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Database: UniProt
Entry: Q9TTS3
LinkDB: Q9TTS3
Original site: Q9TTS3 
ID   ACACA_BOVIN             Reviewed;        2346 AA.
AC   Q9TTS3;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   16-JAN-2019, entry version 133.
DE   RecName: Full=Acetyl-CoA carboxylase 1;
DE            Short=ACC1;
DE            EC=6.4.1.2;
DE   AltName: Full=ACC-alpha;
DE   Includes:
DE     RecName: Full=Biotin carboxylase;
DE              EC=6.3.4.14;
GN   Name=ACACA; Synonyms=ACAC, ACCA;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=11485560; DOI=10.1042/0264-6021:3580127;
RA   Mao J., Marcos S., Davis S.K., Burzlaff J., Seyfert H.-M.;
RT   "Genomic distribution of three promoters of the bovine gene encoding
RT   acetyl-CoA carboxylase alpha and evidence that the nutritionally
RT   regulated promoter I contains a repressive element different from that
RT   in rat.";
RL   Biochem. J. 358:127-135(2001).
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:0000250|UniProtKB:Q13085}.
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:0000250|UniProtKB:Q13085};
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:0000250|UniProtKB:Q13085};
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000250|UniProtKB:O00763};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 2 manganese ions per subunit. {ECO:0000250};
CC   -!- ACTIVITY REGULATION: By phosphorylation (By similarity). Activity
CC       is increased by oligomerization. Citrate and MID1IP1 promote
CC       oligomerization (By similarity). {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- PTM: Phosphorylation on Ser-1263 is required for interaction with
CC       BRCA1. {ECO:0000250}.
DR   EMBL; AJ132890; CAB56826.1; -; mRNA.
DR   RefSeq; NP_776649.1; NM_174224.2.
DR   UniGene; Bt.88312; -.
DR   ProteinModelPortal; Q9TTS3; -.
DR   SMR; Q9TTS3; -.
DR   STRING; 9913.ENSBTAP00000023364; -.
DR   PaxDb; Q9TTS3; -.
DR   PeptideAtlas; Q9TTS3; -.
DR   PRIDE; Q9TTS3; -.
DR   GeneID; 281590; -.
DR   KEGG; bta:281590; -.
DR   CTD; 31; -.
DR   eggNOG; KOG0368; Eukaryota.
DR   eggNOG; COG0439; LUCA.
DR   eggNOG; COG0511; LUCA.
DR   eggNOG; COG4799; LUCA.
DR   HOGENOM; HOG000214115; -.
DR   HOVERGEN; HBG005371; -.
DR   InParanoid; Q9TTS3; -.
DR   KO; K11262; -.
DR   OrthoDB; 156081at2759; -.
DR   UniPathway; UPA00655; UER00711.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006084; P:acetyl-CoA metabolic process; ISS:UniProtKB.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; ISS:UniProtKB.
DR   GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
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   2: Evidence at transcript level;
KW   Acetylation; Allosteric enzyme; ATP-binding; Biotin;
KW   Complete proteome; Cytoplasm; Fatty acid biosynthesis;
KW   Fatty acid metabolism; Ligase; Lipid biosynthesis; Lipid metabolism;
KW   Manganese; Metal-binding; Multifunctional enzyme; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN         1   2346       Acetyl-CoA carboxylase 1.
FT                                /FTId=PRO_0000146763.
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:0000250|UniProtKB:Q13085}.
FT   MOD_RES       5      5       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q13085}.
FT   MOD_RES      23     23       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q13085}.
FT   MOD_RES      25     25       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q13085}.
FT   MOD_RES      29     29       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q13085}.
FT   MOD_RES      34     34       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P11497}.
FT   MOD_RES      48     48       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q13085}.
FT   MOD_RES      50     50       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P11497}.
FT   MOD_RES      53     53       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q13085}.
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; by AMPK.
FT                                {ECO:0000250|UniProtKB:Q5SWU9}.
FT   MOD_RES     610    610       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q13085}.
FT   MOD_RES     786    786       N6-biotinyllysine. {ECO:0000250,
FT                                ECO:0000255|PROSITE-ProRule:PRU01066}.
FT   MOD_RES     835    835       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q13085}.
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:0000250|UniProtKB:Q13085}.
FT   MOD_RES    1273   1273       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q13085}.
FT   MOD_RES    1334   1334       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q13085}.
FT   MOD_RES    2153   2153       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q13085}.
