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Acetyl-CoA carboxylase (ACC) (EC 6.4.1.2) (Fatty acid synthetase 3) (mRNA transport-defective protein 7) [Includes: Biotin carboxylase (EC 6.3.4.14)]

 ACAC_YEAST              Reviewed;        2233 AA.
Q00955; D6W1J1;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 2.
25-OCT-2017, entry version 190.
RecName: Full=Acetyl-CoA carboxylase;
Short=ACC;
EC=6.4.1.2 {ECO:0000269|PubMed:12663926, ECO:0000269|PubMed:15079078};
AltName: Full=Fatty acid synthetase 3;
AltName: Full=mRNA transport-defective protein 7;
Includes:
RecName: Full=Biotin carboxylase;
EC=6.3.4.14;
Name=ACC1; Synonyms=ABP2, FAS3, MTR7; OrderedLocusNames=YNR016C;
ORFNames=N3175;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2015-2022.
PubMed=1350093; DOI=10.1073/pnas.89.10.4534;
Al-Feel W., Chirala S.S., Wakil S.J.;
"Cloning of the yeast FAS3 gene and primary structure of yeast acetyl-
CoA carboxylase.";
Proc. Natl. Acad. Sci. U.S.A. 89:4534-4538(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169873;
Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F.,
Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M.,
Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N.,
Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D.,
Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A.,
Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A.,
Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C.,
Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M.,
Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J.,
Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L.,
Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M.,
Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P.,
Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A.,
Wambutt R., Wedler H., Zollner A., Hani J.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV
and its evolutionary implications.";
Nature 387:93-98(1997).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
FUNCTION.
PubMed=6108218;
Mishina M., Roggenkamp R., Schweizer E.;
"Yeast mutants defective in acetyl-coenzyme A carboxylase and biotin:
apocarboxylase ligase.";
Eur. J. Biochem. 111:79-87(1980).
[5]
FUNCTION.
PubMed=6103540; DOI=10.1073/pnas.77.4.1814;
Roggenkamp R., Numa S., Schweizer E.;
"Fatty acid-requiring mutant of Saccharomyces cerevisiae defective in
acetyl-CoA carboxylase.";
Proc. Natl. Acad. Sci. U.S.A. 77:1814-1817(1980).
[6]
INDUCTION.
PubMed=1359536; DOI=10.1073/pnas.89.21.10232;
Chirala S.S.;
"Coordinated regulation and inositol-mediated and fatty acid-mediated
repression of fatty acid synthase genes in Saccharomyces cerevisiae.";
Proc. Natl. Acad. Sci. U.S.A. 89:10232-10236(1992).
[7]
INDUCTION.
PubMed=8098706;
Hasslacher M., Ivessa A.S., Paltauf F., Kohlwein S.D.;
"Acetyl-CoA carboxylase from yeast is an essential enzyme and is
regulated by factors that control phospholipid metabolism.";
J. Biol. Chem. 268:10946-10952(1993).
[8]
ENZYME REGULATION.
PubMed=7916271; DOI=10.1007/BF00309532;
Vahlensieck H.F., Pridzun L., Reichenbach H., Hinnen A.;
"Identification of the yeast ACC1 gene product (acetyl-CoA
carboxylase) as the target of the polyketide fungicide soraphen A.";
Curr. Genet. 25:95-100(1994).
[9]
INDUCTION.
PubMed=8127678; DOI=10.1093/nar/22.3.412;
Chirala S.S., Zhong Q., Huang W., al-Feel W.;
"Analysis of FAS3/ACC regulatory region of Saccharomyces cerevisiae:
identification of a functional UASINO and sequences responsible for
fatty acid mediated repression.";
Nucleic Acids Res. 22:412-418(1994).
[10]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=8943372; DOI=10.1128/MCB.16.12.7161;
Schneiter R., Hitomi M., Ivessa A.S., Fasch E.V., Kohlwein S.D.,
Tartakoff A.M.;
"A yeast acetyl coenzyme A carboxylase mutant links very-long-chain
fatty acid synthesis to the structure and function of the nuclear
membrane-pore complex.";
Mol. Cell. Biol. 16:7161-7172(1996).
[11]
SUBCELLULAR LOCATION.
PubMed=9438137;
Ivessa A.S., Schneiter R., Kohlwein S.D.;
"Yeast acetyl-CoA carboxylase is associated with the cytoplasmic
surface of the endoplasmic reticulum.";
Eur. J. Cell Biol. 74:399-406(1997).
[12]
FUNCTION.
PubMed=10757783; DOI=10.1128/MCB.20.9.2984-2995.2000;
Schneiter R., Guerra C.E., Lampl M., Tatzer V., Zellnig G.,
Klein H.L., Kohlwein S.D.;
"A novel cold-sensitive allele of the rate-limiting enzyme of fatty
acid synthesis, acetyl coenzyme A carboxylase, affects the morphology
of the yeast vacuole through acylation of Vac8p.";
Mol. Cell. Biol. 20:2984-2995(2000).
[13]
FUNCTION.
