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ACACA_RAT
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   03-AUG-2022, entry version 187.
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. [P11497-1]
DR   AlphaFoldDB; P11497; -.
DR   SMR; P11497; -.
DR   BioGRID; 248868; 1.
DR   STRING; 10116.ENSRNOP00000049438; -.
DR   BindingDB; P11497; -.
DR   ChEMBL; CHEMBL2397; -.
DR   iPTMnet; P11497; -.
DR   PhosphoSitePlus; P11497; -.
DR   jPOST; P11497; -.
DR   PaxDb; P11497; -.
DR   PRIDE; P11497; -.
DR   GeneID; 60581; -.
DR   KEGG; rno:60581; -.
DR   CTD; 31; -.
DR   RGD; 621248; Acaca.
DR   eggNOG; KOG0368; Eukaryota.
DR   InParanoid; P11497; -.
DR   OrthoDB; 477969at2759; -.
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:RGD.
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: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: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   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 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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