ID   Q59FY4_HUMAN            Unreviewed;       998 AA.
AC   Q59FY4;
DT   26-APR-2005, integrated into UniProtKB/TrEMBL.
DT   26-APR-2005, sequence version 1.
DT   27-MAR-2024, entry version 102.
DE   SubName: Full=Acetyl-CoA carboxylase 1 {ECO:0000313|Ensembl:ENSP00000488846.1};
DE   SubName: Full=Acetyl-CoA carboxylase alpha {ECO:0000313|Ensembl:ENSP00000483969.1};
DE   SubName: Full=Acetyl-Coenzyme A carboxylase alpha isoform 2 variant {ECO:0000313|EMBL:BAD92562.1};
DE   Flags: Fragment;
GN   Name=ACACA {ECO:0000313|Ensembl:ENSP00000483969.1};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|EMBL:BAD92562.1};
RN   [1] {ECO:0000313|EMBL:BAD92562.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain {ECO:0000313|EMBL:BAD92562.1};
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA   Ohara O., Nagase T., Kikuno R.F.;
RT   "Homo sapiens protein coding cDNA.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSP00000483969.1, ECO:0000313|Proteomes:UP000005640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16625196; DOI=10.1038/nature04689;
RA   Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA   Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA   Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA   Chang J.L., Chen C.K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA   DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA   Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA   Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA   LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA   Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA   Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA   Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA   Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA   Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT   "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT   human lineage.";
RL   Nature 440:1045-1049(2006).
RN   [3] {ECO:0007829|PubMed:19608861}
RP   IDENTIFICATION BY 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., Walther T.C.,
RA   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   [4] {ECO:0007829|PubMed:21269460}
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., Burckstummer T.,
RA   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   [5] {ECO:0007829|PubMed:23186163}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=23186163;
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   [6] {ECO:0000313|Ensembl:ENSP00000488846.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (AUG-2022) to UniProtKB.
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DR   EMBL; AC003103; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC016482; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC068400; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC243628; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC243654; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC244093; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KF456271; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AB209325; BAD92562.1; -; mRNA.
DR   IntAct; Q59FY4; 3.
DR   Antibodypedia; 73364; 835 antibodies from 39 providers.
DR   Ensembl; ENST00000619546.4; ENSP00000483969.1; ENSG00000278540.5.
DR   Ensembl; ENST00000632453.1; ENSP00000488846.1; ENSG00000275176.4.
DR   UCSC; uc060eje.1; human.
DR   HGNC; HGNC:84; ACACA.
DR   VEuPathDB; HostDB:ENSG00000278540; -.
DR   GeneTree; ENSGT00940000156706; -.
DR   HOGENOM; CLU_004031_0_0_1; -.
DR   ChiTaRS; ACACA; human.
DR   Proteomes; UP000005640; Unplaced.
DR   Bgee; ENSG00000278540; Expressed in cortical plate and 104 other cell types or tissues.
DR   GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   InterPro; IPR049076; ACCA.
DR   InterPro; IPR034733; AcCoA_carboxyl_beta.
DR   InterPro; IPR013537; AcCoA_COase_cen.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR011763; COA_CT_C.
DR   InterPro; IPR011762; COA_CT_N.
DR   PANTHER; PTHR45728:SF5; ACETYL-COA CARBOXYLASE 1; 1.
DR   PANTHER; PTHR45728; ACETYL-COA CARBOXYLASE, ISOFORM A; 1.
DR   Pfam; PF08326; ACC_central; 1.
DR   Pfam; PF01039; Carboxyl_trans; 1.
DR   SUPFAM; SSF52096; ClpP/crotonase; 2.
DR   PROSITE; PS50989; COA_CT_CTER; 1.
DR   PROSITE; PS50980; COA_CT_NTER; 1.
PE   1: Evidence at protein level;
KW   Proteomics identification {ECO:0007829|EPD:Q59FY4,
KW   ECO:0007829|MaxQB:Q59FY4};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005640}.
FT   DOMAIN          310..566
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50980"
FT   DOMAIN          570..886
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50989"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:BAD92562.1"
SQ   SEQUENCE   998 AA;  114618 MW;  78A0767D8144A97C CRC64;
     EDDRLAAMFR EFTQQNKATL VDHGIRRLTF LVAQKDFRKQ VNYEVDRRFH REFPKFFTFR
     ARDKFEEDRI YRHLEPALAF QLELNRMRNF DLTAIPCANH KMHLYLGAAK VEVGTEVTDY
     RFFVRAIIRH SDLVTKEASF EYLQNEGERL LLEAMDELEV AFNNTNVRTD CNHIFLNFVP
     TVIMDPSKIE ESVRSMVMRY GSRLWKLRVL QAELKINIRL TPTGKAIPIR LFLTNESGYY
     LDISLYKEVT DSRTAQIMFQ AYGDKQGPLH GMLINTPYVT KDLLQSKRFQ AQSLGTTYIY
     DIPEMFRQIG MVAWKMTFKS PEYPEGRDII VIGNDITYRI GSFGPQEDLL FLRASELARA
     EGIPRIYVSA NSGARIGLAE EIRHMFHVAW VDPEDPYKGY RYLYLTPQDY KRVSALNSVH
     CEHVEDEGES RYKITDIIGK EEGIGPENLR GSGMIAGESS LAYNEIITIS LVTCRAIGIG
     AYLVRLGQRT IQVENSHLIL TGAGALNKVL GREVYTSNNQ LGGIQIMHNN GVTHCTVCDD
     FEGVFTVLHW LSYMPKSVHS SVPLLNSKDP IDRIIEFVPT KTPYDPRWML AGRPHPTQKG
     QWLSGFFDYG SFSEIMQPWA QTVVVGRARL GGIPVGVVAV ETRTVELSIP ADPANLDSEA
     KIIQQAGQVW FPDSAFKTYQ AIKDFNREGL PLMVFANWRG FSGGMKDMYD QVLKFGAYIV
     DGLRECCQPV LVYIPPQAEL RGGSWVVIDS SINPRHMEMY ADRESRGSVL EPEGTVEIKF
     RRKDLVKTMR RVDPVYIHLA ERLGTPELST AERKELENKL KEREEFLIPI YHQVAVQFAD
     LHDTPGRMQE KGVISDILDW KTSRTFFYWR LRRLLLEDLV KKKIHNANPE LTDGQIQAML
     RRWFVEVEGT VKAYVWDNNK DLAEWLEKQL TEEDGVHSVI EENIKCISRD YVLKQIRSLV
     QANPEVAMDS IIHMTQHISP TQRAEVIRIL STMDSPST
//