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Database: UniProt
Entry: Q13085
LinkDB: Q13085
Original site: Q13085 
ID   ACACA_HUMAN             Reviewed;        2346 AA.
AC   Q13085; B2RP68; B2ZZ90; Q6KEV6; Q6XDA8; Q7Z2G8; Q7Z561; Q7Z563;
AC   Q7Z564; Q86WB2; Q86WB3;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 2.
DT   10-APR-2019, entry version 196.
DE   RecName: Full=Acetyl-CoA carboxylase 1;
DE            Short=ACC1;
DE            EC=6.4.1.2 {ECO:0000269|PubMed:20952656};
DE   AltName: Full=Acetyl-Coenzyme A carboxylase alpha;
DE            Short=ACC-alpha;
DE   Includes:
DE     RecName: Full=Biotin carboxylase;
DE              EC=6.3.4.14 {ECO:0000269|PubMed:20952656};
GN   Name=ACACA; Synonyms=ACAC, ACC1, ACCA;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Liver;
RX   PubMed=7732023; DOI=10.1073/pnas.92.9.4011;
RA   Abu-Elheiga L., Jayakumar A., Baldini A., Chirala S.S., Wakil S.J.;
RT   "Human acetyl-CoA carboxylase: characterization, molecular cloning,
RT   and evidence for two isoforms.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:4011-4015(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF
RP   1-366 (ISOFORMS 2 AND 3), AND NUCLEOTIDE SEQUENCE [MRNA] OF 1-120
RP   (ISOFORM 4).
RC   TISSUE=Adipocyte;
RX   PubMed=12810950; DOI=10.1073/pnas.1332670100;
RA   Mao J., Chirala S.S., Wakil S.J.;
RT   "Human acetyl-CoA carboxylase 1 gene: presence of three promoters and
RT   heterogeneity at the 5'-untranslated mRNA region.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7515-7520(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT VAL-2271.
RX   PubMed=15333468; DOI=10.1093/carcin/bgh273;
RA   Sinilnikova O.M., Ginolhac S.M., Magnard C., Leone M., Anczukow O.,
RA   Hughes D., Moreau K., Thompson D., Coutanson C., Hall J.,
RA   Romestaing P., Gerard J.-P., Bonadona V., Lasset C., Goldgar D.E.,
RA   Joulin V., Venezia N.D., Lenoir G.M.;
RT   "Acetyl-CoA carboxylase alpha gene and breast cancer susceptibility.";
RL   Carcinogenesis 25:2417-2424(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=18487259; DOI=10.1093/dnares/dsn010;
RA   Oshikawa M., Sugai Y., Usami R., Ohtoko K., Toyama S., Kato S.;
RT   "Fine expression profiling of full-length transcripts using a size-
RT   unbiased cDNA library prepared with the vector-capping method.";
RL   DNA Res. 15:123-136(2008).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-113 (ISOFORM 2), AND NUCLEOTIDE
RP   SEQUENCE [MRNA] OF 1-93 (ISOFORM 3).
RC   TISSUE=Mammary gland, and Testis;
RX   PubMed=14643797; DOI=10.1016/j.bbalip.2003.09.005;
RA   Travers M.T., Vallance A.J., Clegg R.A., Thomson R., Price N.T.,
RA   Barber M.C.;
RT   "Characterisation of an N-terminal variant of acetyl-CoA carboxylase-
RT   alpha: expression in human tissues and evolutionary aspects.";
RL   Biochim. Biophys. Acta 1634:97-106(2003).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-47 (ISOFORM 1).
RC   TISSUE=Testis;
RX   PubMed=15607423; DOI=10.1016/j.ygeno.2004.10.001;
RA   Travers M.T., Cambot M., Kennedy H.T., Lenoir G.M., Barber M.C.,
RA   Joulin V.;
RT   "Asymmetric expression of transcripts derived from the shared promoter
RT   between the divergently oriented ACACA and TADA2L genes.";
RL   Genomics 85:71-84(2005).
RN   [9]
RP   PROTEIN SEQUENCE OF 1-18; 39-45; 77-86; 99-111; 121-132; 153-170;
RP   218-224; 267-276; 278-288; 323-335; 568-579; 589-615; 646-657;
RP   748-755; 818-838; 985-992; 997-1008; 1083-1096; 1147-1169; 1192-1199;
RP   1233-1247; 1283-1294; 1317-1325; 1327-1334; 1372-1385; 1401-1420;
RP   1508-1514; 1553-1564; 1668-1687; 1714-1731; 1750-1759; 1782-1798;
RP   1824-1833; 1838-1856; 1905-1916; 1922-1929; 1978-2009; 2063-2072;
RP   2104-2111; 2115-2127; 2139-2161; 2200-2209; 2213-2218; 2221-2229 AND
RP   2261-2293, ACETYLATION AT MET-1, PHOSPHORYLATION AT SER-80, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Hepatoma;
RA   Bienvenut W.V., Boldt K., von Kriegsheim A.F., Kolch W.;
RL   Submitted (JUL-2007) to UniProtKB.
RN   [10]
RP   INTERACTION WITH BRCA1.
RX   PubMed=12360400; DOI=10.1038/sj.onc.1205915;
RA   Magnard C., Bachelier R., Vincent A., Jaquinod M., Kieffer S.,
RA   Lenoir G.M., Venezia N.D.;
RT   "BRCA1 interacts with acetyl-CoA carboxylase through its tandem of
RT   BRCT domains.";
RL   Oncogene 21:6729-6739(2002).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29 AND SER-53, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA   Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in
RT   signaling networks.";
RL   Cell 127:635-648(2006).
RN   [12]
RP   INTERACTION WITH BRCA1.
RX   PubMed=16326698; DOI=10.1074/jbc.M504652200;
RA   Moreau K., Dizin E., Ray H., Luquain C., Lefai E., Foufelle F.,
RA   Billaud M., Lenoir G.M., Venezia N.D.;
RT   "BRCA1 affects lipid synthesis through its interaction with acetyl-CoA
RT   carboxylase.";
RL   J. Biol. Chem. 281:3172-3181(2006).
