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Acetyl-CoA carboxylase 1 (ACC1) (EC 6.4.1.2) (ACC-alpha) [Includes: Biotin carboxylase (EC 6.3.4.14)]

 ACACA_SHEEP             Reviewed;        2346 AA.
Q28559; O62847; Q6KEV5;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
22-NOV-2017, entry version 121.
RecName: Full=Acetyl-CoA carboxylase 1;
Short=ACC1;
EC=6.4.1.2;
AltName: Full=ACC-alpha;
Includes:
RecName: Full=Biotin carboxylase;
EC=6.3.4.14;
Name=ACACA; Synonyms=ACAC;
Ovis aries (Sheep).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Caprinae; Ovis.
NCBI_TaxID=9940;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=Finn-Dorset; TISSUE=Adipose tissue;
PubMed=7890176; DOI=10.1016/0378-1119(94)00871-O;
Barber M.C., Travers M.T.;
"Cloning and characterisation of multiple acetyl-CoA carboxylase
transcripts in ovine adipose tissue.";
Gene 154:271-275(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-144 (ISOFORM 2), TISSUE SPECIFICITY,
AND INDUCTION BY LACTATION.
STRAIN=Finn-Dorset; TISSUE=Mammary gland;
PubMed=9639557; DOI=10.1042/bj3330017;
Barber M.C., Travers M.T.;
"Elucidation of a promoter activity that directs the expression of
acetyl-CoA carboxylase alpha with an alternative N-terminus in a
tissue-restricted fashion.";
Biochem. J. 333:17-25(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-93 (ISOFORM 3).
TISSUE=Brain;
PubMed=15607423; DOI=10.1016/j.ygeno.2004.10.001;
Travers M.T., Cambot M., Kennedy H.T., Lenoir G.M., Barber M.C.,
Joulin V.;
"Asymmetric expression of transcripts derived from the shared promoter
between the divergently oriented ACACA and TADA2L genes.";
Genomics 85:71-84(2005).
-!- FUNCTION: Catalyzes the rate-limiting reaction in the biogenesis
of long-chain fatty acids. Carries out three functions: biotin
carboxyl carrier protein, biotin carboxylase and
carboxyltransferase. {ECO:0000250|UniProtKB:Q13085}.
-!- CATALYTIC ACTIVITY: ATP + acetyl-CoA + HCO(3)(-) = ADP + phosphate
+ malonyl-CoA. {ECO:0000250|UniProtKB:Q13085}.
-!- CATALYTIC ACTIVITY: ATP + biotin-[carboxyl-carrier-protein] +
HCO(3)(-) = ADP + phosphate + carboxy-biotin-[carboxyl-carrier-
protein]. {ECO:0000250|UniProtKB:Q13085}.
-!- 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 (By similarity). Activity is
increased by oligomerization. Citrate and MID1IP1 promote
oligomerization (By similarity). {ECO:0000250}.
-!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA
from acetyl-CoA: step 1/1.
-!- SUBUNIT: Monomer, homodimer, and homotetramer. Can form
filamentous polymers. Interacts in its inactive phosphorylated
form with the BRCT domains of BRCA1 which prevents ACACA
dephosphorylation and inhibits lipid synthesis. Interacts with
MID1IP1; interaction with MID1IP1 promotes oligomerization and
increases its activity (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative promoter usage; Named isoforms=3;
Name=1;
IsoId=Q28559-1; Sequence=Displayed;
Name=2; Synonyms=E5A;
IsoId=Q28559-2; Sequence=VSP_026102;
Name=3;
IsoId=Q28559-3; Sequence=VSP_026103;
-!- TISSUE SPECIFICITY: Isoform 2 is expressed at high levels in
mammary gland. {ECO:0000269|PubMed:9639557}.
-!- INDUCTION: Isoform 2 is induced in mammary gland during lactation.
{ECO:0000269|PubMed:9639557}.
-!- PTM: Phosphorylation on Ser-1263 is required for interaction with
BRCA1. {ECO:0000250}.