SQ   SEQUENCE   2346 AA;  265303 MW;  32886C5D03EEAE0E CRC64;
     MDEPSSLAKP LELNQHSRFI IGSVSEDNSE DEISNLVKLD LLEEKEGSLS PASVSSDTLS
     DLGISSLQDG LALHMRSSMS GLHLVKQGRD RKKIDSQRDF TVASPAEFVT RFGGNKVIEK
     VLIANNGIAA VKCMRSIRRW SYEMFRNERA IRFVVMVTPE DLKANAEYIK MADHYVPVPG
     GPNNNNYANV ELILDIAKRI PVQAVWAGWG HASENPKLPE LLLKNGIAFM GPPSQAMWAL
     GDKIASSIVA QTAGIPTLPW SGSGLCVDWH ENDFSKRILN VPQELYEKGY VKDVDDGLKA
     AEEVGYPVMI KASEGGGGKG IRKVNNADDF PNLFRQVQAE VPGSPIFVMR LAKQSRHLEV
     QILADQYGNA ISLFGRDCSV QRRHQKIIEE APAAIATPAV FEHMEQCAVK LARMVGYVSA
     GTVEYLYSQD GSFYFLELNP RLQVEHPCTE MVADVNLPAA QLQIAMGIPL YRIKDIRMMY
     GVSPWGDAPI DFENSAHVPC PRGHVIAARI TSENPDEGFK PSSGTVQELN FRSNKNVWGY
     FSVAAAGGLH EFADSQFGHC FSWGENREEA ISNMVVALKE LSIRGDFRTT VEYLIKLLET
     ESFQLNRIGT GWLDRLIAEK VQAERPDTML GVVCGALHVA DVSLRNSISN FLHSLERGQV
     LTAHTLLNTV DVELIYEGVK YVLKVTRQSP NSYVVIMNGS CVEVDVHRLS DGGLLLSYDV
     SSYTTYMKEE VDRYRITIGN KTCVFEKEND PSVLRSPSAG KLIQYIVEDG GHVFAGQCYA
     EIEVMKMVMT LTAAESGCIH YVKRPGAALD PGCVIAKMQL DNPSKVQQAE LHTGSLPRIQ
     STALRGEKLH RVFHYVLDNL VNVMNGYCLP DPFFSSRVKD WVERLMKTLR DPSLPLLELQ
     DIMTSVSGRI PPNVEKSIKK EMAQYASNIT SVLCQFPSQQ IANILDSHAA TLNRKSEREV
     FFMNTQSIVQ LVQRYRSGIR GHMKAVVMDL LRQYLRVETQ FQNGHYDKCV FALREENKSD
     MNTVLNYIFS HAQVTRKNLL VTMLIDQLCG RGPTLTDELL NILTELTQLS KTTNAKVALR
     ARQVLIASHL PSYELRLNQV ESIFLSAIDM YGHQFCIENL QKLILSETSI FDVLPNFFYH
     SNQVVRMAAL EVYVRRAYIA YELNSVQHRQ LKDNTCVVEF QFMLPTSHPN RGNIPTLNRM
     SFSSNLNHYG MTHVASVSDV LLDNAFTPPC QRMGGMVSFR TFEDFVRIFD EVMGCFCDSP
     PQSPTFPEAG HTSLYDEDKV PRDEPIHILN VAIKTDCDIE DDSLAAMFRE FTQQNKATLV
     EHGIRRLTFL VAQKDFRKQV NYEVDQRFHR EFPKFFTFRA RDKFEEDRIY RHLEPALAFQ
     LELNRMRNFD LTAIPCANHK MHLYLGAAKV EVGTEVTDYR FFVRAIIRHS DLVTKEASFE
     YLQNEGERLL LEAMDELEVA FNNTNVRTDC NHIFLNFVPT VIMDPSKIEE SVRSMVMRYG
     SRLWKLRVLQ AELKINIRLT PTGKAIPIRL FLTNESGYYL DISLYKEVTD SRTAQIMFQA
     YGDKQGPLHG MLINTPYVTK DQLQSKRFQA QSLGTTYIYD IPEMFRQSLI KLWESMSSQA
     FLPPPPLPSD ILTYTELVLD DQGQLVHMNR LPGGNEIGMV AWKMTLKSPE YPDGRDIIVI
     GNDITYRIGS FGPQEDLLFL RASELARAEG IPRIYVAANS GARIGLAEEI RHMFHVAWVD
     PEDPYKGYKY LYLTPQDYKR VSALNSVHCE HVEDEGESRY KITDIIGKEE GLGAENLRGS
     GMIAGESSLA YDEIITISLV TCRAIGIGAY LVRLGQRTIQ VENSHLILTG AGALNKVLGR
     EVYTSNNQLG GIQIMHNNGV THSTVCDDFE GVFTVLHWLS YMPKSVYSSV PLLNSKDPID
     RVIEFVPTKA PYDPRWMLAG RPHPTQKGQW LSGFFDYGSF SEIMQPWAQT VVVGRARLGG
     IPVGVVAVET RTVELSIPAD PANLDSEAKI IQQAGQVWFP DSAFKTYQAI KDFNREGLPL
     MVFANWRGFS GGMKDMYDQV LKFGAYIVDG LRECSQPVMV YIPPQAELRG GSWVVIDPTI
     NPRHMEMYAD RESRGSVLEP EGTVEIKFRR KDLVKTMRRV DPVYIHLAER LGTPELSVAE
     RKELESKLKE REEFLLPIYH QVAVQFADLH DTPGRMQEKG VINDILDWKT SRTFFYWRLR
     RLLLEDLVKK KIHNANPELT DGQIQAMLRR WFVEVEGTVK AYVWDNNKDL VEWLEKQLTE
     EDGVRSVIEE NIKYISRDYV LKQIRSLVQA NPEVAMDSIV HMTQHISPTQ RAEVVRILST
     MDSPST
//
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