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Acetyl-CoA carboxylase 1 (ACC1) (EC 6.4.1.2) (ACC-alpha) (Acetyl-CoA carboxylase 265) [Includes: Biotin carboxylase (EC 6.3.4.14)]

 ACACA_MOUSE             Reviewed;        2345 AA.
Q5SWU9; A2A6H4; Q5SWU6; Q5SWU7; Q5SWU8; Q6JIZ1; Q6PHL9; Q705X8;
Q705X9; Q91VC8; Q925C4; Q925C5;
31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
21-DEC-2004, sequence version 1.
22-NOV-2017, entry version 136.
RecName: Full=Acetyl-CoA carboxylase 1;
Short=ACC1;
EC=6.4.1.2 {ECO:0000269|PubMed:20952656};
AltName: Full=ACC-alpha;
AltName: Full=Acetyl-CoA carboxylase 265;
Includes:
RecName: Full=Biotin carboxylase;
EC=6.3.4.14 {ECO:0000269|PubMed:20952656};
Name=Acaca {ECO:0000312|MGI:MGI:108451};
Synonyms=Acac {ECO:0000312|EMBL:AAS13685.1}, Gm738;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1] {ECO:0000312|EMBL:AAS13685.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=C57BL/6J {ECO:0000312|EMBL:AAS13685.1};
TISSUE=Liver {ECO:0000312|EMBL:AAS13685.1};
Mao J., Wakil S.J.;
"Characterization of the mouse acetyl-CoA carboxylase 1 (ACC1) gene
and identification of an intronless pseudogene.";
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1-119 (ISOFORM 2).
STRAIN=SWR/J; TISSUE=Brain;
PubMed=15607423; DOI=10.1016/j.ygeno.2004.10.001;
Travers M.T., Cambot M., Kennedy H.T., Lenoir G.M., Barber M.C.,
Joulin V.;
"Asymmetric expression of transcripts derived from the shared promoter
between the divergently oriented ACACA and TADA2L genes.";
Genomics 85:71-84(2005).
[4] {ECO:0000305, ECO:0000312|EMBL:AAK57392.1}
NUCLEOTIDE SEQUENCE [MRNA] OF 1-38; 1221-1348 AND 1681-1891.
STRAIN=C57BL/6J {ECO:0000312|EMBL:AAK57392.1};
PubMed=12668174; DOI=10.1016/S1388-1981(03)00041-6;
Salles J., Sargueil F., Knoll-Gellida A., Witters L.A., Cassagne C.,
Garbay B.;
"Acetyl-CoA carboxylase and SREBP expression during peripheral nervous
system myelination.";
Biochim. Biophys. Acta 1631:229-238(2003).
[5] {ECO:0000305, ECO:0000312|EMBL:AAH56500.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1501-2345.
STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH56500.1};
TISSUE=Brain {ECO:0000312|EMBL:AAH56500.1};
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6] {ECO:0000305}
PROTEIN SEQUENCE OF 298-306 AND 2267-2275, INTERACTION WITH BRCA1, AND
SUBCELLULAR LOCATION.
PubMed=12360400; DOI=10.1038/sj.onc.1205915;
Magnard C., Bachelier R., Vincent A., Jaquinod M., Kieffer S.,
Lenoir G.M., Venezia N.D.;
"BRCA1 interacts with acetyl-CoA carboxylase through its tandem of
BRCT domains.";
Oncogene 21:6729-6739(2002).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17208939; DOI=10.1074/mcp.M600218-MCP200;
Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
"Mitochondrial phosphoproteome revealed by an improved IMAC method and
MS/MS/MS.";
Mol. Cell. Proteomics 6:669-676(2007).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25 AND SER-29, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29 AND SER-79, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=18630941; DOI=10.1021/pr800223m;
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
"Specific phosphopeptide enrichment with immobilized titanium ion
affinity chromatography adsorbent for phosphoproteome analysis.";
J. Proteome Res. 7:3957-3967(2008).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
"Large scale localization of protein phosphorylation by use of
electron capture dissociation mass spectrometry.";
Mol. Cell. Proteomics 8:904-912(2009).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-25; SER-29;
SER-47; THR-57; SER-79; THR-609; SER-1215; SER-1217; THR-1226;
SER-1258 AND SER-1262, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[12]
FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, ENZYME REGULATION, INTERACTION
WITH MID1IP1, PHOSPHORYLATION AT SER-79, AND SUBCELLULAR LOCATION.
