalyzes the carboxylation of acetyl-
CC CoA to malonyl-CoA, the first and rate-limiting step of de novo fatty
CC acid biosynthesis. This is a 2 steps reaction starting with the ATP-
CC dependent carboxylation of the biotin carried by the biotin carboxyl
CC carrier (BCC) domain followed by the transfer of the carboxyl group
CC from carboxylated biotin to acetyl-CoA. {ECO:0000250|UniProtKB:Q13085}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-
CC CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2;
CC Evidence={ECO:0000250|UniProtKB:Q13085};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11309;
CC Evidence={ECO:0000250|UniProtKB:Q13085};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00409,
CC ECO:0000255|PROSITE-ProRule:PRU00969};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00409,
CC ECO:0000255|PROSITE-ProRule:PRU00969};
CC Note=Binds 2 magnesium or manganese ions per subunit.
CC {ECO:0000255|PROSITE-ProRule:PRU00409, ECO:0000255|PROSITE-
CC ProRule:PRU00969};
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU01066,
CC ECO:0000305|PubMed:2567668};
CC -!- ACTIVITY REGULATION: Inhibited by phosphorylation (By similarity).
CC Citrate promotes oligomerization of the protein into filaments that
CC correspond to the most active form of the carboxylase (By similarity).
CC {ECO:0000250|UniProtKB:Q13085}.
CC -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from
CC acetyl-CoA: step 1/1. {ECO:0000250|UniProtKB:Q13085}.
CC -!- SUBUNIT: Monomer, homodimer, and homotetramer. Can form filamentous
CC polymers. Interacts in its inactive phosphorylated form with the BRCT
CC domains of BRCA1 which prevents ACACA dephosphorylation and inhibits
CC lipid synthesis. Interacts with MID1IP1; interaction with MID1IP1
CC promotes oligomerization and increases its activity.
CC {ECO:0000250|UniProtKB:Q13085}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q5SWU9}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P11497-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P11497-2; Sequence=VSP_011753;
CC -!- DOMAIN: Consists of an N-terminal biotin carboxylation/carboxylase (BC)
CC domain that catalyzes the ATP-dependent transient carboxylation of the
CC biotin covalently attached to the central biotinyl-binding/biotin
CC carboxyl carrier (BCC) domain. The C-terminal carboxyl transferase (CT)
CC domain catalyzes the transfer of the carboxyl group from carboxylated
CC biotin to acetyl-CoA to produce malonyl-CoA.
CC {ECO:0000250|UniProtKB:Q13085}.
CC -!- PTM: The N-terminus is blocked.
CC -!- PTM: Phosphorylation on Ser-1262 is required for interaction with
CC BRCA1. {ECO:0000250}.
CC -!- PTM: Phosphorylation at Ser-79 by AMPK inactivates enzyme activity.
CC Phosphorylated in vitro at Ser-1200 and Ser-1215 by AMPK; the relevance
CC of phosphorylation of these sites in vivo is however unclear.
CC {ECO:0000269|PubMed:1346520, ECO:0000269|PubMed:1974251,
CC ECO:0000269|PubMed:2900138, ECO:0000269|PubMed:9029219}.
CC -!- PTM: The biotin cofactor is covalently attached to the central
CC biotinyl-binding domain and is required for the catalytic activity.
CC {ECO:0000305|PubMed:2567668}.
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DR EMBL; J03808; AAA40653.1; -; mRNA.
DR EMBL; M26731; AAA40652.1; -; Genomic_DNA.
DR EMBL; EF121986; ABL63425.1; -; mRNA.
DR EMBL; EF121987; ABL63426.1; -; mRNA.
DR EMBL; M26195; AAA40654.1; -; mRNA.
DR EMBL; M26196; AAA40655.1; -; mRNA.
DR EMBL; M26197; AAA40656.1; -; mRNA.
DR EMBL; M55315; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; A35578; A35578.
DR RefSeq; NP_071529.1; NM_022193.1.
DR AlphaFoldDB; P11497; -.
DR SMR; P11497; -.
DR BioGRID; 248868; 1.
DR STRING; 10116.ENSRNOP00000073421; -.
DR BindingDB; P11497; -.
DR ChEMBL; CHEMBL2397; -.
DR GuidetoPHARMACOLOGY; 1263; -.
DR iPTMnet; P11497; -.
DR PhosphoSitePlus; P11497; -.
DR jPOST; P11497; -.
DR PaxDb; 10116-ENSRNOP00000049438; -.
DR GeneID; 60581; -.