RN   [13]
RP   PHOSPHORYLATION AT SER-1263, AND MUTAGENESIS OF SER-78; SER-344;
RP   SER-432; SER-1201; SER-1263; SER-1585; SER-1952 AND SER-2211.
RX   PubMed=16698035; DOI=10.1016/j.jmb.2006.04.010;
RA   Ray H., Moreau K., Dizin E., Callebaut I., Venezia N.D.;
RT   "ACCA phosphopeptide recognition by the BRCT repeats of BRCA1.";
RL   J. Mol. Biol. 359:973-982(2006).
RN   [14]
RP   INVOLVEMENT IN ACACAD.
RX   PubMed=6114432;
RA   Blom W., de Muinck Keizer S.M.P.F., Scholte H.R.;
RT   "Acetyl-CoA carboxylase deficiency: an inborn error of de novo fatty
RT   acid synthesis.";
RL   N. Engl. J. Med. 305:465-466(1981).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-488, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18220336; DOI=10.1021/pr0705441;
RA   Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA   Yates J.R. III;
RT   "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT   efficient phosphoproteomic analysis.";
RL   J. Proteome Res. 7:1346-1351(2008).
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT   the kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-25; SER-29 AND
RP   SER-80, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [18]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA   Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT   a refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [19]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE
RP   SCALE ANALYSIS] AT SER-5 AND SER-29, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
RA   Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA   Mann M., Daub H.;
RT   "Large-scale proteomics analysis of the human kinome.";
RL   Mol. Cell. Proteomics 8:1751-1764(2009).
RN   [20]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-25 AND SER-29,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [21]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1334, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA   Walther T.C., Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [22]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, ACTIVITY REGULATION, AND
RP   INTERACTION WITH MID1IP1.
RX   PubMed=20952656; DOI=10.1073/pnas.1012736107;
RA   Colbert C.L., Kim C.W., Moon Y.A., Henry L., Palnitkar M.,
RA   McKean W.B., Fitzgerald K., Deisenhofer J., Horton J.D., Kwon H.J.;
RT   "Crystal structure of Spot 14, a modulator of fatty acid synthesis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:18820-18825(2010).
RN   [23]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE
RP   SCALE ANALYSIS] AT SER-5; SER-23; SER-29; SER-48 AND SER-80, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [24]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [25]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29 AND SER-80, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA   Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA   Blagoev B.;
RT   "System-wide temporal characterization of the proteome and
RT   phosphoproteome of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [26]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5; SER-25; SER-29;
RP   SER-80; THR-610; SER-835 AND THR-2153, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [27]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25; SER-29 AND SER-1273,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [28]
RP   VARIANT [LARGE SCALE ANALYSIS] GLN-1687.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA   Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA   Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA   Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA   Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal
RT   cancers.";
RL   Science 314:268-274(2006).
CC   -!- FUNCTION: Catalyzes the rate-limiting reaction in the biogenesis
CC       of long-chain fatty acids. Carries out three functions: biotin
CC       carboxyl carrier protein, biotin carboxylase and
CC       carboxyltransferase. {ECO:0000269|PubMed:20952656}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) +
CC         malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384,
CC         ChEBI:CHEBI:456216; EC=6.4.1.2;
CC         Evidence={ECO:0000269|PubMed:20952656};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein]
CC         = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505,
CC         Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144,
CC         ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14;
CC         Evidence={ECO:0000269|PubMed:20952656};
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC       Note=Binds 2 manganese ions per subunit.;
CC   -!- ACTIVITY REGULATION: By phosphorylation (By similarity). Activity
CC       is increased by oligomerization. Citrate and MID1IP1 promote
CC       oligomerization. {ECO:0000250, ECO:0000269|PubMed:20952656}.
CC   -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA
CC       from acetyl-CoA: step 1/1.
CC   -!- SUBUNIT: Monomer, homodimer, and homotetramer. Can form
CC       filamentous polymers. Interacts in its inactive phosphorylated
CC       form with the BRCT domains of BRCA1 which prevents ACACA
CC       dephosphorylation and inhibits lipid synthesis. Interacts with
CC       MID1IP1; interaction with MID1IP1 promotes oligomerization and
CC       increases its activity. {ECO:0000269|PubMed:12360400,
CC       ECO:0000269|PubMed:16326698, ECO:0000269|PubMed:20952656}.
CC   -!- INTERACTION:
CC       Self; NbExp=2; IntAct=EBI-717681, EBI-717681;
CC       O60218:AKR1B10; NbExp=4; IntAct=EBI-717681, EBI-1572139;
CC       P38398:BRCA1; NbExp=2; IntAct=EBI-717681, EBI-349905;
CC       Q9CQ20:Mid1ip1 (xeno); NbExp=4; IntAct=EBI-717681, EBI-473024;
CC       Q96EB6:SIRT1; NbExp=3; IntAct=EBI-717681, EBI-1802965;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative promoter usage; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q13085-1; Sequence=Displayed;
CC       Name=2; Synonyms=E5A;
CC         IsoId=Q13085-2; Sequence=VSP_026099;
CC       Name=3; Synonyms=E5B;
CC         IsoId=Q13085-3; Sequence=VSP_026098;
CC       Name=4;
CC         IsoId=Q13085-4; Sequence=VSP_026100;
CC   -!- TISSUE SPECIFICITY: Expressed in brain, placental, skeletal
CC       muscle, renal, pancreatic and adipose tissues; expressed at low
CC       level in pulmonary tissue; not detected in the liver.
CC   -!- PTM: Phosphorylation on Ser-1263 is required for interaction with
CC       BRCA1. {ECO:0000269|PubMed:16698035, ECO:0000269|Ref.9}.
CC   -!- DISEASE: Acetyl-CoA carboxylase 1 deficiency (ACACAD)
CC       [MIM:613933]: An inborn error of de novo fatty acid synthesis
CC       associated with severe brain damage, persistent myopathy and poor
CC       growth. {ECO:0000269|PubMed:6114432}. Note=The disease is caused
CC       by mutations affecting the gene represented in this entry.