PubMed=20952656; DOI=10.1073/pnas.1012736107;
Colbert C.L., Kim C.W., Moon Y.A., Henry L., Palnitkar M.,
McKean W.B., Fitzgerald K., Deisenhofer J., Horton J.D., Kwon H.J.;
"Crystal structure of Spot 14, a modulator of fatty acid synthesis.";
Proc. Natl. Acad. Sci. U.S.A. 107:18820-18825(2010).
[13]
INDUCTION BY ENDOCANNABINOID ANANDAMIDE.
PubMed=21987372; DOI=10.1002/hep.24733;
Jourdan T., Demizieux L., Gresti J., Djaouti L., Gaba L., Verges B.,
Degrace P.;
"Antagonism of peripheral hepatic cannabinoid receptor-1 improves
liver lipid metabolism in mice: evidence from cultured explants.";
Hepatology 55:790-799(2012).
-!- FUNCTION: Catalyzes the rate-limiting reaction in the biogenesis
of long-chain fatty acids. Carries out three functions: biotin
carboxyl carrier protein, biotin carboxylase and
carboxyltransferase. {ECO:0000250|UniProtKB:Q13085,
ECO:0000269|PubMed:20952656}.
-!- CATALYTIC ACTIVITY: ATP + acetyl-CoA + HCO(3)(-) = ADP + phosphate
+ malonyl-CoA. {ECO:0000269|PubMed:20952656}.
-!- CATALYTIC ACTIVITY: ATP + biotin-[carboxyl-carrier-protein] +
HCO(3)(-) = ADP + phosphate + carboxy-biotin-[carboxyl-carrier-
protein]. {ECO:0000269|PubMed:20952656}.
-!- COFACTOR:
Name=biotin; Xref=ChEBI:CHEBI:57586;
Evidence={ECO:0000250|UniProtKB:O00763};
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
Note=Binds 2 manganese ions per subunit. {ECO:0000250};
-!- ENZYME REGULATION: By phosphorylation (By similarity). Activity is
increased by oligomerization. Citrate and MID1IP1 promote
oligomerization. {ECO:0000250, ECO:0000269|PubMed:20952656}.
-!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA
from acetyl-CoA: step 1/1.
-!- SUBUNIT: Monomer, homodimer, and homotetramer. Can form
filamentous polymers. Interacts in its inactive phosphorylated
form with the BRCT domains of BRCA1 which prevents ACACA
dephosphorylation and inhibits lipid synthesis. Interacts with
MID1IP1; interaction with MID1IP1 promotes oligomerization and
increases its activity. {ECO:0000269|PubMed:12360400,
ECO:0000269|PubMed:20952656}.
-!- INTERACTION:
Q9CQ20:Mid1ip1; NbExp=2; IntAct=EBI-773043, EBI-473024;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12360400,
ECO:0000269|PubMed:20952656}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative promoter usage; Named isoforms=2;
Name=1;
IsoId=Q5SWU9-1; Sequence=Displayed;
Name=2;
IsoId=Q5SWU9-2; Sequence=VSP_026101;
-!- INDUCTION: Up-regulated by endocannabinoid anandamide/AEA.
{ECO:0000269|PubMed:21987372}.
-!- PTM: Phosphorylation on Ser-1262 is required for interaction with
BRCA1. {ECO:0000250|UniProtKB:Q13085}.
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EMBL; AY451393; AAS13685.1; -; mRNA.
EMBL; AL596252; CAI24019.1; -; Genomic_DNA.
EMBL; AL596447; CAI24019.1; JOINED; Genomic_DNA.
