GenomeNet

Database: RefSeq
Entry: NP_014413
LinkDB: NP_014413
Original site: NP_014413 
LOCUS       NP_014413               2233 aa            linear   PLN 15-SEP-2023
DEFINITION  acetyl-CoA carboxylase ACC1 [Saccharomyces cerevisiae S288C].
ACCESSION   NP_014413
VERSION     NP_014413.1
DBLINK      BioProject: PRJNA128
DBSOURCE    REFSEQ: accession NM_001183193.1
KEYWORDS    RefSeq.
SOURCE      Saccharomyces cerevisiae S288C
  ORGANISM  Saccharomyces cerevisiae S288C
            Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
            Saccharomycetes; Saccharomycetales; Saccharomycetaceae;
            Saccharomyces.
REFERENCE   1  (residues 1 to 2233)
  AUTHORS   Engel,S.R., Wong,E.D., Nash,R.S., Aleksander,S., Alexander,M.,
            Douglass,E., Karra,K., Miyasato,S.R., Simison,M., Skrzypek,M.S.,
            Weng,S. and Cherry,J.M.
  TITLE     New data and collaborations at the Saccharomyces Genome Database:
            updated reference genome, alleles, and the Alliance of Genome
            Resources
  JOURNAL   Genetics 220 (4) (2022)
   PUBMED   34897464
REFERENCE   2  (residues 1 to 2233)
  AUTHORS   Philippsen,P., Kleine,K., Pohlmann,R., Dusterhoft,A., Hamberg,K.,
            Hegemann,J.H., Obermaier,B., Urrestarazu,L.A., Aert,R.,
            Albermann,K., Altmann,R., Andre,B., Baladron,V., Ballesta,J.P.,
            Becam,A.M., Beinhauer,J., Boskovic,J., Buitrago,M.J., Bussereau,F.,
            Coster,F., Crouzet,M., D'Angelo,M., Dal Pero,F., De Antoni,A.,
            Hani,J. et al.
  TITLE     The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV
            and its evolutionary implications
  JOURNAL   Nature 387 (6632 SUPPL), 93-98 (1997)
   PUBMED   9169873
REFERENCE   3  (residues 1 to 2233)
  AUTHORS   Goffeau,A., Barrell,B.G., Bussey,H., Davis,R.W., Dujon,B.,
            Feldmann,H., Galibert,F., Hoheisel,J.D., Jacq,C., Johnston,M.,
            Louis,E.J., Mewes,H.W., Murakami,Y., Philippsen,P., Tettelin,H. and
            Oliver,S.G.
  TITLE     Life with 6000 genes
  JOURNAL   Science 274 (5287), 546 (1996)
   PUBMED   8849441
REFERENCE   4  (residues 1 to 2233)
  CONSRTM   NCBI Genome Project
  TITLE     Direct Submission
  JOURNAL   Submitted (14-SEP-2023) National Center for Biotechnology
            Information, NIH, Bethesda, MD 20894, USA
REFERENCE   5  (residues 1 to 2233)
  CONSRTM   Saccharomyces Genome Database
  TITLE     Direct Submission
  JOURNAL   Submitted (04-MAY-2012) Department of Genetics, Stanford
            University, Stanford, CA 94305-5120, USA
  REMARK    Protein update by submitter
REFERENCE   6  (residues 1 to 2233)
  CONSRTM   Saccharomyces Genome Database
  TITLE     Direct Submission
  JOURNAL   Submitted (31-MAR-2011) Department of Genetics, Stanford
            University, Stanford, CA 94305-5120, USA
  REMARK    Sequence update by submitter
REFERENCE   7  (residues 1 to 2233)
  CONSRTM   Saccharomyces Genome Database
  TITLE     Direct Submission
  JOURNAL   Submitted (26-MAY-2010) Department of Genetics, Stanford
            University, Stanford, CA 94305-5120, USA
  REMARK    Sequence update by submitter
REFERENCE   8  (residues 1 to 2233)
  CONSRTM   Saccharomyces Genome Database
  TITLE     Direct Submission
  JOURNAL   Submitted (14-DEC-2009) Department of Genetics, Stanford
            University, Stanford, CA 94305-5120, USA
COMMENT     REVIEWED REFSEQ: This record has been curated by SGD. The reference
            sequence is identical to DAA10557.