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=Acetyl-CoA carboxylase entry;
CC       URL="https://en.wikipedia.org/wiki/Acetyl-CoA_carboxylase";
DR   EMBL; U19822; AAC50139.1; -; mRNA.
DR   EMBL; AY315619; AAP94114.1; -; mRNA.
DR   EMBL; AY315620; AAP94115.1; -; mRNA.
DR   EMBL; AY315621; AAP94116.1; -; mRNA.
DR   EMBL; AY315623; AAP94118.1; -; mRNA.
DR   EMBL; AY315627; AAP94122.1; -; mRNA.
DR   EMBL; AY237919; AAP69841.1; -; mRNA.
DR   EMBL; AB371587; BAG48316.1; -; mRNA.
DR   EMBL; CH471199; EAW57582.1; -; Genomic_DNA.
DR   EMBL; CH471199; EAW57577.1; -; Genomic_DNA.
DR   EMBL; CH471199; EAW57578.1; -; Genomic_DNA.
DR   EMBL; CH471199; EAW57581.1; -; Genomic_DNA.
DR   EMBL; BC137287; AAI37288.1; -; mRNA.
DR   EMBL; AJ534888; CAD59556.1; -; mRNA.
DR   EMBL; AJ534889; CAD59557.1; -; mRNA.
DR   EMBL; AJ564444; CAD92089.1; -; mRNA.
DR   CCDS; CCDS11317.1; -. [Q13085-1]
DR   CCDS; CCDS11318.1; -. [Q13085-2]
DR   CCDS; CCDS42302.1; -. [Q13085-4]
DR   CCDS; CCDS42303.1; -. [Q13085-3]
DR   PIR; I38928; I38928.
DR   RefSeq; NP_942131.1; NM_198834.2. [Q13085-4]
DR   RefSeq; NP_942133.1; NM_198836.2. [Q13085-1]
DR   RefSeq; NP_942134.1; NM_198837.1. [Q13085-2]
DR   RefSeq; NP_942135.1; NM_198838.1. [Q13085-3]
DR   RefSeq; NP_942136.1; NM_198839.2. [Q13085-1]
DR   RefSeq; XP_011523005.1; XM_011524703.1. [Q13085-1]
DR   RefSeq; XP_016880044.1; XM_017024555.1. [Q13085-1]
DR   UniGene; Hs.160556; -.
DR   PDB; 2YL2; X-ray; 2.30 A; A/B=78-617.
DR   PDB; 3COJ; X-ray; 3.21 A; H/I/J/K/L/M/N/O=1258-1270.
DR   PDB; 4ASI; X-ray; 2.80 A; A/B/C/D/E/F=1571-2338.
DR   PDB; 6G2D; EM; 5.40 A; B/C/D/F=1-2346.
DR   PDB; 6G2H; EM; 4.60 A; A/B/C/D/E/F=1-2346.
DR   PDB; 6G2I; EM; 5.90 A; A/B/C/D/E/F/G/J/Q/R=1-2346.
DR   PDBsum; 2YL2; -.
DR   PDBsum; 3COJ; -.
DR   PDBsum; 4ASI; -.
DR   PDBsum; 6G2D; -.
DR   PDBsum; 6G2H; -.
DR   PDBsum; 6G2I; -.
DR   ProteinModelPortal; Q13085; -.
DR   SMR; Q13085; -.
DR   BioGrid; 106549; 89.
DR   DIP; DIP-36122N; -.
DR   ELM; Q13085; -.
DR   IntAct; Q13085; 40.
DR   MINT; Q13085; -.
DR   STRING; 9606.ENSP00000483300; -.
DR   BindingDB; Q13085; -.
DR   ChEMBL; CHEMBL3351; -.
DR   DrugBank; DB00121; Biotin.
DR   GuidetoPHARMACOLOGY; 1263; -.
DR   SwissLipids; SLP:000000729; -.
DR   iPTMnet; Q13085; -.
DR   PhosphoSitePlus; Q13085; -.
DR   SwissPalm; Q13085; -.
DR   BioMuta; ACACA; -.
DR   DMDM; 118601083; -.
DR   EPD; Q13085; -.
DR   jPOST; Q13085; -.
DR   MaxQB; Q13085; -.
DR   PaxDb; Q13085; -.
DR   PeptideAtlas; Q13085; -.
DR   PRIDE; Q13085; -.
DR   ProteomicsDB; 59139; -.
DR   ProteomicsDB; 59140; -. [Q13085-2]
DR   ProteomicsDB; 59141; -. [Q13085-3]
DR   ProteomicsDB; 59142; -. [Q13085-4]
DR   Ensembl; ENST00000611803; ENSP00000479901; ENSG00000275176. [Q13085-2]
DR   Ensembl; ENST00000612895; ENSP00000482269; ENSG00000278540. [Q13085-2]
DR   Ensembl; ENST00000613687; ENSP00000483674; ENSG00000275176. [Q13085-1]
DR   Ensembl; ENST00000614428; ENSP00000478547; ENSG00000278540. [Q13085-1]
DR   Ensembl; ENST00000616317; ENSP00000483300; ENSG00000278540. [Q13085-4]
DR   Ensembl; ENST00000617649; ENSP00000482368; ENSG00000278540. [Q13085-3]
DR   Ensembl; ENST00000619487; ENSP00000478577; ENSG00000275176. [Q13085-4]
DR   Ensembl; ENST00000621312; ENSP00000480031; ENSG00000275176. [Q13085-3]
DR   GeneID; 31; -.
DR   KEGG; hsa:31; -.
DR   UCSC; uc002hnk.4; human. [Q13085-1]
DR   CTD; 31; -.
DR   DisGeNET; 31; -.
DR   EuPathDB; HostDB:ENSG00000278540.4; -.
DR   GeneCards; ACACA; -.
DR   HGNC; HGNC:84; ACACA.