EMBL; AL596447; CAI25271.1; -; Genomic_DNA.
EMBL; AL596252; CAI25271.1; JOINED; Genomic_DNA.
EMBL; AL596447; CAI25272.1; -; Genomic_DNA.
EMBL; AL596447; CAI25273.1; -; Genomic_DNA.
EMBL; AL596447; CAI25274.1; -; Genomic_DNA.
EMBL; AL596447; CAM21560.1; -; Genomic_DNA.
EMBL; AJ619664; CAF02251.1; -; mRNA.
EMBL; AJ619665; CAF02252.1; -; Genomic_DNA.
EMBL; AF374167; AAK57389.1; -; mRNA.
EMBL; AF374168; AAK57390.1; -; mRNA.
EMBL; AF374169; AAK57391.1; -; mRNA.
EMBL; AF374170; AAK57392.1; -; mRNA.
EMBL; BC056500; AAH56500.1; -; mRNA.
CCDS; CCDS25185.1; -. [Q5SWU9-1]
RefSeq; NP_579938.2; NM_133360.2. [Q5SWU9-1]
RefSeq; XP_006532016.1; XM_006531953.1. [Q5SWU9-2]
RefSeq; XP_006532017.1; XM_006531954.2. [Q5SWU9-1]
RefSeq; XP_006532018.1; XM_006531955.1. [Q5SWU9-1]
RefSeq; XP_006532019.1; XM_006531956.2. [Q5SWU9-1]
RefSeq; XP_006532020.1; XM_006531957.3. [Q5SWU9-1]
RefSeq; XP_011246969.1; XM_011248667.1. [Q5SWU9-1]
UniGene; Mm.31374; -.
ProteinModelPortal; Q5SWU9; -.
SMR; Q5SWU9; -.
BioGrid; 223322; 4.
DIP; DIP-32276N; -.
IntAct; Q5SWU9; 12.
MINT; MINT-4091386; -.
STRING; 10090.ENSMUSP00000020843; -.
BindingDB; Q5SWU9; -.
ChEMBL; CHEMBL3086; -.
iPTMnet; Q5SWU9; -.
PhosphoSitePlus; Q5SWU9; -.
SwissPalm; Q5SWU9; -.
EPD; Q5SWU9; -.
PaxDb; Q5SWU9; -.
PeptideAtlas; Q5SWU9; -.
PRIDE; Q5SWU9; -.
Ensembl; ENSMUST00000020843; ENSMUSP00000020843; ENSMUSG00000020532. [Q5SWU9-1]
Ensembl; ENSMUST00000103201; ENSMUSP00000099490; ENSMUSG00000020532. [Q5SWU9-1]
GeneID; 107476; -.
KEGG; mmu:107476; -.
UCSC; uc007kql.1; mouse. [Q5SWU9-1]
CTD; 31; -.
MGI; MGI:108451; Acaca.
eggNOG; KOG0368; Eukaryota.
eggNOG; COG0439; LUCA.
eggNOG; COG0511; LUCA.
eggNOG; COG4799; LUCA.
GeneTree; ENSGT00550000074703; -.
HOVERGEN; HBG005371; -.
InParanoid; Q5SWU9; -.
KO; K11262; -.
OMA; FTPPCQR; -.
OrthoDB; EOG091G02ND; -.
PhylomeDB; Q5SWU9; -.
TreeFam; TF300061; -.
BRENDA; 6.4.1.2; 3474.
Reactome; R-MMU-163765; ChREBP activates metabolic gene expression.
Reactome; R-MMU-196780; Biotin transport and metabolism.
Reactome; R-MMU-200425; Import of palmitoyl-CoA into the mitochondrial matrix.
Reactome; R-MMU-75105; Fatty acyl-CoA biosynthesis.
UniPathway; UPA00655; UER00711.
PRO; PR:Q5SWU9; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000020532; -.
CleanEx; MM_ACACA; -.
ExpressionAtlas; Q5SWU9; baseline and differential.