PubMed=12730220; DOI=10.1074/jbc.M301607200;
Gao H., Sumanaweera N., Bailer S.M., Stochaj U.;
"Nuclear accumulation of the small GTPase Gsp1p depends on
nucleoporins Nup133p, Rat2p/Nup120p, Nup85p, Nic96p, and the acetyl-
CoA carboxylase Acc1p.";
J. Biol. Chem. 278:25331-25340(2003).
[14]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[15]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-2; SER-1148 AND SER-1157, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=YAL6B;
PubMed=15665377; DOI=10.1074/mcp.M400219-MCP200;
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,
Mann M., Jensen O.N.;
"Quantitative phosphoproteomics applied to the yeast pheromone
signaling pathway.";
Mol. Cell. Proteomics 4:310-327(2005).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1157, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1148 AND SER-1157, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-790; SER-1148; SER-1157
AND SER-1162, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
[19]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[20]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1429-2233 IN COMPLEX WITH
COA, CATALYTIC ACTIVITY AS ACETYL-COA CARBOXYLASE, MUTAGENESIS OF
LEU-1705; ARG-1731; TYR-1738; ARG-1954; GLU-1994; GLU-2026 AND
ARG-2036, AND HOMODIMERIZATION.
PubMed=12663926; DOI=10.1126/science.1081366;
Zhang H., Yang Z., Shen Y., Tong L.;
"Crystal structure of the carboxyltransferase domain of acetyl-
coenzyme A carboxylase.";
Science 299:2064-2067(2003).
[21]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 13-566 IN COMPLEX WITH
SORAPHEN, AND SUBUNIT.
PubMed=15610732; DOI=10.1016/j.molcel.2004.11.034;
Shen Y., Volrath S.L., Weatherly S.C., Elich T.D., Tong L.;
"A mechanism for the potent inhibition of eukaryotic acetyl-coenzyme A
carboxylase by soraphen A, a macrocyclic polyketide natural product.";
Mol. Cell 16:881-891(2004).
[22]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1482-2218 IN COMPLEXES WITH
THE INHIBITORS HALOXYFOP OR DICLOFOP, SUBUNIT, AND CATALYTIC ACTIVITY
AS ACETYL-COA CARBOXYLASE.
PubMed=15079078; DOI=10.1073/pnas.0400891101;
Zhang H., Tweel B., Tong L.;
"Molecular basis for the inhibition of the carboxyltransferase domain
of acetyl-coenzyme-A carboxylase by haloxyfop and diclofop.";
Proc. Natl. Acad. Sci. U.S.A. 101:5910-5915(2004).
-!- FUNCTION: Carries out three functions: biotin carboxyl carrier
protein, biotin carboxylase and carboxyltransferase. Involved in
the synthesis of very-long-chain fatty acid synthesis which is
required to maintain a functional nuclear envelope. Required for
acylation and vacuolar membrane association of VAC8 which is
necessary to maintain a normal morphology of the vacuole.
{ECO:0000269|PubMed:10757783, ECO:0000269|PubMed:12730220,
ECO:0000269|PubMed:6103540, ECO:0000269|PubMed:6108218,
ECO:0000269|PubMed:8943372}.
-!- CATALYTIC ACTIVITY: ATP + acetyl-CoA + HCO(3)(-) = ADP + phosphate
+ malonyl-CoA. {ECO:0000269|PubMed:12663926,
ECO:0000269|PubMed:15079078}.
-!- CATALYTIC ACTIVITY: ATP + biotin-[carboxyl-carrier-protein] +
HCO(3)(-) = ADP + phosphate + carboxy-biotin-[carboxyl-carrier-
protein]. {ECO:0000250|UniProtKB:Q5SWU9}.
-!- 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. The catalytic activity is
inhibited by soraphen A, a polyketide isolated from the
myxobacterium Sorangium cellulosum and a potent inhibitor of
fungal growth. {ECO:0000269|PubMed:7916271}.
-!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA
from acetyl-CoA: step 1/1.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12663926,
ECO:0000269|PubMed:15079078, ECO:0000269|PubMed:15610732}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-4814, EBI-4814;
-!- SUBCELLULAR LOCATION: Cytoplasm. Endoplasmic reticulum membrane;
Peripheral membrane protein; Cytoplasmic side.
-!- INDUCTION: Repressed in presence of fatty acids. Repressed 3-fold
by lipid precursors, inositol and choline, and also controlled by
regulatory factors INO2, INO4 and OPI1.
{ECO:0000269|PubMed:1359536, ECO:0000269|PubMed:8098706,
ECO:0000269|PubMed:8127678}.
-!- MISCELLANEOUS: Present with 20200 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
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EMBL; M92156; AAA20073.1; -; Genomic_DNA.
EMBL; Z71631; CAA96294.1; -; Genomic_DNA.
EMBL; BK006947; DAA10557.1; -; Genomic_DNA.
PIR; S63347; S63347.
RefSeq; NP_014413.1; NM_001183193.1.
PDB; 1OD2; X-ray; 2.70 A; A/B=1429-2233.
PDB; 1OD4; X-ray; 2.70 A; A/B/C=1429-2233.
PDB; 1UYR; X-ray; 2.50 A; A/B=1482-2218.
PDB; 1UYS; X-ray; 2.80 A; A/B/C=1482-2218.
PDB; 1UYT; X-ray; 2.50 A; A/B/C=1482-2218.
PDB; 1UYV; X-ray; 2.60 A; A/B/C=1482-2218.