DR   HPA; CAB013715; -.
DR   HPA; HPA036650; -.
DR   HPA; HPA063018; -.
DR   MalaCards; ACACA; -.
DR   MIM; 200350; gene.
DR   MIM; 613933; phenotype.
DR   neXtProt; NX_Q13085; -.
DR   OpenTargets; ENSG00000278540; -.
DR   PharmGKB; PA24421; -.
DR   eggNOG; KOG0368; Eukaryota.
DR   eggNOG; COG0439; LUCA.
DR   eggNOG; COG0511; LUCA.
DR   eggNOG; COG4799; LUCA.
DR   GeneTree; ENSGT00940000156706; -.
DR   HOVERGEN; HBG005371; -.
DR   InParanoid; Q13085; -.
DR   KO; K11262; -.
DR   OMA; LPYGEWN; -.
DR   OrthoDB; 1270467at2759; -.
DR   PhylomeDB; Q13085; -.
DR   TreeFam; TF300061; -.
DR   BioCyc; MetaCyc:HS05598-MONOMER; -.
DR   BRENDA; 6.4.1.2; 2681.
DR   Reactome; R-HSA-163765; ChREBP activates metabolic gene expression.
DR   Reactome; R-HSA-196780; Biotin transport and metabolism.
DR   Reactome; R-HSA-200425; Import of palmitoyl-CoA into the mitochondrial matrix.
DR   Reactome; R-HSA-2426168; Activation of gene expression by SREBF (SREBP).
DR   Reactome; R-HSA-3371599; Defective HLCS causes multiple carboxylase deficiency.
DR   Reactome; R-HSA-75105; Fatty acyl-CoA biosynthesis.
DR   SABIO-RK; Q13085; -.
DR   SIGNOR; Q13085; -.
DR   UniPathway; UPA00655; UER00711.
DR   ChiTaRS; ACACA; human.
DR   EvolutionaryTrace; Q13085; -.
DR   GeneWiki; ACACA; -.
DR   GenomeRNAi; 31; -.
DR   PRO; PR:Q13085; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   Bgee; ENSG00000278540; Expressed in 219 organ(s), highest expression level in adrenal tissue.
DR   ExpressionAtlas; Q13085; baseline and differential.
DR   Genevisible; Q13085; HS.
DR   GO; GO:0015629; C:actin cytoskeleton; IDA:HPA.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0001650; C:fibrillar center; IDA:HPA.
DR   GO; GO:0003989; F:acetyl-CoA carboxylase activity; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004075; F:biotin carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006084; P:acetyl-CoA metabolic process; ISS:UniProtKB.
DR   GO; GO:0006853; P:carnitine shuttle; TAS:Reactome.
DR   GO; GO:0071380; P:cellular response to prostaglandin E stimulus; IEA:Ensembl.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0046949; P:fatty-acyl-CoA biosynthetic process; TAS:Reactome.
DR   GO; GO:0055088; P:lipid homeostasis; IEA:Ensembl.
DR   GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0031325; P:positive regulation of cellular metabolic process; TAS:Reactome.
DR   GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
DR   GO; GO:0019538; P:protein metabolic process; IEA:Ensembl.
DR   GO; GO:0045540; P:regulation of cholesterol biosynthetic process; TAS:Reactome.
DR   GO; GO:0001894; P:tissue homeostasis; IEA:Ensembl.
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   3D-structure; Acetylation; Allosteric enzyme;
KW   Alternative promoter usage; ATP-binding; Biotin; Complete proteome;
KW   Cytoplasm; Direct protein sequencing; Fatty acid biosynthesis;
KW   Fatty acid metabolism; Ligase; Lipid biosynthesis; Lipid metabolism;
KW   Manganese; Metal-binding; Multifunctional enzyme; Nucleotide-binding;
KW   Phosphoprotein; Polymorphism; Reference proteome.
FT   CHAIN         1   2346       Acetyl-CoA carboxylase 1.
FT                                /FTId=PRO_0000146764.
FT   DOMAIN      117    618       Biotin carboxylation.
FT   DOMAIN      275    466       ATP-grasp. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   DOMAIN      745    819       Biotinyl-binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01066}.
FT   DOMAIN     1576   1914       CoA carboxyltransferase N-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01136}.
FT   DOMAIN     1918   2234       CoA carboxyltransferase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01137}.
FT   NP_BIND     315    320       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   REGION     1576   2234       Carboxyltransferase.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01138}.
FT   ACT_SITE    441    441       {ECO:0000250}.
FT   METAL       424    424       Manganese 1. {ECO:0000250}.
FT   METAL       437    437       Manganese 1. {ECO:0000250}.
FT   METAL       437    437       Manganese 2. {ECO:0000250}.
FT   METAL       439    439       Manganese 2. {ECO:0000250}.
FT   BINDING    1823   1823       Coenzyme A. {ECO:0000250}.
FT   BINDING    2127   2127       Coenzyme A. {ECO:0000250}.
FT   BINDING    2129   2129       Coenzyme A. {ECO:0000250}.
FT   MOD_RES       1      1       N-acetylmethionine.
FT                                {ECO:0000244|PubMed:19369195,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000269|Ref.9}.
FT   MOD_RES       5      5       Phosphoserine.
FT                                {ECO:0000244|PubMed:19369195,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:23186163}.
FT   MOD_RES      23     23       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:20068231}.
FT   MOD_RES      25     25       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:23186163,
FT                                ECO:0000244|PubMed:24275569}.
FT   MOD_RES      29     29       Phosphoserine.
FT                                {ECO:0000244|PubMed:17081983,
FT                                ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:18691976,
FT                                ECO:0000244|PubMed:19369195,
FT                                ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:21406692,
FT                                ECO:0000244|PubMed:23186163,
FT                                ECO:0000244|PubMed:24275569}.
FT   MOD_RES      34     34       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P11497}.
FT   MOD_RES      48     48       Phosphoserine.
FT                                {ECO:0000244|PubMed:20068231}.
FT   MOD_RES      50     50       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P11497}.