Genevisible; Q5SWU9; MM.
GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0001650; C:fibrillar center; ISO:MGI.
GO; GO:0005739; C:mitochondrion; IDA:MGI.
GO; GO:0003989; F:acetyl-CoA carboxylase activity; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004075; F:biotin carboxylase activity; IEA:UniProtKB-EC.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006084; P:acetyl-CoA metabolic process; IDA:UniProtKB.
GO; GO:0071380; P:cellular response to prostaglandin E stimulus; IDA:MGI.
GO; GO:0006633; P:fatty acid biosynthetic process; IDA:UniProtKB.
GO; GO:0055088; P:lipid homeostasis; IMP:MGI.
GO; GO:0006629; P:lipid metabolic process; IMP:MGI.
GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0044268; P:multicellular organismal protein metabolic process; IMP:MGI.
GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
GO; GO:0001894; P:tissue homeostasis; IMP:MGI.
Gene3D; 3.30.1490.20; -; 1.
InterPro; IPR034733; AcCoA_carboxyl.
InterPro; IPR013537; AcCoA_COase_cen.
InterPro; IPR011761; ATP-grasp.
InterPro; IPR013815; ATP_grasp_subdomain_1.
InterPro; IPR005481; BC-like_N.
InterPro; IPR001882; Biotin_BS.
InterPro; IPR011764; Biotin_carboxylation_dom.
InterPro; IPR005482; Biotin_COase_C.
InterPro; IPR000089; Biotin_lipoyl.
InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
InterPro; IPR011763; COA_CT_C.
InterPro; IPR011762; COA_CT_N.
InterPro; IPR016185; PreATP-grasp_dom_sf.
InterPro; IPR011054; Rudment_hybrid_motif.
InterPro; IPR011053; Single_hybrid_motif.
Pfam; PF08326; ACC_central; 1.
Pfam; PF02785; Biotin_carb_C; 1.
Pfam; PF00289; Biotin_carb_N; 1.
Pfam; PF00364; Biotin_lipoyl; 1.
Pfam; PF01039; Carboxyl_trans; 1.
Pfam; PF02786; CPSase_L_D2; 1.
SMART; SM00878; Biotin_carb_C; 1.
SUPFAM; SSF51230; SSF51230; 1.
SUPFAM; SSF51246; SSF51246; 1.
SUPFAM; SSF52096; SSF52096; 2.
SUPFAM; SSF52440; SSF52440; 1.
PROSITE; PS50975; ATP_GRASP; 1.
PROSITE; PS50979; BC; 1.
PROSITE; PS00188; BIOTIN; 1.
PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
PROSITE; PS50989; COA_CT_CTER; 1.
PROSITE; PS50980; COA_CT_NTER; 1.
PROSITE; PS00866; CPSASE_1; 1.
PROSITE; PS00867; CPSASE_2; 1.
1: Evidence at protein level;
Acetylation; Allosteric enzyme; Alternative promoter usage;
ATP-binding; Biotin; Complete proteome; Cytoplasm;
Direct protein sequencing; Fatty acid biosynthesis;
Fatty acid metabolism; Ligase; Lipid biosynthesis; Lipid metabolism;
Manganese; Metal-binding; Multifunctional enzyme; Nucleotide-binding;
Phosphoprotein; Reference proteome.
CHAIN 1 2345 Acetyl-CoA carboxylase 1.
/FTId=PRO_0000258040.
DOMAIN 116 617 Biotin carboxylation. {ECO:0000255}.
DOMAIN 274 465 ATP-grasp. {ECO:0000255|PROSITE-
ProRule:PRU00409}.
DOMAIN 744 818 Biotinyl-binding. {ECO:0000255|PROSITE-
ProRule:PRU01066}.
DOMAIN 1575 1913 CoA carboxyltransferase N-terminal.
{ECO:0000255|PROSITE-ProRule:PRU01136}.
DOMAIN 1917 2233 CoA carboxyltransferase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU01137}.
NP_BIND 300 357 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00409}.