            
            ##Genome-Annotation-Data-START##
            Annotation Provider :: SGD
            Annotation Status   :: Full Annotation
            Annotation Version  :: R64-4-1
            URL                 :: http://www.yeastgenome.org/
            ##Genome-Annotation-Data-END##
            Method: conceptual translation.
FEATURES             Location/Qualifiers
     source          1..2233
                     /organism="Saccharomyces cerevisiae S288C"
                     /strain="S288C"
                     /db_xref="taxon:559292"
                     /chromosome="XIV"
     Protein         1..2233
                     /product="acetyl-CoA carboxylase ACC1"
                     /EC_number="6.3.4.14"
                     /EC_number="6.4.1.2"
                     /calculated_mol_wt=250223
     Region          59..570
                     /region_name="AccC"
                     /note="Biotin carboxylase [Lipid transport and
                     metabolism]; COG0439"
                     /db_xref="CDD:223516"
     Region          622..769
                     /region_name="AccB"
                     /note="Biotin carboxyl carrier protein [Coenzyme transport
                     and metabolism, Lipid transport and metabolism]; COG0511"
                     /db_xref="CDD:223585"
     Region          768..1479
                     /region_name="ACC_central"
                     /note="Acetyl-CoA carboxylase, central region; pfam08326"
                     /db_xref="CDD:429920"
     Region          1574..2118
                     /region_name="Carboxyl_trans"
                     /note="Carboxyl transferase domain; pfam01039"
                     /db_xref="CDD:426008"
     CDS             1..2233
                     /gene="ACC1"
                     /locus_tag="YNR016C"
                     /gene_synonym="ABP2; FAS3; MTR7"
                     /coded_by="NM_001183193.1:1..6702"
                     /experiment="EXISTENCE:direct assay:GO:0005739
                     mitochondrion [PMID:14576278|PMID:16823961]"
                     /experiment="EXISTENCE:direct assay:GO:0005789 endoplasmic
                     reticulum membrane [PMID:9438137]"
                     /experiment="EXISTENCE:direct assay:GO:0005829 cytosol
                     [PMID:26928762]"
                     /experiment="EXISTENCE:mutant phenotype:GO:0003989
                     acetyl-CoA carboxylase activity [PMID:8098706]"
                     /experiment="EXISTENCE:mutant phenotype:GO:0004075 biotin
                     carboxylase activity [PMID:6108218]"
                     /experiment="EXISTENCE:mutant phenotype:GO:0006606 protein
                     import into nucleus [PMID:12730220]"
                     /experiment="EXISTENCE:mutant phenotype:GO:0042759
                     long-chain fatty acid biosynthetic process [PMID:6103540]"
                     /note="Acetyl-CoA carboxylase, biotin containing enzyme;
                     catalyzes carboxylation of cytosolic acetyl-CoA to form
                     malonyl-CoA and regulates histone acetylation by
                     regulating the availability of acetyl-CoA; rate-limiting
                     step for de novo biosynthesis of long-chain fatty acids;