DR KEGG; rno:60581; -.
DR AGR; RGD:621248; -.
DR CTD; 31; -.
DR RGD; 621248; Acaca.
DR eggNOG; KOG0368; Eukaryota.
DR InParanoid; P11497; -.
DR OrthoDB; 911at2759; -.
DR PhylomeDB; P11497; -.
DR Reactome; R-RNO-163765; ChREBP activates metabolic gene expression.
DR Reactome; R-RNO-196780; Biotin transport and metabolism.
DR Reactome; R-RNO-200425; Carnitine metabolism.
DR Reactome; R-RNO-75105; Fatty acyl-CoA biosynthesis.
DR UniPathway; UPA00655; UER00711.
DR PRO; PR:P11497; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IDA:CACAO.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0009374; F:biotin binding; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006084; P:acetyl-CoA metabolic process; ISO:RGD.
DR GO; GO:0071380; P:cellular response to prostaglandin E stimulus; ISO:RGD.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IDA:RGD.
DR GO; GO:0008610; P:lipid biosynthetic process; ISO:RGD.
DR GO; GO:0055088; P:lipid homeostasis; ISO:RGD.
DR GO; GO:0006629; P:lipid metabolic process; ISO:RGD.
DR GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
DR GO; GO:0019538; P:protein metabolic process; ISO:RGD.
DR GO; GO:0007584; P:response to nutrient; IEP:RGD.
DR GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IMP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0001894; P:tissue homeostasis; ISO:RGD.
DR CDD; cd06850; biotinyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.40.50.20; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 2.40.460.10; Biotin dependent carboxylase carboxyltransferase; 1.
DR Gene3D; 3.90.1770.10; PreATP-grasp domain; 1.
DR InterPro; IPR049076; ACCA.
DR InterPro; IPR049074; ACCA_BT.
DR InterPro; IPR034733; AcCoA_carboxyl_beta.
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 PANTHER; PTHR45728:SF5; ACETYL-COA CARBOXYLASE 1; 1.
DR PANTHER; PTHR45728; ACETYL-COA CARBOXYLASE, ISOFORM A; 1.
DR Pfam; PF08326; ACC_central; 1.
DR Pfam; PF21385; ACCA_BT; 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; SSF52096; ClpP/crotonase; 2.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding 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; 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 splicing; ATP-binding; Biotin;
KW Cytoplasm; Direct protein sequencing; Fatty acid biosynthesis;
KW Fatty acid metabolism; Ligase; Lipid biosynthesis; Lipid metabolism;
KW Magnesium; Manganese; Metal-binding; Multifunctional enzyme;
KW Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..2345
FT /note="Acetyl-CoA carboxylase 1"
FT /id="PRO_0000146765"
FT DOMAIN 116..617
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00969"
FT DOMAIN 274..465
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT DOMAIN 744..818
FT /note="Biotinyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT DOMAIN 1575..1913
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01136"
FT DOMAIN 1917..2233
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01137"
FT REGION 1575..2233
FT /note="Carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01138"
FT ACT_SITE 440
FT /evidence="ECO:0000250"
FT BINDING 314..319
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 423
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409,
FT ECO:0000255|PROSITE-ProRule:PRU00969"
FT BINDING 423
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409,
FT ECO:0000255|PROSITE-ProRule:PRU00969"
FT BINDING 436
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409,
FT ECO:0000255|PROSITE-ProRule:PRU00969"
FT BINDING 436
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409,
FT ECO:0000255|PROSITE-ProRule:PRU00969"
FT BINDING 436
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409,
FT ECO:0000255|PROSITE-ProRule:PRU00969"
FT BINDING 436
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409,
FT ECO:0000255|PROSITE-ProRule:PRU00969"
