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UniProtKB - Q5SWU9 (ACACA_MOUSE)

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Protein

Acetyl-CoA carboxylase 1

Gene

Acaca

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.By similarity1 Publication

Catalytic activityi

ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA.1 Publication
ATP + biotin-[carboxyl-carrier-protein] + HCO3- = ADP + phosphate + carboxy-biotin-[carboxyl-carrier-protein].1 Publication

Cofactori

Protein has several cofactor binding sites:
  • biotinBy similarity
  • Mn2+By similarityNote: Binds 2 manganese ions per subunit.By similarity

Enzyme regulationi

By phosphorylation (By similarity). Activity is increased by oligomerization. Citrate and MID1IP1 promote oligomerization.By similarity1 Publication

Pathwayi: malonyl-CoA biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes malonyl-CoA from acetyl-CoA.
Proteins known to be involved in this subpathway in this organism are:
  1. Acetyl-CoA carboxylase 1 (Acaca), Acetyl-CoA carboxylase 2 (Acacb)
This subpathway is part of the pathway malonyl-CoA biosynthesis, which is itself part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes malonyl-CoA from acetyl-CoA, the pathway malonyl-CoA biosynthesis and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi423Manganese 1Sequence analysis1
Metal bindingi436Manganese 1Sequence analysis1
Metal bindingi436Manganese 2Sequence analysis1
Metal bindingi438Manganese 2Sequence analysis1
Active sitei440Sequence analysis1
Binding sitei1822Coenzyme ABy similarity1
Binding sitei2126Coenzyme ABy similarity1
Binding sitei2128Coenzyme ABy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi300 – 357ATPPROSITE-ProRule annotationAdd BLAST58

GO - Molecular functioni

Complete GO annotation...

GO - Biological processi

  • acetyl-CoA metabolic process Source: UniProtKB
  • cellular response to prostaglandin E stimulus Source: MGI
  • fatty acid biosynthetic process Source: UniProtKB
  • lipid homeostasis Source: MGI
  • lipid metabolic process Source: MGI
  • malonyl-CoA biosynthetic process Source: UniProtKB-UniPathway
  • multicellular organismal protein metabolic process Source: MGI
  • protein homotetramerization Source: UniProtKB
  • tissue homeostasis Source: MGI
Complete GO annotation...

Keywordsi

Molecular functionLigase
Biological processFatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism
LigandATP-binding, Biotin, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi6.4.1.2. 3474.
ReactomeiR-MMU-163765. ChREBP activates metabolic gene expression.
R-MMU-196780. Biotin transport and metabolism.
R-MMU-200425. Import of palmitoyl-CoA into the mitochondrial matrix.
R-MMU-75105. Fatty acyl-CoA biosynthesis.
UniPathwayiUPA00655; UER00711.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetyl-CoA carboxylase 1 (EC:6.4.1.21 Publication)
Short name:
ACC1
Alternative name(s):
ACC-alpha
Acetyl-CoA carboxylase 265
Including the following 1 domains:
Biotin carboxylase (EC:6.3.4.141 Publication)
Gene namesi
Name:AcacaImported
Synonyms:AcacImported, Gm738
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:108451. Acaca.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3086.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002580401 – 2345Acetyl-CoA carboxylase 1Add BLAST2345

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei5PhosphoserineBy similarity1
Modified residuei23PhosphoserineCombined sources1
Modified residuei25PhosphoserineCombined sources1
Modified residuei29PhosphoserineCombined sources1
Modified residuei34PhosphoserineBy similarity1
Modified residuei47PhosphoserineCombined sources1
Modified residuei49PhosphoserineBy similarity1
Modified residuei52PhosphoserineBy similarity1
Modified residuei57PhosphothreonineCombined sources1
Modified residuei77PhosphoserineBy similarity1
Modified residuei79PhosphoserineCombined sources1 Publication1
Modified residuei79Phosphoserine; by AMPKCombined sources1 Publication1
Modified residuei609PhosphothreonineCombined sources1
Modified residuei785N6-biotinyllysinePROSITE-ProRule annotationBy similarity1
Modified residuei834PhosphoserineBy similarity1
Modified residuei1200PhosphoserineBy similarity1
Modified residuei1215PhosphoserineCombined sources1
Modified residuei1217PhosphoserineCombined sources1
Modified residuei1226PhosphothreonineCombined sources1
Modified residuei1258PhosphoserineCombined sources1
Modified residuei1262PhosphoserineCombined sources1
Modified residuei1272PhosphoserineBy similarity1
Modified residuei1333N6-acetyllysineBy similarity1
Modified residuei2152PhosphothreonineBy similarity1