-----------------------------------------------------------------------
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EMBL; X80045; CAA56352.1; -; mRNA.
EMBL; AJ001056; CAA04506.1; -; mRNA.
EMBL; AJ564445; CAD92090.1; -; mRNA.
RefSeq; NP_001009256.1; NM_001009256.1. [Q28559-1]
UniGene; Oar.994; -.
ProteinModelPortal; Q28559; -.
SMR; Q28559; -.
PRIDE; Q28559; -.
GeneID; 443186; -.
KEGG; oas:443186; -.
CTD; 31; -.
HOVERGEN; HBG005371; -.
KO; K11262; -.
UniPathway; UPA00655; UER00711.
Proteomes; UP000002356; Unplaced.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0003989; F:acetyl-CoA carboxylase activity; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004075; F:biotin carboxylase activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006084; P:acetyl-CoA metabolic process; ISS:UniProtKB.
GO; GO:0006633; P:fatty acid biosynthetic process; ISS:UniProtKB.
GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
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_sf.
InterPro; IPR011763; COA_CT_C.
InterPro; IPR011762; COA_CT_N.
InterPro; IPR016185; PreATP-grasp_dom_sf.
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.
2: Evidence at transcript level;
Acetylation; Allosteric enzyme; Alternative promoter usage;
ATP-binding; Biotin; Complete proteome; Cytoplasm;
Fatty acid biosynthesis; Fatty acid metabolism; Ligase;
Lipid biosynthesis; Lipid metabolism; Manganese; Metal-binding;
Multifunctional enzyme; Nucleotide-binding; Phosphoprotein;
Reference proteome.
CHAIN 1 2346 Acetyl-CoA carboxylase 1.
/FTId=PRO_0000146766.
DOMAIN 117 618 Biotin carboxylation.
DOMAIN 275 466 ATP-grasp. {ECO:0000255|PROSITE-
ProRule:PRU00409}.
DOMAIN 745 819 Biotinyl-binding. {ECO:0000255|PROSITE-
ProRule:PRU01066}.
DOMAIN 1576 1914 CoA carboxyltransferase N-terminal.
{ECO:0000255|PROSITE-ProRule:PRU01136}.
DOMAIN 1918 2234 CoA carboxyltransferase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU01137}.
NP_BIND 315 320 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00409}.
REGION 1576 2234 Carboxyltransferase.
{ECO:0000255|PROSITE-ProRule:PRU01138}.
ACT_SITE 441 441 {ECO:0000250}.
METAL 424 424 Manganese 1. {ECO:0000250}.
METAL 437 437 Manganese 1. {ECO:0000250}.
METAL 437 437 Manganese 2. {ECO:0000250}.
METAL 439 439 Manganese 2. {ECO:0000250}.
BINDING 1823 1823 Coenzyme A. {ECO:0000250}.
BINDING 2127 2127 Coenzyme A. {ECO:0000250}.
BINDING 2129 2129 Coenzyme A. {ECO:0000250}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:Q13085}.
MOD_RES 5 5 Phosphoserine.
{ECO:0000250|UniProtKB:Q13085}.
MOD_RES 23 23 Phosphoserine.
{ECO:0000250|UniProtKB:Q13085}.
MOD_RES 25 25 Phosphoserine.
{ECO:0000250|UniProtKB:Q13085}.
MOD_RES 29 29 Phosphoserine.
{ECO:0000250|UniProtKB:Q13085}.
MOD_RES 34 34 Phosphoserine.
{ECO:0000250|UniProtKB:P11497}.
MOD_RES 48 48 Phosphoserine.
{ECO:0000250|UniProtKB:Q13085}.
MOD_RES 50 50 Phosphoserine.
{ECO:0000250|UniProtKB:P11497}.
MOD_RES 53 53 Phosphoserine.
{ECO:0000250|UniProtKB:Q13085}.
MOD_RES 58 58 Phosphothreonine.
{ECO:0000250|UniProtKB:Q5SWU9}.