REGION 1575 2233 Carboxyltransferase.
{ECO:0000255|PROSITE-ProRule:PRU01138}.
ACT_SITE 440 440 {ECO:0000255}.
METAL 423 423 Manganese 1. {ECO:0000255}.
METAL 436 436 Manganese 1. {ECO:0000255}.
METAL 436 436 Manganese 2. {ECO:0000255}.
METAL 438 438 Manganese 2. {ECO:0000255}.
BINDING 1822 1822 Coenzyme A.
{ECO:0000250|UniProtKB:Q00955}.
BINDING 2126 2126 Coenzyme A.
{ECO:0000250|UniProtKB:Q00955}.
BINDING 2128 2128 Coenzyme A.
{ECO:0000250|UniProtKB:Q00955}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:Q13085}.
MOD_RES 5 5 Phosphoserine.
{ECO:0000250|UniProtKB:Q13085}.
MOD_RES 23 23 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 25 25 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 29 29 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:18630941,
ECO:0000244|PubMed:21183079}.
MOD_RES 34 34 Phosphoserine.
{ECO:0000250|UniProtKB:P11497}.
MOD_RES 47 47 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 49 49 Phosphoserine.
{ECO:0000250|UniProtKB:P11497}.
MOD_RES 52 52 Phosphoserine.
{ECO:0000250|UniProtKB:Q13085}.
MOD_RES 57 57 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 77 77 Phosphoserine.
{ECO:0000250|UniProtKB:P11497}.
MOD_RES 79 79 Phosphoserine.
{ECO:0000244|PubMed:17208939,
ECO:0000244|PubMed:18630941,
ECO:0000244|PubMed:19131326,
ECO:0000244|PubMed:21183079,
ECO:0000269|PubMed:20952656}.
MOD_RES 79 79 Phosphoserine; by AMPK.
{ECO:0000244|PubMed:17208939,
ECO:0000244|PubMed:18630941,
ECO:0000244|PubMed:19131326,
ECO:0000244|PubMed:21183079,
ECO:0000305|PubMed:20952656}.
MOD_RES 609 609 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 785 785 N6-biotinyllysine. {ECO:0000250,
ECO:0000255|PROSITE-ProRule:PRU01066}.
MOD_RES 834 834 Phosphoserine.
{ECO:0000250|UniProtKB:Q13085}.
MOD_RES 1200 1200 Phosphoserine.
{ECO:0000250|UniProtKB:P11497}.
MOD_RES 1215 1215 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1217 1217 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1226 1226 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1258 1258 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1262 1262 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1272 1272 Phosphoserine.
{ECO:0000250|UniProtKB:Q13085}.
MOD_RES 1333 1333 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q13085}.
MOD_RES 2152 2152 Phosphothreonine.
{ECO:0000250|UniProtKB:Q13085}.
VAR_SEQ 1 1 M -> MMWWSTLMSLLRASSFWRRISAETIRIIRALRAYFE
RIM (in isoform 2).
{ECO:0000303|PubMed:15607423}.
/FTId=VSP_026101.
CONFLICT 623 623 E -> G (in Ref. 1; AAS13685).
{ECO:0000305}.
CONFLICT 906 906 S -> P (in Ref. 1; AAS13685).
{ECO:0000305}.
CONFLICT 933 933 C -> Y (in Ref. 1; AAS13685).
{ECO:0000305}.
CONFLICT 1456 1456 L -> S (in Ref. 1; AAS13685).
{ECO:0000305}.
CONFLICT 1995 1995 S -> G (in Ref. 1; AAS13685).
{ECO:0000305}.
CONFLICT 2077 2077 V -> I (in Ref. 1; AAS13685).
{ECO:0000305}.
CONFLICT 2169 2169 E -> K (in Ref. 1; AAS13685).
{ECO:0000305}.
CONFLICT 2251 2251 F -> S (in Ref. 1; AAS13685).
{ECO:0000305}.
CONFLICT 2257 2257 T -> A (in Ref. 1; AAS13685).
{ECO:0000305}.
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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