Post-translational modificationi

Phosphorylation on Ser-1262 is required for interaction with BRCA1.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ5SWU9.
PaxDbiQ5SWU9.
PeptideAtlasiQ5SWU9.
PRIDEiQ5SWU9.

PTM databases

iPTMnetiQ5SWU9.
PhosphoSitePlusiQ5SWU9.
SwissPalmiQ5SWU9.

Expressioni

Inductioni

Up-regulated by endocannabinoid anandamide/AEA.1 Publication

Gene expression databases

BgeeiENSMUSG00000020532.
CleanExiMM_ACACA.
ExpressionAtlasiQ5SWU9. baseline and differential.
GenevisibleiQ5SWU9. MM.

Interactioni

Subunit structurei

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.2 Publications

Protein-protein interaction databases

BioGridi223322. 4 interactors.
DIPiDIP-32276N.
IntActiQ5SWU9. 11 interactors.
MINTiMINT-4091386.
STRINGi10090.ENSMUSP00000020843.

Chemistry databases

BindingDBiQ5SWU9.

Structurei

3D structure databases

ProteinModelPortaliQ5SWU9.
SMRiQ5SWU9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini116 – 617Biotin carboxylationSequence analysisAdd BLAST502
Domaini274 – 465ATP-graspPROSITE-ProRule annotationAdd BLAST192
Domaini744 – 818Biotinyl-bindingPROSITE-ProRule annotationAdd BLAST75
Domaini1575 – 1913CoA carboxyltransferase N-terminalPROSITE-ProRule annotationAdd BLAST339
Domaini1917 – 2233CoA carboxyltransferase C-terminalPROSITE-ProRule annotationAdd BLAST317

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1575 – 2233CarboxyltransferasePROSITE-ProRule annotationAdd BLAST659

Phylogenomic databases

eggNOGiKOG0368. Eukaryota.
COG0439. LUCA.
COG0511. LUCA.
COG4799. LUCA.
GeneTreeiENSGT00550000074703.
HOVERGENiHBG005371.
InParanoidiQ5SWU9.
KOiK11262.
OMAiFTPPCQR.
OrthoDBiEOG091G02ND.
PhylomeDBiQ5SWU9.
TreeFamiTF300061.

Family and domain databases

Gene3Di3.30.1490.20. 1 hit.
InterProiView protein in InterPro
IPR034733. AcCoA_carboxyl.
IPR013537. AcCoA_COase_cen.
IPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR005481. BC-like_N.
IPR001882. Biotin_BS.
IPR011764. Biotin_carboxylation_dom.
IPR005482. Biotin_COase_C.
IPR000089. Biotin_lipoyl.
IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
IPR029045. ClpP/crotonase-like_dom.
IPR011763. COA_CT_C.
IPR011762. COA_CT_N.
IPR016185. PreATP-grasp_dom.
IPR011054. Rudment_hybrid_motif.
IPR011053. Single_hybrid_motif.
PfamiView protein in Pfam
PF08326. ACC_central. 1 hit.
PF02785. Biotin_carb_C. 1 hit.
PF00289. Biotin_carb_N. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF01039. Carboxyl_trans. 1 hit.
PF02786. CPSase_L_D2. 1 hit.
SMARTiView protein in SMART
SM00878. Biotin_carb_C. 1 hit.
SUPFAMiSSF51230. SSF51230. 1 hit.
SSF51246. SSF51246. 1 hit.
SSF52096. SSF52096. 2 hits.
SSF52440. SSF52440. 1 hit.
PROSITEiView protein in PROSITE
PS50975. ATP_GRASP. 1 hit.
PS50979. BC. 1 hit.
PS00188. BIOTIN. 1 hit.
PS50968. BIOTINYL_LIPOYL. 1 hit.
PS50989. COA_CT_CTER. 1 hit.
PS50980. COA_CT_NTER. 1 hit.
PS00866. CPSASE_1. 1 hit.
PS00867. CPSASE_2. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative promoter usage. AlignAdd to basket