FT   MOD_RES      53     53       Phosphoserine.
FT                                {ECO:0000244|PubMed:17081983}.
FT   MOD_RES      58     58       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q5SWU9}.
FT   MOD_RES      78     78       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P11497}.
FT   MOD_RES      80     80       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:21406692,
FT                                ECO:0000244|PubMed:23186163,
FT                                ECO:0000269|Ref.9}.
FT   MOD_RES     488    488       Phosphoserine.
FT                                {ECO:0000244|PubMed:18220336}.
FT   MOD_RES     610    610       Phosphothreonine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     786    786       N6-biotinyllysine. {ECO:0000250,
FT                                ECO:0000255|PROSITE-ProRule:PRU01066}.
FT   MOD_RES     835    835       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES    1201   1201       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P11497}.
FT   MOD_RES    1216   1216       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P11497}.
FT   MOD_RES    1218   1218       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q5SWU9}.
FT   MOD_RES    1227   1227       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q5SWU9}.
FT   MOD_RES    1259   1259       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q5SWU9}.
FT   MOD_RES    1263   1263       Phosphoserine.
FT                                {ECO:0000269|PubMed:16698035}.
FT   MOD_RES    1273   1273       Phosphoserine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   MOD_RES    1334   1334       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:19608861}.
FT   MOD_RES    2153   2153       Phosphothreonine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   VAR_SEQ       1     78       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:12810950,
FT                                ECO:0000303|PubMed:14643797}.
FT                                /FTId=VSP_026098.
FT   VAR_SEQ       1     75       MDEPSPLAQPLELNQHSRFIIGSVSEDNSEDEISNLVKLDL
FT                                LEEKEGSLSPASVGSDTLSDLGISSLQDGLALHI -> MEG
FT                                SPEENKEMRYYMLQ (in isoform 2).
FT                                {ECO:0000303|PubMed:12810950,
FT                                ECO:0000303|PubMed:14643797}.
FT                                /FTId=VSP_026099.
FT   VAR_SEQ       1      1       M -> MWWSTLMSILRARSFWKWISTQTVRIIRAVRAHFGG
FT                                IM (in isoform 4).
FT                                {ECO:0000303|PubMed:12810950,
FT                                ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_026100.
FT   VARIANT     838    838       R -> W (in dbSNP:rs2287351).
FT                                /FTId=VAR_042941.
FT   VARIANT    1687   1687       R -> Q (in a colorectal cancer sample;
FT                                somatic mutation; dbSNP:rs1357271377).
FT                                {ECO:0000269|PubMed:16959974}.
FT                                /FTId=VAR_036514.
FT   VARIANT    2271   2271       A -> V (rare polymorphism; frequency
FT                                <0.004; may play a role in breast cancer
FT                                susceptibility; dbSNP:rs146351326).
FT                                {ECO:0000269|PubMed:15333468}.
FT                                /FTId=VAR_028929.
FT   MUTAGEN      78     78       S->A: No effect on interaction with
FT                                BRCA1. {ECO:0000269|PubMed:16698035}.
FT   MUTAGEN     344    344       S->A: No effect on interaction with
FT                                BRCA1. {ECO:0000269|PubMed:16698035}.
FT   MUTAGEN     432    432       S->A: No effect on interaction with
FT                                BRCA1. {ECO:0000269|PubMed:16698035}.
FT   MUTAGEN    1201   1201       S->A: No effect on interaction with
FT                                BRCA1. {ECO:0000269|PubMed:16698035}.
FT   MUTAGEN    1263   1263       S->A: Abolishes interaction with BRCA1.
FT                                {ECO:0000269|PubMed:16698035}.
FT   MUTAGEN    1585   1585       S->A: No effect on interaction with
FT                                BRCA1. {ECO:0000269|PubMed:16698035}.
FT   MUTAGEN    1952   1952       S->A: No effect on interaction with
FT                                BRCA1. {ECO:0000269|PubMed:16698035}.
FT   MUTAGEN    2211   2211       S->A: No effect on interaction with
FT                                BRCA1. {ECO:0000269|PubMed:16698035}.
FT   CONFLICT     66     66       S -> A (in Ref. 1; AAC50139).
FT                                {ECO:0000305}.
FT   CONFLICT     79     79       M -> W (in Ref. 1; AAC50139).
FT                                {ECO:0000305}.
FT   CONFLICT     89     89       R -> G (in Ref. 1; AAC50139).
FT                                {ECO:0000305}.
FT   CONFLICT    182    182       P -> A (in Ref. 1; AAC50139).
FT                                {ECO:0000305}.
FT   CONFLICT    234    234       S -> N (in Ref. 1; AAC50139).
FT                                {ECO:0000305}.
FT   CONFLICT    299    299       Q -> K (in Ref. 1; AAC50139).
FT                                {ECO:0000305}.
FT   CONFLICT    303    303       E -> K (in Ref. 1; AAC50139).
FT                                {ECO:0000305}.
FT   CONFLICT    364    364       A -> V (in Ref. 2; AAP94122).
FT                                {ECO:0000305}.
FT   CONFLICT    446    446       H -> Q (in Ref. 1; AAC50139).
FT                                {ECO:0000305}.
FT   CONFLICT    494    494       D -> N (in Ref. 1; AAC50139).
FT                                {ECO:0000305}.
FT   CONFLICT    554    554       D -> G (in Ref. 1; AAC50139).
FT                                {ECO:0000305}.
FT   CONFLICT    622    622       Q -> R (in Ref. 1; AAC50139).
FT                                {ECO:0000305}.
FT   CONFLICT    640    640       A -> G (in Ref. 1; AAC50139).
FT                                {ECO:0000305}.
FT   CONFLICT    814    814       V -> I (in Ref. 2; AAP94122).
FT                                {ECO:0000305}.
FT   CONFLICT   1061   1061       N -> S (in Ref. 1; AAC50139).
FT                                {ECO:0000305}.
FT   CONFLICT   1094   1095       EL -> DV (in Ref. 1; AAC50139).