FT BINDING 438
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409,
FT ECO:0000255|PROSITE-ProRule:PRU00969"
FT BINDING 438
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409,
FT ECO:0000255|PROSITE-ProRule:PRU00969"
FT BINDING 1822
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 2126
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 2128
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q13085"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13085"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13085"
FT MOD_RES 57
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5SWU9"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:2900138"
FT MOD_RES 79
FT /note="Phosphoserine; by AMPK"
FT /evidence="ECO:0000269|PubMed:1346520,
FT ECO:0000269|PubMed:2900138, ECO:0007744|PubMed:22673903"
FT MOD_RES 609
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 785
FT /note="N6-biotinyllysine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066,
FT ECO:0000269|PubMed:2567668"
FT MOD_RES 834
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13085"
FT MOD_RES 1200
FT /note="Phosphoserine; by AMPK; in vitro"
FT /evidence="ECO:0000269|PubMed:1346520,
FT ECO:0000269|PubMed:1974251, ECO:0000269|PubMed:2900138"
FT MOD_RES 1215
FT /note="Phosphoserine; by AMPK; in vitro"
FT /evidence="ECO:0000269|PubMed:1346520"
FT MOD_RES 1217
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5SWU9"
FT MOD_RES 1226
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5SWU9"
FT MOD_RES 1258
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1262
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13085"
FT MOD_RES 1272
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13085"
FT MOD_RES 1333
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q13085"
FT MOD_RES 2152
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13085"
FT VAR_SEQ 1189..1196
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1974251"
FT /id="VSP_011753"
SQ SEQUENCE 2345 AA; 265194 MW; 78E9CF9ADE1E8771 CRC64;
MDEPSPLAKT LELNQHSRFI IGSVSEDNSE DEISNLVKLD LEEKEGSLSP ASVSSDTLSD
LGISALQDGL AFHMRSSMSG LHLVKQGRDR KKIDSQRDFT VASPAEFVTR FGGNKVIEKV
LIANNGIAAV KCMRSIRRWS YEMFRNERAI RFVVMVTPED LKANAEYIKM ADHYVPVPGG
ANNNNYANVE 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 VNLRNSISNF LHSLERGQVL
PAHTLLNTVD VELIYEGIKY VLKVTRQSPN SYVVIMNGSC VEVDVHRLSD GGLLLSYDGS
SYTTYMKEEV DRYRITIGNK TCVFEKENDP SVMRSPSAGK LIQYIVEDGG HVFAGQCYAE
IEVMKMVMTL TAVESGCIHY VKRPGAALDP GCVIAKMQLD NPSKVQQAEL HTGSLPQIQS
TALRGEKLHR VFHYVLDNLV NVMNGYCLPD PFFSSKVKDW VERLMKTLRD PSLPLLELQD
IMTSVSGRIP LNVEKSIKKE MAQYASNITS VLCQFPSQQI ANILDSHAAT LNRKSEREVF
FMNTQSIVQL VQRYRSGIRG HMKAVVMDLL RQYLRVETQF QNGHYDKCVF ALREENKSDM
NTVLNYIFSH AQVTKKNLLV TMLIDQLCGR DPTLTDELLN ILTELTQLSK TTNAKVALRA
RQVLIASHLP SYDVRHNQVE SIFLSAIDMY GHQFCIENLQ KLILSETSIF DVLPNFFYHS
NQVVRMAALE VYVRRAYIAY ELNSVQHRQL KDNTCVVEFQ FMLPTSHPNR GNIPTLNRMS
FASNLNHYGM THVASVSDVL LDNAFTPPCQ RMGGMVSFRT FEDFVRIFDE VMGCFCDSPP
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 PDGRDVIVIG
NDITYRIGSF GPQEDLLFLR ASELARAEGI PRIYVAANSG ARIGLAEEIR HMFHVAWVDS
EDPYKGYKYL YLTPQDYKRV SALNSVHCEH VEDEGESRYK ITDIIGKEEG LGAENLRGSG
MIAGESSLAY DEIITISLVT CRAIGIGAYL VRLGQRTIQV ENSHLILTGA GALNKVLGRE
VYTSNNQLGG IQIMHNNGVT HCTVCDDFEG VFTVLHWLSY MPKNVHSSVP LLNSKDPIDR
IIEFVPTKAP YDPRWMLAGR PHPTQKGQWL SGFFDYGSFS EIMQPWAQTV VVGRARLGGI
PVGVVAVETR TVELSVPADP ANLDSEAKII QQAGQVWFPD SAFKTYQAIK DFNREGLPLM
VFANWRGFSG GMKDMYDQVL KFGAYIVDGL RECSQPVMVY IPPQAELRGG SWVVIDPTIN
PRHMEMYADR ESRGSVLEPE GTVEIKFRKK DLVKTMRRVD PVYIRLAERL GTPELSPTER
KELESKLKER EEFLIPIYHQ VAVQFADLHD TPGRMQEKGV INDILDWKTS RTFFYWRLRR
LLLEDLVKKK IHSANPELTD GQIQAMLRRW FVEVEGTVKA YVWDNNKDLV EWLEKQLTEE
DGVRSVIEEN IKYISRDYVL KQIRSLVQAN PEVAMDSIVH MTQHISPTQR AEVVRILSTM
DSPST
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