                     translational regulation in response to nutrients and cell
                     cycle stage depends on its upstream ORF; ACC1 has a
                     paralog, HFA1, that arose from the whole genome
                     duplication"
                     /db_xref="GeneID:855750"
                     /db_xref="SGD:S000005299"
ORIGIN      
        1 mseeslfess pqkmeyeitn yserhtelpg hfiglntvdk leesplrdfv kshgghtvis
       61 kilianngia avkeirsvrk wayetfgddr tvqfvamatp edleanaeyi rmadqyievp
      121 ggtnnnnyan vdlivdiaer advdavwagw ghasenpllp eklsqskrkv ifigppgnam
      181 rslgdkisst ivaqsakvpc ipwsgtgvdt vhvdektglv svdddiyqkg cctspedglq
      241 kakrigfpvm ikaseggggk girqvereed fialyhqaan eipgspifim klagrarhle
      301 vqlladqygt nislfgrdcs vqrrhqkiie eapvtiakae tfhemekaav rlgklvgyvs
      361 agtveylysh ddgkfyflel nprlqvehpt temvsgvnlp aaqlqiamgi pmhrisdirt
      421 lygmnphsas eidfefktqd atkkqrrpip kghctacrit sedpndgfkp sggtlhelnf
      481 rsssnvwgyf svgnngnihs fsdsqfghif afgenrqasr khmvvalkel sirgdfrttv
      541 eylikllete dfedntittg wlddlithkm taekpdptla vicgaatkaf laseearhky
      601 ieslqkgqvl skdllqtmfp vdfihegkry kftvaksgnd rytlfingsk cdiilrqlsd
      661 gglliaiggk shtiywkeev aatrlsvdsm ttllevendp tqlrtpspgk lvkflvenge
      721 hiikgqpyae ievmkmqmpl vsqengivql lkqpgstiva gdimaimtld dpskvkhalp
      781 fegmlpdfgs pviegtkpay kfkslvstle nilkgydnqv imnaslqqli evlrnpklpy
      841 sewklhisal hsrlpaklde qmeelvarsl rrgavfparq lsklidmavk npeynpdkll
      901 gavvepladi ahkysnglea hehsifvhfl eeyyeveklf ngpnvreeni ilklrdenpk
      961 dldkvaltvl shskvsaknn lilailkhyq plcklsskvs aifstplqhi veleskatak
     1021 valqareili qgalpsvker teqiehilks svvkvaygss npkrsepdln ilkdlidsny
     1081 vvfdvllqfl thqdpvvtaa aaqvyirray raytigdirv hegvtvpive wkfqlpsaaf
     1141 stfptvkskm gmnravsvsd lsyvansqss plregilmav dhlddvdeil sqsleviprh
     1201 qsssngpapd rsgssaslsn vanvcvaste gfeseeeilv rlreildlnk qelinasirr
     1261 itfmfgfkdg sypkyytfng pnynenetir hiepalafql elgrlsnfni kpiftdnrni
     1321 hvyeavskts pldkrfftrg iirtghirdd isiqeyltse anrlmsdild nlevtdtsns
     1381 dlnhifinfi avfdispedv eaafggfler fgkrllrlrv ssaeiriiik dpqtgapvpl
     1441 ralinnvsgy viktemytev knakgewvfk slgkpgsmhl rpiatpypvk ewlqpkryka
     1501 hlmgttyvyd fpelfrqass sqwknfsadv kltddffisn eliedengel teverepgan
     1561 aigmvafkit vktpeyprgr qfvvvandit fkigsfgpqe deffnkvtey arkrgipriy
     1621 laansgarig maeeivplfq vawndaanpd kgfqylylts egmetlkkfd kensvltert
     1681 vingeerfvi ktiigsedgl gveclrgsgl iagatsrayh diftitlvtc rsvgigaylv
     1741 rlgqraiqve gqpiiltgap ainkmlgrev ytsnlqlggt qimynngvsh ltavddlagv
     1801 ekivewmsyv pakrnmpvpi letkdtwdrp vdftptndet ydvrwmiegr etesgfeygl
     1861 fdkgsffetl sgwakgvvvg rarlggiplg vigvetrtve nlipadpanp nsaetliqep
     1921 gqvwhpnsaf ktaqaindfn ngeqlpmmil anwrgfsggq rdmfnevlky gsfivdalvd
     1981 ykqpiiiyip ptgelrggsw vvvdptinad qmemyadvna ragvlepqgm vgikfrrekl
     2041 ldtmnrlddk yrelrsqlsn kslapevhqq iskqladrer ellpiygqis lqfadlhdrs
     2101 srmvakgvis kelewtearr fffwrlrrrl neeylikrls hqvgeasrle kiarirswyp
     2161 asvdheddrq vatwieenyk tlddklkglk lesfaqdlak kirsdhdnai dglsevikml
     2221 stddkekllk tlk
//
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