FT                                {ECO:0000305}.
FT   CONFLICT   1225   1225       S -> A (in Ref. 1; AAC50139).
FT                                {ECO:0000305}.
FT   CONFLICT   1257   1257       S -> C (in Ref. 1; AAC50139).
FT                                {ECO:0000305}.
FT   CONFLICT   1297   1297       C -> G (in Ref. 1; AAC50139).
FT                                {ECO:0000305}.
FT   CONFLICT   1320   1320       V -> A (in Ref. 1; AAC50139).
FT                                {ECO:0000305}.
FT   CONFLICT   1444   1444       N -> S (in Ref. 1; AAC50139).
FT                                {ECO:0000305}.
FT   CONFLICT   1474   1474       F -> L (in Ref. 1; AAC50139).
FT                                {ECO:0000305}.
FT   CONFLICT   1665   1666       TF -> SL (in Ref. 1; AAC50139).
FT                                {ECO:0000305}.
FT   CONFLICT   1677   1677       I -> V (in Ref. 1; AAC50139).
FT                                {ECO:0000305}.
FT   CONFLICT   1741   1741       P -> S (in Ref. 1; AAC50139).
FT                                {ECO:0000305}.
FT   CONFLICT   1762   1762       S -> G (in Ref. 1; AAC50139).
FT                                {ECO:0000305}.
FT   CONFLICT   1822   1822       C -> S (in Ref. 1; AAC50139).
FT                                {ECO:0000305}.
FT   CONFLICT   1875   1875       M -> T (in Ref. 1; AAC50139).
FT                                {ECO:0000305}.
FT   CONFLICT   1888   1888       D -> G (in Ref. 1; AAC50139).
FT                                {ECO:0000305}.
FT   CONFLICT   1997   1997       I -> V (in Ref. 1; AAC50139).
FT                                {ECO:0000305}.
FT   CONFLICT   2013   2013       Q -> H (in Ref. 1; AAC50139).
FT                                {ECO:0000305}.
FT   CONFLICT   2058   2058       D -> H (in Ref. 1; AAC50139).
FT                                {ECO:0000305}.
FT   CONFLICT   2075   2075       C -> S (in Ref. 1; AAC50139).
FT                                {ECO:0000305}.
FT   CONFLICT   2098   2099       SS -> PT (in Ref. 1; AAC50139).
FT                                {ECO:0000305}.
FT   CONFLICT   2158   2159       TA -> PT (in Ref. 1; AAC50139).
FT                                {ECO:0000305}.
FT   CONFLICT   2166   2166       N -> S (in Ref. 1; AAC50139).
FT                                {ECO:0000305}.
FT   CONFLICT   2234   2234       N -> S (in Ref. 1; AAC50139).
FT                                {ECO:0000305}.
FT   CONFLICT   2321   2321       H -> R (in Ref. 2; AAP94122).
FT                                {ECO:0000305}.
FT   HELIX       105    111       {ECO:0000244|PDB:2YL2}.
FT   STRAND      120    123       {ECO:0000244|PDB:2YL2}.
FT   HELIX       127    145       {ECO:0000244|PDB:2YL2}.
FT   STRAND      150    157       {ECO:0000244|PDB:2YL2}.
FT   HELIX       159    163       {ECO:0000244|PDB:2YL2}.
FT   HELIX       168    171       {ECO:0000244|PDB:2YL2}.
FT   STRAND      172    177       {ECO:0000244|PDB:2YL2}.
FT   HELIX       183    185       {ECO:0000244|PDB:2YL2}.
FT   TURN        186    188       {ECO:0000244|PDB:2YL2}.
FT   HELIX       190    199       {ECO:0000244|PDB:2YL2}.
FT   STRAND      203    206       {ECO:0000244|PDB:2YL2}.
FT   TURN        211    214       {ECO:0000244|PDB:2YL2}.
FT   HELIX       217    224       {ECO:0000244|PDB:2YL2}.
FT   STRAND      228    231       {ECO:0000244|PDB:2YL2}.
FT   HELIX       234    241       {ECO:0000244|PDB:2YL2}.
FT   HELIX       243    252       {ECO:0000244|PDB:2YL2}.
FT   TURN        261    264       {ECO:0000244|PDB:2YL2}.
FT   HELIX       283    289       {ECO:0000244|PDB:2YL2}.
FT   HELIX       294    304       {ECO:0000244|PDB:2YL2}.
FT   STRAND      306    312       {ECO:0000244|PDB:2YL2}.
FT   STRAND      320    324       {ECO:0000244|PDB:2YL2}.
FT   TURN        327    329       {ECO:0000244|PDB:2YL2}.
FT   HELIX       330    340       {ECO:0000244|PDB:2YL2}.
FT   STRAND      346    350       {ECO:0000244|PDB:2YL2}.
FT   STRAND      356    364       {ECO:0000244|PDB:2YL2}.
FT   STRAND      370    382       {ECO:0000244|PDB:2YL2}.
FT   STRAND      385    392       {ECO:0000244|PDB:2YL2}.
FT   HELIX       398    415       {ECO:0000244|PDB:2YL2}.
FT   STRAND      419    427       {ECO:0000244|PDB:2YL2}.
FT   STRAND      433    439       {ECO:0000244|PDB:2YL2}.
FT   TURN        444    446       {ECO:0000244|PDB:2YL2}.
FT   HELIX       447    453       {ECO:0000244|PDB:2YL2}.
FT   HELIX       457    465       {ECO:0000244|PDB:2YL2}.
FT   HELIX       470    472       {ECO:0000244|PDB:2YL2}.
FT   HELIX       474    479       {ECO:0000244|PDB:2YL2}.
FT   TURN        492    495       {ECO:0000244|PDB:2YL2}.
FT   STRAND      496    498       {ECO:0000244|PDB:2YL2}.
FT   STRAND      503    510       {ECO:0000244|PDB:2YL2}.
FT   STRAND      526    530       {ECO:0000244|PDB:2YL2}.