MOD_RES 78 78 Phosphoserine.
{ECO:0000250|UniProtKB:P11497}.
MOD_RES 80 80 Phosphoserine; by AMPK.
{ECO:0000250|UniProtKB:Q5SWU9}.
MOD_RES 610 610 Phosphothreonine.
{ECO:0000250|UniProtKB:Q13085}.
MOD_RES 786 786 N6-biotinyllysine. {ECO:0000250,
ECO:0000255|PROSITE-ProRule:PRU01066}.
MOD_RES 835 835 Phosphoserine.
{ECO:0000250|UniProtKB:Q13085}.
MOD_RES 1201 1201 Phosphoserine.
{ECO:0000250|UniProtKB:P11497}.
MOD_RES 1216 1216 Phosphoserine.
{ECO:0000250|UniProtKB:P11497}.
MOD_RES 1218 1218 Phosphoserine.
{ECO:0000250|UniProtKB:Q5SWU9}.
MOD_RES 1227 1227 Phosphothreonine.
{ECO:0000250|UniProtKB:Q5SWU9}.
MOD_RES 1259 1259 Phosphoserine.
{ECO:0000250|UniProtKB:Q5SWU9}.
MOD_RES 1263 1263 Phosphoserine.
{ECO:0000250|UniProtKB:Q13085}.
MOD_RES 1273 1273 Phosphoserine.
{ECO:0000250|UniProtKB:Q13085}.
MOD_RES 1334 1334 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q13085}.
MOD_RES 2153 2153 Phosphothreonine.
{ECO:0000250|UniProtKB:Q13085}.
VAR_SEQ 1 75 MGEPSSLAKPLELNQHSRFIIGSVSEDNSEDEISNLVKLDL
LEEKEGSLSPASVSSDTLSDLGISSLQDGLALHM -> MEG
SAEESKEMRYYMLQ (in isoform 2).
{ECO:0000303|PubMed:9639557}.
/FTId=VSP_026102.
VAR_SEQ 1 1 M -> MWWSTLMSILRASSFWKWISAQTIRIIRALRARFEG
TM (in isoform 3).
{ECO:0000303|PubMed:15607423}.
/FTId=VSP_026103.
SEQUENCE 2346 AA; 265251 MW; BCA010ADF6CD24EF CRC64;
MGEPSSLAKP LELNQHSRFI IGSVSEDNSE DEISNLVKLD LLEEKEGSLS PASVSSDTLS
DLGISSLQDG LALHMRSSMS GLHLVKQGRD RKKIDSQRDF TVASPAEFVT RFGGNKVIEK
VLIANNGIAA VKCMRSIRRW SYEMFRNERA IRFVVMVTPE DLKANAEYIK MADHYVPVPG
GPNNNNYANV ELILDIARRI 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
ESFQLNRIDT GWLDRLIAEK VQAERPDTML GVVCGALHVA DVSLRNSISN FLHSLERGQV
LSAHTLLNTV DVELIYEGEK IVLKVTRQSP NSYVVIMNGS CVEVDVHRLS DGGLLLSYDG
SSYTTYMKEE VDRYRITIGN KTCVFEKEND PSVLRSPSAG KLIQYIVEDG GHVFAGQCYA
EIEVMKMVMT LTAAESGCIH YVKRPGAALD PGCVIAKMQL DNPSKVQQAE LHTGSLPRIQ
STALRGEKLH RVFHYVLDNL VNVMNGYCLP DPFFSSRVKD WVEGLMKTLR 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 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 DLLQSKRFQA 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 LGTPELSARE
RKELESKLKE REEFLLPIYH QVAVQFADLH DTPGRMQEKG VINDILDWKT SRTFFYWRLR
RLLLEDLVKK KIHNANPELT DGQIQAMLRR WFVEVEGTVK AYVWDNNKDL VEWLEKQLTE
EDGVRSVIEE NIKYISRDYV LKQIRSLVQA NPEVAMDSIV HMTQHISPTQ RAEVVRILST
MDSPST


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