PDB; 1W2X; X-ray; 2.80 A; A/B/C=1476-2233.
PDB; 1W93; X-ray; 2.50 A; A=14-566.
PDB; 1W96; X-ray; 1.80 A; A/B/C=13-566.
PDB; 3H0J; X-ray; 2.80 A; A/B/C=1476-2233.
PDB; 3H0Q; X-ray; 2.50 A; A/B/C=1476-2233.
PDB; 3H0S; X-ray; 2.43 A; A/B/C=1476-2233.
PDB; 3K8X; X-ray; 2.30 A; A/B/C=1476-2233.
PDB; 3PGQ; X-ray; 2.80 A; A/B/C=1476-2233.
PDB; 3TV5; X-ray; 2.80 A; A/B/C=1476-2233.
PDB; 3TVU; X-ray; 2.40 A; A/B/C=1476-2233.
PDB; 3TVW; X-ray; 2.80 A; A/B/C=1476-2233.
PDB; 3TZ3; X-ray; 2.70 A; A/B/C=1476-2233.
PDB; 4WYO; X-ray; 2.89 A; B/C=1476-2233.
PDB; 4WZ8; X-ray; 2.23 A; B/C=1476-2233.
PDB; 5CS0; X-ray; 2.50 A; A/B=797-1033.
PDB; 5CS4; X-ray; 3.19 A; A/B=1036-1503.
PDB; 5CSA; X-ray; 3.00 A; A/B=569-1494.
PDB; 5CSK; X-ray; 3.10 A; A/B=22-2233.
PDB; 5CSL; X-ray; 3.20 A; A/B=22-2233.
PDB; 5CTB; X-ray; 2.40 A; A/B/C=1476-2233.
PDB; 5CTC; X-ray; 2.70 A; A/B/C=1476-2233.
PDB; 5CTE; X-ray; 2.34 A; B/C=1476-2233.
PDB; 5I6E; X-ray; 3.00 A; A=768-1494.
PDB; 5TRC; X-ray; 2.90 A; A/B=1036-1503.
PDBsum; 1OD2; -.
PDBsum; 1OD4; -.
PDBsum; 1UYR; -.
PDBsum; 1UYS; -.
PDBsum; 1UYT; -.
PDBsum; 1UYV; -.
PDBsum; 1W2X; -.
PDBsum; 1W93; -.
PDBsum; 1W96; -.
PDBsum; 3H0J; -.
PDBsum; 3H0Q; -.
PDBsum; 3H0S; -.
PDBsum; 3K8X; -.
PDBsum; 3PGQ; -.
PDBsum; 3TV5; -.
PDBsum; 3TVU; -.
PDBsum; 3TVW; -.
PDBsum; 3TZ3; -.
PDBsum; 4WYO; -.
PDBsum; 4WZ8; -.
PDBsum; 5CS0; -.
PDBsum; 5CS4; -.
PDBsum; 5CSA; -.
PDBsum; 5CSK; -.
PDBsum; 5CSL; -.
PDBsum; 5CTB; -.
PDBsum; 5CTC; -.
PDBsum; 5CTE; -.
PDBsum; 5I6E; -.
PDBsum; 5TRC; -.
DisProt; DP00557; -.
ProteinModelPortal; Q00955; -.
SMR; Q00955; -.
BioGrid; 35841; 261.
DIP; DIP-975N; -.
IntAct; Q00955; 41.
MINT; MINT-636412; -.
STRING; 4932.YNR016C; -.
iPTMnet; Q00955; -.
MaxQB; Q00955; -.
PRIDE; Q00955; -.
EnsemblFungi; YNR016C; YNR016C; YNR016C.
GeneID; 855750; -.
KEGG; sce:YNR016C; -.
EuPathDB; FungiDB:YNR016C; -.
SGD; S000005299; ACC1.
GeneTree; ENSGT00550000074703; -.
HOGENOM; HOG000214115; -.
InParanoid; Q00955; -.
KO; K11262; -.
OMA; FTPPCQR; -.
OrthoDB; EOG092C00TE; -.
BioCyc; YEAST:MONOMER3O-7; -.
BRENDA; 6.3.4.14; 984.
BRENDA; 6.4.1.2; 984.
Reactome; R-SCE-163765; ChREBP activates metabolic gene expression.
Reactome; R-SCE-196780; Biotin transport and metabolism.
Reactome; R-SCE-200425; Import of palmitoyl-CoA into the mitochondrial matrix.
Reactome; R-SCE-75105; Fatty acyl-CoA biosynthesis.
UniPathway; UPA00655; UER00711.
EvolutionaryTrace; Q00955; -.
PRO; PR:Q00955; -.
Proteomes; UP000002311; Chromosome XIV.
GO; GO:0009317; C:acetyl-CoA carboxylase complex; IMP:CAFA.
GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:SGD.
GO; GO:1905502; F:acetyl-CoA binding; IMP:CAFA.
GO; GO:0003989; F:acetyl-CoA carboxylase activity; IMP:SGD.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004075; F:biotin carboxylase activity; IMP:SGD.
GO; GO:0016743; F:carboxyl- or carbamoyltransferase activity; IMP:CAFA.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0042803; F:protein homodimerization activity; IMP:CAFA.