Isoform 1 (identifier: Q5SWU9-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MDEPSPLAKT LELNQHSRFI IGSVSEDNSE DEISNLVKLD LEEKEGSLSP 
        60         70         80         90        100
ASVSSDTLSD LGISGLQDGL AFHMRSSMSG LHLVKQGRDR KKIDSQRDFT 
       110        120        130        140        150
VASPAEFVTR FGGNKVIEKV LIANNGIAAV KCMRSIRRWS YEMFRNERAI 
       160        170        180        190        200
RFVVMVTPED LKANAEYIKM ADHYVPVPGG PNNNNYANVE LILDIAKRIP 
       210        220        230        240        250
VQAVWAGWGH ASENPKLPEL LLKNGIAFMG PPSQAMWALG DKIASSIVAQ 
       260        270        280        290        300
TAGIPTLPWS GSGLRVDWQE NDFSKRILNV PQDLYEKGYV KDVDDGLKAA 
       310        320        330        340        350
EEVGYPVMIK ASEGGGGKGI RKVNNADDFP NLFRQVQAEV PGSPIFVMRL 
       360        370        380        390        400
AKQSRHLEVQ ILADQYGNAI SLFGRDCSVQ RRHQKIIEEA PAAIATPAVF 
       410        420        430        440        450
EHMEQCAVKL AKMVGYVSAG TVEYLYSQDG SFYFLELNPR LQVEHPCTEM 
       460        470        480        490        500
VADVNLPAAQ LQIAMGIPLF RIKDIRMMYG VSPWGDAPID FENSAHVPCP 
       510        520        530        540        550
RGHVIAARIT SENPDEGFKP SSGTVQELNF RSNKNVWGYF SVAAAGGLHE 
       560        570        580        590        600
FADSQFGHCF SWGENREEAI SNMVVALKEL SIRGDFRTTV EYLIKLLETE 
       610        620        630        640        650
SFQLNRIDTG WLDRLIAEKV QAERPDTMLG VVCGALHVAD VSLRNSISNF 
       660        670        680        690        700
LHSLERGQVL PAHTLLNTVD VELIYEGIKY VLKVTRQSPN SYVVIMNGSC 
       710        720        730        740        750
VEVDVHRLSD GGLLLSYDGS SYTTYMKEEV DRYRITIGNK TCVFEKENDP 
       760        770        780        790        800
SVMRSPSAGK LIQYIVEDGG HVFAGQCYAE IEVMKMVMTL TAVESGCIHY 
       810        820        830        840        850
VKRPGAALDP GCVIAKMQLD NPSKVQQAEL HTGSLPQIQS TALRGEKLHR 
       860        870        880        890        900
VFHYVLDNLV NVMNGYCLPD PFFSSRVKDW VERLMKTLRD PSLPLLELQD 
       910        920        930        940        950
IMTSVSGRIP LNVEKSIKKE MAQYASNITS VLCQFPSQQI ANILDSHAAT 
       960        970        980        990       1000
LNRKSEREVF FMNTQSIVQL VQRYRSGIRG HMKAVVMDLL RQYLRVETQF 
      1010       1020       1030       1040       1050
QNGHYDKCVF ALREENKSDM NTVLNYIFSH AQVTKKNLLV TMLIDQLCGR 
      1060       1070       1080       1090       1100
DPTLTDELLN ILTELTQLSK TTNAKVALRA RQVLIASHLP SYELRHNQVE 
      1110       1120       1130       1140       1150
SIFLSAIDMY GHQFCIENLQ KLILSETSIF DVLPNFFYHS NQVVRMAALE 
      1160       1170       1180       1190       1200
VYVRRAYIAY ELNSVQHRQL KDNTCVVEFQ FMLPTSHPNR GNIPTLNRMS 
      1210       1220       1230       1240       1250