FT   STRAND      537    542       {ECO:0000244|PDB:2YL2}.
FT   STRAND      557    566       {ECO:0000244|PDB:2YL2}.
FT   HELIX       567    582       {ECO:0000244|PDB:2YL2}.
FT   HELIX       589    599       {ECO:0000244|PDB:2YL2}.
FT   HELIX       601    604       {ECO:0000244|PDB:2YL2}.
FT   HELIX       612    616       {ECO:0000244|PDB:2YL2}.
FT   HELIX      1582   1592       {ECO:0000244|PDB:4ASI}.
FT   HELIX      1598   1600       {ECO:0000244|PDB:4ASI}.
FT   HELIX      1601   1619       {ECO:0000244|PDB:4ASI}.
FT   HELIX      1628   1631       {ECO:0000244|PDB:4ASI}.
FT   STRAND     1632   1639       {ECO:0000244|PDB:4ASI}.
FT   STRAND     1645   1648       {ECO:0000244|PDB:4ASI}.
FT   STRAND     1656   1666       {ECO:0000244|PDB:4ASI}.
FT   STRAND     1675   1682       {ECO:0000244|PDB:4ASI}.
FT   HELIX      1687   1689       {ECO:0000244|PDB:4ASI}.
FT   HELIX      1693   1709       {ECO:0000244|PDB:4ASI}.
FT   STRAND     1713   1717       {ECO:0000244|PDB:4ASI}.
FT   HELIX      1728   1731       {ECO:0000244|PDB:4ASI}.
FT   STRAND     1735   1739       {ECO:0000244|PDB:4ASI}.
FT   HELIX      1744   1746       {ECO:0000244|PDB:4ASI}.
FT   STRAND     1748   1753       {ECO:0000244|PDB:4ASI}.
FT   HELIX      1755   1761       {ECO:0000244|PDB:4ASI}.
FT   HELIX      1762   1764       {ECO:0000244|PDB:4ASI}.
FT   STRAND     1767   1774       {ECO:0000244|PDB:4ASI}.
FT   STRAND     1777   1785       {ECO:0000244|PDB:4ASI}.
FT   HELIX      1795   1813       {ECO:0000244|PDB:4ASI}.
FT   STRAND     1816   1820       {ECO:0000244|PDB:4ASI}.
FT   STRAND     1822   1825       {ECO:0000244|PDB:4ASI}.
FT   HELIX      1827   1834       {ECO:0000244|PDB:4ASI}.
FT   STRAND     1837   1841       {ECO:0000244|PDB:4ASI}.
FT   STRAND     1845   1849       {ECO:0000244|PDB:4ASI}.
FT   HELIX      1851   1858       {ECO:0000244|PDB:4ASI}.
FT   HELIX      1866   1870       {ECO:0000244|PDB:4ASI}.
FT   HELIX      1872   1875       {ECO:0000244|PDB:4ASI}.
FT   TURN       1876   1879       {ECO:0000244|PDB:4ASI}.
FT   STRAND     1882   1887       {ECO:0000244|PDB:4ASI}.
FT   HELIX      1888   1899       {ECO:0000244|PDB:4ASI}.
FT   STRAND     1914   1917       {ECO:0000244|PDB:4ASI}.
FT   HELIX      1934   1939       {ECO:0000244|PDB:4ASI}.
FT   STRAND     1944   1946       {ECO:0000244|PDB:4ASI}.
FT   STRAND     1961   1964       {ECO:0000244|PDB:4ASI}.
FT   STRAND     1971   1978       {ECO:0000244|PDB:4ASI}.
FT   STRAND     1981   1988       {ECO:0000244|PDB:4ASI}.
FT   STRAND     1993   1996       {ECO:0000244|PDB:4ASI}.
FT   STRAND     2010   2013       {ECO:0000244|PDB:4ASI}.
FT   HELIX      2020   2036       {ECO:0000244|PDB:4ASI}.
FT   STRAND     2040   2043       {ECO:0000244|PDB:4ASI}.
FT   HELIX      2053   2057       {ECO:0000244|PDB:4ASI}.
FT   HELIX      2060   2072       {ECO:0000244|PDB:4ASI}.
FT   STRAND     2078   2082       {ECO:0000244|PDB:4ASI}.
FT   STRAND     2087   2089       {ECO:0000244|PDB:4ASI}.
FT   HELIX      2090   2094       {ECO:0000244|PDB:4ASI}.
FT   HELIX      2098   2100       {ECO:0000244|PDB:4ASI}.
FT   TURN       2102   2104       {ECO:0000244|PDB:4ASI}.
FT   STRAND     2105   2110       {ECO:0000244|PDB:4ASI}.
FT   STRAND     2114   2118       {ECO:0000244|PDB:4ASI}.
FT   HELIX      2120   2127       {ECO:0000244|PDB:4ASI}.
FT   HELIX      2130   2140       {ECO:0000244|PDB:4ASI}.
FT   HELIX      2142   2150       {ECO:0000244|PDB:4ASI}.
FT   HELIX      2158   2188       {ECO:0000244|PDB:4ASI}.
FT   HELIX      2193   2198       {ECO:0000244|PDB:4ASI}.
FT   STRAND     2201   2206       {ECO:0000244|PDB:4ASI}.
FT   HELIX      2208   2210       {ECO:0000244|PDB:4ASI}.
FT   HELIX      2211   2235       {ECO:0000244|PDB:4ASI}.
FT   HELIX      2241   2256       {ECO:0000244|PDB:4ASI}.
FT   HELIX      2258   2265       {ECO:0000244|PDB:4ASI}.
FT   HELIX      2267   2278       {ECO:0000244|PDB:4ASI}.
FT   HELIX      2289   2310       {ECO:0000244|PDB:4ASI}.
FT   HELIX      2312   2314       {ECO:0000244|PDB:4ASI}.
FT   HELIX      2315   2322       {ECO:0000244|PDB:4ASI}.
FT   HELIX      2323   2325       {ECO:0000244|PDB:4ASI}.