GO; GO:0006085; P:acetyl-CoA biosynthetic process; IMP:CAFA.
GO; GO:0042759; P:long-chain fatty acid biosynthetic process; IMP:SGD.
GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0006998; P:nuclear envelope organization; TAS:SGD.
GO; GO:0006606; P:protein import into nucleus; IMP:SGD.
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.
InterPro; IPR011763; COA_CT_C.
InterPro; IPR011762; COA_CT_N.
InterPro; IPR016185; PreATP-grasp_dom.
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;
3D-structure; Acetylation; ATP-binding; Biotin; Complete proteome;
Cytoplasm; Direct protein sequencing; Endoplasmic reticulum;
Fatty acid biosynthesis; Fatty acid metabolism; Ligase;
Lipid biosynthesis; Lipid metabolism; Manganese; Membrane;
Metal-binding; Multifunctional enzyme; Nucleotide-binding;
Phosphoprotein; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:15665377,
ECO:0000244|PubMed:22814378}.
CHAIN 2 2233 Acetyl-CoA carboxylase.
/FTId=PRO_0000146770.
DOMAIN 58 567 Biotin carboxylation.
DOMAIN 216 408 ATP-grasp. {ECO:0000255|PROSITE-
ProRule:PRU00409}.
DOMAIN 694 768 Biotinyl-binding. {ECO:0000255|PROSITE-
ProRule:PRU01066}.
DOMAIN 1486 1822 CoA carboxyltransferase N-terminal.
{ECO:0000255|PROSITE-ProRule:PRU01136}.
DOMAIN 1826 2141 CoA carboxyltransferase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU01137}.
NP_BIND 256 261 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00409}.
REGION 1486 2141 Carboxyltransferase.
{ECO:0000255|PROSITE-ProRule:PRU01138}.
REGION 1627 1629 Acetyl-CoA binding.
ACT_SITE 383 383 {ECO:0000250}.
METAL 365 365 Manganese 1. {ECO:0000250}.
METAL 379 379 Manganese 1. {ECO:0000250}.
METAL 379 379 Manganese 2. {ECO:0000250}.
METAL 381 381 Manganese 2. {ECO:0000250}.
BINDING 1731 1731 Coenzyme A.
BINDING 1998 1998 Acetyl-CoA; via amide nitrogen.
BINDING 2034 2034 Coenzyme A.
BINDING 2036 2036 Coenzyme A.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:15665377,
ECO:0000244|PubMed:22814378}.
MOD_RES 2 2 Phosphoserine.
{ECO:0000244|PubMed:15665377}.
MOD_RES 735 735 N6-biotinyllysine. {ECO:0000250,
ECO:0000255|PROSITE-ProRule:PRU01066}.
MOD_RES 790 790 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 1148 1148 Phosphoserine.
{ECO:0000244|PubMed:15665377,
ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
MOD_RES 1157 1157 Phosphoserine.
{ECO:0000244|PubMed:15665377,
ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
MOD_RES 1162 1162 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MUTAGEN 1705 1705 L->I: Raises KM for malonyl-CoA by a
factor of 20.
{ECO:0000269|PubMed:12663926}.
MUTAGEN 1731 1731 R->S: Raises KM for malonyl-CoA by a
factor of 15.
{ECO:0000269|PubMed:12663926}.
MUTAGEN 1738 1738 Y->F: Does not affect catalytic activity.
{ECO:0000269|PubMed:12663926}.
MUTAGEN 1954 1954 R->S: Raises KM for malonyl-CoA by a
factor of 70.
{ECO:0000269|PubMed:12663926}.
MUTAGEN 1994 1994 E->Q: Does not affect catalytic activity.
{ECO:0000269|PubMed:12663926}.
MUTAGEN 2026 2026 E->Q: Does not affect catalytic activity.
{ECO:0000269|PubMed:12663926}.
MUTAGEN 2036 2036 R->E: Affects only slightly binding of
Co-A. {ECO:0000269|PubMed:12663926}.
CONFLICT 1523 1523 W -> G (in Ref. 1; AAA20073).
{ECO:0000305}.
CONFLICT 1755 1755 I -> IWYRCL (in Ref. 1; AAA20073).
{ECO:0000305}.
CONFLICT 1761 1766 AINKML -> ESTNA (in Ref. 1; AAA20073).
{ECO:0000305}.
HELIX 22 27 {ECO:0000244|PDB:1W96}.
HELIX 30 32 {ECO:0000244|PDB:1W96}.
STRAND 35 37 {ECO:0000244|PDB:1W96}.
HELIX 38 40 {ECO:0000244|PDB:1W96}.
HELIX 45 52 {ECO:0000244|PDB:1W96}.
STRAND 61 64 {ECO:0000244|PDB:1W96}.
HELIX 68 86 {ECO:0000244|PDB:1W96}.
STRAND 91 98 {ECO:0000244|PDB:1W96}.
HELIX 100 104 {ECO:0000244|PDB:1W96}.
HELIX 108 112 {ECO:0000244|PDB:1W96}.
STRAND 113 118 {ECO:0000244|PDB:1W96}.
HELIX 124 126 {ECO:0000244|PDB:1W96}.
TURN 127 129 {ECO:0000244|PDB:1W96}.
HELIX 131 140 {ECO:0000244|PDB:1W96}.
STRAND 144 147 {ECO:0000244|PDB:1W96}.
TURN 152 155 {ECO:0000244|PDB:1W96}.
HELIX 158 165 {ECO:0000244|PDB:1W96}.
STRAND 171 174 {ECO:0000244|PDB:1W96}.
HELIX 177 182 {ECO:0000244|PDB:1W96}.
HELIX 186 195 {ECO:0000244|PDB:1W96}.
TURN 204 207 {ECO:0000244|PDB:1W96}.
TURN 215 217 {ECO:0000244|PDB:1W96}.
HELIX 224 227 {ECO:0000244|PDB:1W96}.
HELIX 228 230 {ECO:0000244|PDB:1W96}.
HELIX 235 245 {ECO:0000244|PDB:1W96}.
STRAND 247 253 {ECO:0000244|PDB:1W96}.
TURN 258 261 {ECO:0000244|PDB:1W96}.
STRAND 262 265 {ECO:0000244|PDB:1W96}.
HELIX 268 281 {ECO:0000244|PDB:1W96}.
STRAND 287 291 {ECO:0000244|PDB:1W96}.
STRAND 297 305 {ECO:0000244|PDB:1W96}.
TURN 307 309 {ECO:0000244|PDB:1W93}.
STRAND 311 323 {ECO:0000244|PDB:1W96}.
STRAND 326 333 {ECO:0000244|PDB:1W96}.
HELIX 339 356 {ECO:0000244|PDB:1W96}.
STRAND 360 368 {ECO:0000244|PDB:1W96}.
TURN 370 372 {ECO:0000244|PDB:1W96}.
STRAND 375 381 {ECO:0000244|PDB:1W96}.
HELIX 388 395 {ECO:0000244|PDB:1W96}.
HELIX 399 407 {ECO:0000244|PDB:1W96}.
HELIX 412 414 {ECO:0000244|PDB:1W96}.
HELIX 416 421 {ECO:0000244|PDB:1W96}.
HELIX 439 444 {ECO:0000244|PDB:1W96}.
STRAND 452 462 {ECO:0000244|PDB:1W96}.
STRAND 466 468 {ECO:0000244|PDB:1W93}.
STRAND 472 478 {ECO:0000244|PDB:1W96}.
STRAND 484 492 {ECO:0000244|PDB:1W96}.
STRAND 503 515 {ECO:0000244|PDB:1W96}.
HELIX 516 530 {ECO:0000244|PDB:1W96}.
STRAND 531 536 {ECO:0000244|PDB:5CSK}.
HELIX 541 547 {ECO:0000244|PDB:1W96}.
HELIX 550 553 {ECO:0000244|PDB:1W96}.
HELIX 561 565 {ECO:0000244|PDB:1W96}.
HELIX 577 605 {ECO:0000244|PDB:5CSA}.
HELIX 612 615 {ECO:0000244|PDB:5CSA}.
STRAND 618 624 {ECO:0000244|PDB:5CSA}.
STRAND 626 636 {ECO:0000244|PDB:5CSA}.
STRAND 638 648 {ECO:0000244|PDB:5CSA}.
STRAND 650 657 {ECO:0000244|PDB:5CSA}.
STRAND 659 661 {ECO:0000244|PDB:5CSA}.
STRAND 663 669 {ECO:0000244|PDB:5CSA}.
STRAND 671 675 {ECO:0000244|PDB:5CSA}.
STRAND 682 687 {ECO:0000244|PDB:5CSA}.
STRAND 690 695 {ECO:0000244|PDB:5CSA}.
STRAND 702 704 {ECO:0000244|PDB:5CSA}.
STRAND 709 716 {ECO:0000244|PDB:5CSA}.
STRAND 727 733 {ECO:0000244|PDB:5CSA}.
STRAND 736 741 {ECO:0000244|PDB:5CSA}.
STRAND 746 750 {ECO:0000244|PDB:5CSA}.
STRAND 763 767 {ECO:0000244|PDB:5CSA}.
HELIX 772 774 {ECO:0000244|PDB:5CSA}.
STRAND 793 795 {ECO:0000244|PDB:5I6E}.
HELIX 798 813 {ECO:0000244|PDB:5CS0}.
HELIX 818 833 {ECO:0000244|PDB:5CS0}.
HELIX 838 850 {ECO:0000244|PDB:5CS0}.
HELIX 851 853 {ECO:0000244|PDB:5CS0}.
HELIX 856 871 {ECO:0000244|PDB:5CS0}.
HELIX 878 889 {ECO:0000244|PDB:5CS0}.
TURN 892 894 {ECO:0000244|PDB:5CS0}.
STRAND 896 898 {ECO:0000244|PDB:5CS0}.
HELIX 900 913 {ECO:0000244|PDB:5CS0}.
TURN 914 916 {ECO:0000244|PDB:5CS0}.
HELIX 918 937 {ECO:0000244|PDB:5CS0}.
HELIX 938 940 {ECO:0000244|PDB:5CSA}.
STRAND 942 944 {ECO:0000244|PDB:5CSL}.
HELIX 947 957 {ECO:0000244|PDB:5CSA}.
HELIX 962 972 {ECO:0000244|PDB:5CS0}.