FASNLNHYGM THVASVSDVL LDNAFTPPCQ RMGGMVSFRT FEDFVRIFDE 
      1260       1270       1280       1290       1300
IMGCFCDSPP QSPTFPESGH TSLYDEDKVP RDEPIHILNV AIKTDGDIED 
      1310       1320       1330       1340       1350
DRLAAMFREF TQQNKATLVE HGIRRLTFLV AQKDFRKQVN CEVDQRFHRE 
      1360       1370       1380       1390       1400
FPKFFTFRAR DKFEEDRIYR HLEPALAFQL ELNRMRNFDL TAIPCANHKM 
      1410       1420       1430       1440       1450
HLYLGAAKVE VGTEVTDYRF FVRAIIRHSD LVTKEASFEY LQNEGERLLL 
      1460       1470       1480       1490       1500
EAMDELEVAF NNTNVRTDCN HIFLNFVPTV IMDPSKIEES VRSMVMRYGS 
      1510       1520       1530       1540       1550
RLWKLRVLQA ELKINIRLTT TGKAIPIRLF LTNESGYYLD ISLYKEVTDS 
      1560       1570       1580       1590       1600
RTAQIMFQAY GDKQGPLHGM LINTPYVTKD LLQSKRFQAQ SLGTTYIYDI 
      1610       1620       1630       1640       1650
PEMFRQSLIK LWESMSTQAF LPSPPLPSDI LTYTELVLDD QGQLVHMNRL 
      1660       1670       1680       1690       1700
PGGNEIGMVA WKMSLKSPEY PDGRDIIVIG NDITYRIGSF GPQEDLLFLR 
      1710       1720       1730       1740       1750
ASELARAEGI PRIYVAANSG ARIGLAEEIR HMFHVAWVDP EDPYKGYKYL 
      1760       1770       1780       1790       1800
YLTPQDYKRV SALNSVHCEH VEDEGESRYK ITDIIGKEEG LGAENLRGSG 
      1810       1820       1830       1840       1850
MIAGESSLAY DEVITISLVT CRAIGIGAYL VRLGQRTIQV ENSHLILTGA 
      1860       1870       1880       1890       1900
GALNKVLGRE VYTSNNQLGG IQIMHNNGVT HSTVCDDFEG VFTVLHWLSY 
      1910       1920       1930       1940       1950
MPKSVHSSVP LLNSKDPIDR IIEFVPTKAP YDPRWMLAGR PHPTQKGQWL 
      1960       1970       1980       1990       2000
SGFFDYGSFS EIMQPWAQTV VVGRARLGGI PVGVVAVETR TVELSIPADP 
      2010       2020       2030       2040       2050
ANLDSEAKII QQAGQVWFPD SAFKTYQAIK DFNREGLPLM VFANWRGFSG 
      2060       2070       2080       2090       2100
GMKDMYDQVL KFGAYIVDGL RECSQPVMVY IPPQAELRGG SWVVIDPTIN 
      2110       2120       2130       2140       2150
PRHMEMYADR ESRGSVLEPE GTVEIKFRKK DLVKTMRRVD PVYIRLAERL 
      2160       2170       2180       2190       2200
GTPELSPTER KELESKLKER EEFLIPIYHQ VAVQFADLHD TPGRMQEKGV 
      2210       2220       2230       2240       2250
INDILDWKTS RTFFYWRLRR LLLEDLVKKK IHNANPELTD GQIQAMLRRW 
      2260       2270       2280       2290       2300
FVEVEGTVKA YVWDNNKDLV EWLEKQLTEE DGVRSVIEEN IKYISRDYVL 
      2310       2320       2330       2340 
KQIRSLVQAN PEVAMDSIVH MTQHISPTQR AEVVRILSTM DSPST
Length:2,345
Mass (Da):265,257
Last modified:December 21, 2004 - v1
Checksum:i6995C534B054FE02
GO
Isoform 2 (identifier: Q5SWU9-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MMWWSTLMSLLRASSFWRRISAETIRIIRALRAYFERIM