FT   HELIX      2328   2337       {ECO:0000244|PDB:4ASI}.
SQ   SEQUENCE   2346 AA;  265554 MW;  F1F0A518F8824FFC CRC64;
     MDEPSPLAQP LELNQHSRFI IGSVSEDNSE DEISNLVKLD LLEEKEGSLS PASVGSDTLS
     DLGISSLQDG LALHIRSSMS GLHLVKQGRD RKKIDSQRDF TVASPAEFVT RFGGNKVIEK
     VLIANNGIAA VKCMRSIRRW SYEMFRNERA IRFVVMVTPE DLKANAEYIK MADHYVPVPG
     GPNNNNYANV ELILDIAKRI PVQAVWAGWG HASENPKLPE LLLKNGIAFM GPPSQAMWAL
     GDKIASSIVA QTAGIPTLPW SGSGLRVDWQ ENDFSKRILN VPQELYEKGY VKDVDDGLQA
     AEEVGYPVMI KASEGGGGKG IRKVNNADDF PNLFRQVQAE VPGSPIFVMR LAKQSRHLEV
     QILADQYGNA ISLFGRDCSV QRRHQKIIEE APATIATPAV FEHMEQCAVK LAKMVGYVSA
     GTVEYLYSQD GSFYFLELNP RLQVEHPCTE MVADVNLPAA QLQIAMGIPL YRIKDIRMMY
     GVSPWGDSPI DFEDSAHVPC PRGHVIAARI TSENPDEGFK PSSGTVQELN FRSNKNVWGY
     FSVAAAGGLH EFADSQFGHC FSWGENREEA ISNMVVALKE LSIRGDFRTT VEYLIKLLET
     ESFQMNRIDT GWLDRLIAEK VQAERPDTML GVVCGALHVA DVSLRNSVSN FLHSLERGQV
     LPAHTLLNTV DVELIYEGVK YVLKVTRQSP NSYVVIMNGS CVEVDVHRLS DGGLLLSYDG
     SSYTTYMKEE VDRYRITIGN KTCVFEKEND PSVMRSPSAG KLIQYIVEDG GHVFAGQCYA
     EIEVMKMVMT LTAVESGCIH YVKRPGAALD PGCVLAKMQL DNPSKVQQAE LHTGSLPRIQ
     STALRGEKLH RVFHYVLDNL VNVMNGYCLP DPFFSSKVKD WVERLMKTLR DPSLPLLELQ
     DIMTSVSGRI PPNVEKSIKK EMAQYASNIT SVLCQFPSQQ IANILDSHAA TLNRKSEREV
     FFMNTQSIVQ LVQRYRSGIR GHMKAVVMDL LRQYLRVETQ FQNGHYDKCV FALREENKSD
     MNTVLNYIFS HAQVTKKNLL VTMLIDQLCG RDPTLTDELL NILTELTQLS KTTNAKVALR
     ARQVLIASHL PSYELRHNQV ESIFLSAIDM YGHQFCIENL QKLILSETSI FDVLPNFFYH
     SNQVVRMAAL EVYVRRAYIA YELNSVQHRQ LKDNTCVVEF QFMLPTSHPN RGNIPTLNRM
     SFSSNLNHYG MTHVASVSDV LLDNSFTPPC QRMGGMVSFR TFEDFVRIFD EVMGCFSDSP
     PQSPTFPEAG HTSLYDEDKV PRDEPIHILN VAIKTDCDIE DDRLAAMFRE FTQQNKATLV
     DHGIRRLTFL VAQKDFRKQV NYEVDRRFHR EFPKFFTFRA RDKFEEDRIY RHLEPALAFQ
     LELNRMRNFD LTAIPCANHK MHLYLGAAKV EVGTEVTDYR FFVRAIIRHS DLVTKEASFE
     YLQNEGERLL LEAMDELEVA FNNTNVRTDC NHIFLNFVPT VIMDPSKIEE SVRSMVMRYG
     SRLWKLRVLQ AELKINIRLT PTGKAIPIRL FLTNESGYYL DISLYKEVTD SRTAQIMFQA
     YGDKQGPLHG MLINTPYVTK DLLQSKRFQA QSLGTTYIYD IPEMFRQSLI KLWESMSTQA
     FLPSPPLPSD MLTYTELVLD DQGQLVHMNR LPGGNEIGMV AWKMTFKSPE YPEGRDIIVI
     GNDITYRIGS FGPQEDLLFL RASELARAEG IPRIYVSANS GARIGLAEEI RHMFHVAWVD
     PEDPYKGYRY LYLTPQDYKR VSALNSVHCE HVEDEGESRY KITDIIGKEE GIGPENLRGS
     GMIAGESSLA YNEIITISLV TCRAIGIGAY LVRLGQRTIQ VENSHLILTG AGALNKVLGR
     EVYTSNNQLG GIQIMHNNGV THCTVCDDFE GVFTVLHWLS YMPKSVHSSV PLLNSKDPID
     RIIEFVPTKT PYDPRWMLAG RPHPTQKGQW LSGFFDYGSF SEIMQPWAQT VVVGRARLGG
     IPVGVVAVET RTVELSIPAD PANLDSEAKI IQQAGQVWFP DSAFKTYQAI KDFNREGLPL
     MVFANWRGFS GGMKDMYDQV LKFGAYIVDG LRECCQPVLV YIPPQAELRG GSWVVIDSSI
     NPRHMEMYAD RESRGSVLEP EGTVEIKFRR KDLVKTMRRV DPVYIHLAER LGTPELSTAE
     RKELENKLKE REEFLIPIYH QVAVQFADLH DTPGRMQEKG VISDILDWKT SRTFFYWRLR
     RLLLEDLVKK KIHNANPELT DGQIQAMLRR WFVEVEGTVK AYVWDNNKDL AEWLEKQLTE
     EDGVHSVIEE NIKCISRDYV LKQIRSLVQA NPEVAMDSII HMTQHISPTQ RAEVIRILST
     MDSPST
//
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