HELIX 975 995 {ECO:0000244|PDB:5CS0}.
HELIX 997 1002 {ECO:0000244|PDB:5CS0}.
HELIX 1004 1011 {ECO:0000244|PDB:5CS0}.
HELIX 1016 1018 {ECO:0000244|PDB:5CS0}.
HELIX 1019 1030 {ECO:0000244|PDB:5CS0}.
HELIX 1037 1052 {ECO:0000244|PDB:5TRC}.
STRAND 1054 1056 {ECO:0000244|PDB:5CSA}.
STRAND 1057 1059 {ECO:0000244|PDB:5TRC}.
STRAND 1062 1066 {ECO:0000244|PDB:5CSA}.
HELIX 1069 1076 {ECO:0000244|PDB:5TRC}.
HELIX 1083 1086 {ECO:0000244|PDB:5TRC}.
HELIX 1087 1090 {ECO:0000244|PDB:5TRC}.
TURN 1095 1097 {ECO:0000244|PDB:5TRC}.
HELIX 1098 1109 {ECO:0000244|PDB:5TRC}.
TURN 1110 1112 {ECO:0000244|PDB:5TRC}.
STRAND 1113 1122 {ECO:0000244|PDB:5TRC}.
STRAND 1124 1134 {ECO:0000244|PDB:5TRC}.
HELIX 1138 1140 {ECO:0000244|PDB:5I6E}.
STRAND 1155 1157 {ECO:0000244|PDB:5CSL}.
HELIX 1158 1160 {ECO:0000244|PDB:5CSL}.
STRAND 1167 1170 {ECO:0000244|PDB:5I6E}.
STRAND 1173 1178 {ECO:0000244|PDB:5TRC}.
HELIX 1183 1185 {ECO:0000244|PDB:5TRC}.
HELIX 1186 1194 {ECO:0000244|PDB:5TRC}.
STRAND 1220 1225 {ECO:0000244|PDB:5TRC}.
HELIX 1235 1255 {ECO:0000244|PDB:5TRC}.
STRAND 1258 1265 {ECO:0000244|PDB:5TRC}.
STRAND 1268 1270 {ECO:0000244|PDB:5TRC}.
STRAND 1274 1279 {ECO:0000244|PDB:5TRC}.
TURN 1280 1283 {ECO:0000244|PDB:5TRC}.
HELIX 1287 1289 {ECO:0000244|PDB:5TRC}.
HELIX 1294 1300 {ECO:0000244|PDB:5TRC}.
HELIX 1303 1305 {ECO:0000244|PDB:5TRC}.
STRAND 1308 1313 {ECO:0000244|PDB:5TRC}.
STRAND 1320 1327 {ECO:0000244|PDB:5TRC}.
STRAND 1334 1342 {ECO:0000244|PDB:5TRC}.
STRAND 1349 1351 {ECO:0000244|PDB:5TRC}.
HELIX 1353 1372 {ECO:0000244|PDB:5TRC}.
STRAND 1378 1380 {ECO:0000244|PDB:5I6E}.
STRAND 1382 1389 {ECO:0000244|PDB:5TRC}.
HELIX 1397 1403 {ECO:0000244|PDB:5TRC}.
TURN 1404 1408 {ECO:0000244|PDB:5TRC}.
HELIX 1409 1411 {ECO:0000244|PDB:5TRC}.
HELIX 1412 1418 {ECO:0000244|PDB:5TRC}.
STRAND 1420 1430 {ECO:0000244|PDB:5TRC}.
TURN 1432 1434 {ECO:0000244|PDB:5TRC}.
STRAND 1437 1445 {ECO:0000244|PDB:5TRC}.
STRAND 1447 1450 {ECO:0000244|PDB:5I6E}.
STRAND 1453 1461 {ECO:0000244|PDB:5TRC}.
STRAND 1463 1465 {ECO:0000244|PDB:5TRC}.
STRAND 1467 1474 {ECO:0000244|PDB:5TRC}.
TURN 1477 1480 {ECO:0000244|PDB:5TRC}.
STRAND 1482 1484 {ECO:0000244|PDB:4WZ8}.
HELIX 1490 1493 {ECO:0000244|PDB:4WZ8}.
HELIX 1495 1502 {ECO:0000244|PDB:4WZ8}.
HELIX 1508 1510 {ECO:0000244|PDB:4WZ8}.
HELIX 1511 1526 {ECO:0000244|PDB:4WZ8}.
HELIX 1534 1536 {ECO:0000244|PDB:4WZ8}.
STRAND 1537 1544 {ECO:0000244|PDB:4WZ8}.
STRAND 1546 1548 {ECO:0000244|PDB:1OD2}.
STRAND 1550 1553 {ECO:0000244|PDB:4WZ8}.
STRAND 1561 1571 {ECO:0000244|PDB:4WZ8}.
STRAND 1580 1587 {ECO:0000244|PDB:4WZ8}.
HELIX 1592 1594 {ECO:0000244|PDB:4WZ8}.
HELIX 1598 1614 {ECO:0000244|PDB:4WZ8}.
STRAND 1618 1622 {ECO:0000244|PDB:4WZ8}.
TURN 1633 1638 {ECO:0000244|PDB:4WZ8}.
STRAND 1640 1645 {ECO:0000244|PDB:4WZ8}.
HELIX 1649 1651 {ECO:0000244|PDB:4WZ8}.
STRAND 1653 1658 {ECO:0000244|PDB:4WZ8}.
HELIX 1660 1668 {ECO:0000244|PDB:4WZ8}.
HELIX 1672 1674 {ECO:0000244|PDB:4WZ8}.
STRAND 1675 1682 {ECO:0000244|PDB:4WZ8}.
STRAND 1685 1693 {ECO:0000244|PDB:4WZ8}.
STRAND 1696 1698 {ECO:0000244|PDB:4WZ8}.
HELIX 1702 1719 {ECO:0000244|PDB:4WZ8}.
STRAND 1724 1728 {ECO:0000244|PDB:4WZ8}.
HELIX 1735 1742 {ECO:0000244|PDB:4WZ8}.
STRAND 1745 1749 {ECO:0000244|PDB:4WZ8}.
STRAND 1754 1757 {ECO:0000244|PDB:4WZ8}.
HELIX 1759 1766 {ECO:0000244|PDB:4WZ8}.
HELIX 1775 1778 {ECO:0000244|PDB:4WZ8}.
HELIX 1780 1783 {ECO:0000244|PDB:4WZ8}.
TURN 1784 1787 {ECO:0000244|PDB:4WZ8}.
STRAND 1788 1795 {ECO:0000244|PDB:4WZ8}.
HELIX 1796 1807 {ECO:0000244|PDB:4WZ8}.
STRAND 1812 1816 {ECO:0000244|PDB:5CSK}.
STRAND 1827 1829 {ECO:0000244|PDB:5CTE}.
STRAND 1837 1839 {ECO:0000244|PDB:3K8X}.
HELIX 1843 1848 {ECO:0000244|PDB:4WZ8}.
STRAND 1850 1852 {ECO:0000244|PDB:4WZ8}.
STRAND 1855 1857 {ECO:0000244|PDB:4WZ8}.
STRAND 1867 1870 {ECO:0000244|PDB:4WZ8}.
STRAND 1877 1884 {ECO:0000244|PDB:4WZ8}.
STRAND 1887 1894 {ECO:0000244|PDB:4WZ8}.
STRAND 1899 1903 {ECO:0000244|PDB:4WZ8}.
STRAND 1909 1911 {ECO:0000244|PDB:1OD4}.
STRAND 1915 1919 {ECO:0000244|PDB:4WZ8}.
HELIX 1926 1940 {ECO:0000244|PDB:4WZ8}.
TURN 1941 1943 {ECO:0000244|PDB:4WZ8}.
STRAND 1947 1950 {ECO:0000244|PDB:4WZ8}.
STRAND 1953 1956 {ECO:0000244|PDB:5CTE}.
HELIX 1960 1964 {ECO:0000244|PDB:4WZ8}.
HELIX 1967 1979 {ECO:0000244|PDB:4WZ8}.
STRAND 1985 1989 {ECO:0000244|PDB:4WZ8}.
STRAND 1994 1996 {ECO:0000244|PDB:3K8X}.
HELIX 1997 2000 {ECO:0000244|PDB:4WZ8}.
TURN 2001 2003 {ECO:0000244|PDB:4WZ8}.
HELIX 2005 2008 {ECO:0000244|PDB:4WZ8}.
TURN 2009 2011 {ECO:0000244|PDB:4WZ8}.
STRAND 2012 2017 {ECO:0000244|PDB:4WZ8}.
STRAND 2021 2025 {ECO:0000244|PDB:3K8X}.
HELIX 2027 2034 {ECO:0000244|PDB:4WZ8}.
HELIX 2039 2047 {ECO:0000244|PDB:4WZ8}.
HELIX 2049 2058 {ECO:0000244|PDB:4WZ8}.
HELIX 2059 2063 {ECO:0000244|PDB:5CTB}.
HELIX 2065 2072 {ECO:0000244|PDB:4WZ8}.
HELIX 2078 2095 {ECO:0000244|PDB:4WZ8}.
HELIX 2100 2106 {ECO:0000244|PDB:4WZ8}.
STRAND 2108 2113 {ECO:0000244|PDB:4WZ8}.
HELIX 2115 2117 {ECO:0000244|PDB:4WZ8}.
HELIX 2118 2139 {ECO:0000244|PDB:4WZ8}.
STRAND 2142 2144 {ECO:0000244|PDB:4WZ8}.
HELIX 2148 2157 {ECO:0000244|PDB:4WZ8}.
HELIX 2168 2186 {ECO:0000244|PDB:4WZ8}.
TURN 2189 2191 {ECO:0000244|PDB:3TVU}.
TURN 2196 2199 {ECO:0000244|PDB:1UYV}.
TURN 2203 2205 {ECO:0000244|PDB:1UYR}.
HELIX 2206 2215 {ECO:0000244|PDB:5CTE}.
HELIX 2223 2233 {ECO:0000244|PDB:5CTE}.
SEQUENCE 2233 AA; 250353 MW; 0A335AAD9B1F8308 CRC64;
MSEESLFESS PQKMEYEITN YSERHTELPG HFIGLNTVDK LEESPLRDFV KSHGGHTVIS
KILIANNGIA AVKEIRSVRK WAYETFGDDR TVQFVAMATP EDLEANAEYI RMADQYIEVP
GGTNNNNYAN VDLIVDIAER ADVDAVWAGW GHASENPLLP EKLSQSKRKV IFIGPPGNAM
RSLGDKISST IVAQSAKVPC IPWSGTGVDT VHVDEKTGLV SVDDDIYQKG CCTSPEDGLQ
KAKRIGFPVM IKASEGGGGK GIRQVEREED FIALYHQAAN EIPGSPIFIM KLAGRARHLE
VQLLADQYGT NISLFGRDCS VQRRHQKIIE EAPVTIAKAE TFHEMEKAAV RLGKLVGYVS
AGTVEYLYSH DDGKFYFLEL NPRLQVEHPT TEMVSGVNLP AAQLQIAMGI PMHRISDIRT
LYGMNPHSAS EIDFEFKTQD ATKKQRRPIP KGHCTACRIT SEDPNDGFKP SGGTLHELNF
RSSSNVWGYF SVGNNGNIHS FSDSQFGHIF AFGENRQASR KHMVVALKEL SIRGDFRTTV
EYLIKLLETE DFEDNTITTG WLDDLITHKM TAEKPDPTLA VICGAATKAF LASEEARHKY
IESLQKGQVL SKDLLQTMFP VDFIHEGKRY KFTVAKSGND RYTLFINGSK CDIILRQLSD
GGLLIAIGGK SHTIYWKEEV AATRLSVDSM TTLLEVENDP TQLRTPSPGK LVKFLVENGE
HIIKGQPYAE IEVMKMQMPL VSQENGIVQL LKQPGSTIVA GDIMAIMTLD DPSKVKHALP
FEGMLPDFGS PVIEGTKPAY KFKSLVSTLE NILKGYDNQV IMNASLQQLI EVLRNPKLPY
SEWKLHISAL HSRLPAKLDE QMEELVARSL RRGAVFPARQ LSKLIDMAVK NPEYNPDKLL
GAVVEPLADI AHKYSNGLEA HEHSIFVHFL EEYYEVEKLF NGPNVREENI ILKLRDENPK
DLDKVALTVL SHSKVSAKNN LILAILKHYQ PLCKLSSKVS AIFSTPLQHI VELESKATAK
VALQAREILI QGALPSVKER TEQIEHILKS SVVKVAYGSS NPKRSEPDLN ILKDLIDSNY
VVFDVLLQFL THQDPVVTAA AAQVYIRRAY RAYTIGDIRV HEGVTVPIVE WKFQLPSAAF
STFPTVKSKM GMNRAVSVSD LSYVANSQSS PLREGILMAV DHLDDVDEIL SQSLEVIPRH
QSSSNGPAPD RSGSSASLSN VANVCVASTE GFESEEEILV RLREILDLNK QELINASIRR
ITFMFGFKDG SYPKYYTFNG PNYNENETIR HIEPALAFQL ELGRLSNFNI KPIFTDNRNI
HVYEAVSKTS PLDKRFFTRG IIRTGHIRDD ISIQEYLTSE ANRLMSDILD NLEVTDTSNS
DLNHIFINFI AVFDISPEDV EAAFGGFLER FGKRLLRLRV SSAEIRIIIK DPQTGAPVPL
RALINNVSGY VIKTEMYTEV KNAKGEWVFK SLGKPGSMHL RPIATPYPVK EWLQPKRYKA
HLMGTTYVYD FPELFRQASS SQWKNFSADV KLTDDFFISN ELIEDENGEL TEVEREPGAN
AIGMVAFKIT VKTPEYPRGR QFVVVANDIT FKIGSFGPQE DEFFNKVTEY ARKRGIPRIY
LAANSGARIG MAEEIVPLFQ VAWNDAANPD KGFQYLYLTS EGMETLKKFD KENSVLTERT
VINGEERFVI KTIIGSEDGL GVECLRGSGL IAGATSRAYH DIFTITLVTC RSVGIGAYLV
RLGQRAIQVE GQPIILTGAP AINKMLGREV YTSNLQLGGT QIMYNNGVSH LTAVDDLAGV
EKIVEWMSYV PAKRNMPVPI LETKDTWDRP VDFTPTNDET YDVRWMIEGR ETESGFEYGL
FDKGSFFETL SGWAKGVVVG RARLGGIPLG VIGVETRTVE NLIPADPANP NSAETLIQEP
GQVWHPNSAF KTAQAINDFN NGEQLPMMIL ANWRGFSGGQ RDMFNEVLKY GSFIVDALVD
YKQPIIIYIP PTGELRGGSW VVVDPTINAD QMEMYADVNA RAGVLEPQGM VGIKFRREKL
LDTMNRLDDK YRELRSQLSN KSLAPEVHQQ ISKQLADRER ELLPIYGQIS LQFADLHDRS
SRMVAKGVIS KELEWTEARR FFFWRLRRRL NEEYLIKRLS HQVGEASRLE KIARIRSWYP
ASVDHEDDRQ VATWIEENYK TLDDKLKGLK LESFAQDLAK KIRSDHDNAI DGLSEVIKML
STDDKEKLLK TLK


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