Show »
Length:2,383
Mass (Da):269,958
Checksum:i57B7FB88C694692E
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti623E → G in AAS13685 (Ref. 1) Curated1
Sequence conflicti906S → P in AAS13685 (Ref. 1) Curated1
Sequence conflicti933C → Y in AAS13685 (Ref. 1) Curated1
Sequence conflicti1456L → S in AAS13685 (Ref. 1) Curated1
Sequence conflicti1995S → G in AAS13685 (Ref. 1) Curated1
Sequence conflicti2077V → I in AAS13685 (Ref. 1) Curated1
Sequence conflicti2169E → K in AAS13685 (Ref. 1) Curated1
Sequence conflicti2251F → S in AAS13685 (Ref. 1) Curated1
Sequence conflicti2257T → A in AAS13685 (Ref. 1) Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0261011M → MMWWSTLMSLLRASSFWRRI SAETIRIIRALRAYFERIM in isoform 2. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY451393 mRNA. Translation: AAS13685.1.
AL596252, AL596447 Genomic DNA. Translation: CAI24019.1.
AL596447, AL596252 Genomic DNA. Translation: CAI25271.1.
AL596447 Genomic DNA. Translation: CAI25272.1.
AL596447 Genomic DNA. Translation: CAI25273.1.
AL596447 Genomic DNA. Translation: CAI25274.1.
AL596447 Genomic DNA. Translation: CAM21560.1.
AJ619664 mRNA. Translation: CAF02251.1.
AJ619665 Genomic DNA. Translation: CAF02252.1.
AF374167 mRNA. Translation: AAK57389.1.
AF374168 mRNA. Translation: AAK57390.1.
AF374169 mRNA. Translation: AAK57391.1.
AF374170 mRNA. Translation: AAK57392.1.
BC056500 mRNA. Translation: AAH56500.1.
CCDSiCCDS25185.1. [Q5SWU9-1]
RefSeqiNP_579938.2. NM_133360.2. [Q5SWU9-1]
XP_006532016.1. XM_006531953.1. [Q5SWU9-2]
XP_006532017.1. XM_006531954.2. [Q5SWU9-1]
XP_006532018.1. XM_006531955.1. [Q5SWU9-1]
XP_006532019.1. XM_006531956.2. [Q5SWU9-1]
XP_006532020.1. XM_006531957.3. [Q5SWU9-1]
XP_011246969.1. XM_011248667.1. [Q5SWU9-1]
UniGeneiMm.31374.

Genome annotation databases

EnsembliENSMUST00000020843; ENSMUSP00000020843; ENSMUSG00000020532. [Q5SWU9-1]
ENSMUST00000103201; ENSMUSP00000099490; ENSMUSG00000020532. [Q5SWU9-1]
GeneIDi107476.
KEGGimmu:107476.
UCSCiuc007kql.1. mouse. [Q5SWU9-1]

Keywords - Coding sequence diversityi

Alternative promoter usage

Similar proteinsi

Entry informationi

Entry nameiACACA_MOUSE
AccessioniPrimary (citable) accession number: Q5SWU9
Secondary accession number(s): A2A6H4
, Q5SWU6, Q5SWU7, Q5SWU8, Q6JIZ1, Q6PHL9, Q705X8, Q705X9, Q91VC8, Q925C4, Q925C5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: December 21, 2004
Last modified: August 30, 2017
This is version 134 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Direct protein sequencing, Multifunctional enzyme, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways