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Q5SWU9 (ACACA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acetyl-CoA carboxylase 1

Short name=ACC1
EC=6.4.1.2
Alternative name(s):
ACC-alpha
Acetyl-CoA carboxylase 265

Including the following 1 domains:

  1. Biotin carboxylase
    EC=6.3.4.14
Gene names
Name:Acaca
Synonyms:Acac, Gm738
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length2345 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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 By similarity. Ref.10 UniProtKB P11497

Catalytic activity

ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA. Ref.10 UniProtKB P11497

ATP + biotin-[carboxyl-carrier-protein] + CO2 = ADP + phosphate + carboxy-biotin-[carboxyl-carrier-protein]. Ref.10

Cofactor

Biotin By similarity.

Binds 2 manganese ions per subunit By similarity.

Enzyme regulation

By phosphorylation By similarity. Activity is increased by oligomerization. Citrate and MID1IP1 promote oligomerization. Ref.10 UniProtKB P11497

Pathway

Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1.

Subunit structure

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. Ref.6 Ref.10

Subcellular location

Cytoplasm Ref.6 Ref.10.

Post-translational modification

Phosphorylation on Ser-1262 is required for interaction with BRCA1 By similarity. UniProtKB Q13085

Sequence similarities

Contains 1 ATP-grasp domain.

Contains 1 biotin carboxylation domain.

Contains 1 biotinyl-binding domain.

Contains 1 carboxyltransferase domain.

Ontologies

Keywords
   Biological processFatty acid biosynthesis
Fatty acid metabolism
Lipid biosynthesis
Lipid metabolism
   Cellular componentCytoplasm
   Coding sequence diversityAlternative promoter usage
   LigandATP-binding
Biotin
Manganese
Metal-binding
Nucleotide-binding
   Molecular functionLigase
   PTMAcetylation
Phosphoprotein
   Technical termAllosteric enzyme
Complete proteome
Direct protein sequencing
Multifunctional enzyme
Reference proteome
Gene Ontology (GO)
   Biological_processacetyl-CoA metabolic process

Inferred from direct assay Ref.10. Source: UniProtKB

fatty acid biosynthetic process

Inferred from direct assay Ref.10. Source: UniProtKB

lipid homeostasis

Inferred from mutant phenotype PubMed 17210641. Source: MGI

lipid metabolic process

Inferred from mutant phenotype PubMed 17210641. Source: MGI

malonyl-CoA biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

multicellular organismal protein metabolic process

Inferred from mutant phenotype PubMed 17210641. Source: MGI

protein homotetramerization

Inferred from direct assay Ref.10. Source: UniProtKB

tissue homeostasis

Inferred from mutant phenotype PubMed 17210641. Source: MGI

   Cellular_componentcytosol

Inferred from direct assay Ref.10. Source: UniProtKB

mitochondrion

Inferred from direct assay PubMed 18614015. Source: MGI

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

acetyl-CoA carboxylase activity

Inferred from direct assay Ref.10. Source: UniProtKB

biotin carboxylase activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative promoter usage. [Align] [Select]
Isoform 1 (identifier: Q5SWU9-1)

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.
Isoform 2 (identifier: Q5SWU9-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 23452345Acetyl-CoA carboxylase 1
PRO_0000258040

Regions

Domain116 – 617502Biotin carboxylation
Domain274 – 465192ATP-grasp
Domain751 – 81767Biotinyl-binding
Domain1697 – 2193497Carboxyltransferase
Nucleotide binding300 – 35758ATP Potential

Sites

Active site4401 By similarity
Metal binding4231Manganese 1 By similarity
Metal binding4361Manganese 1 By similarity
Metal binding4361Manganese 2 By similarity
Metal binding4381Manganese 2 By similarity
Binding site18221Coenzyme A By similarity UniProtKB Q00955
Binding site21261Coenzyme A By similarity UniProtKB Q00955
Binding site21281Coenzyme A By similarity UniProtKB Q00955

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue51Phosphoserine By similarity
Modified residue231Phosphoserine By similarity
Modified residue251Phosphoserine Ref.7
Modified residue291Phosphoserine Ref.7 Ref.8 UniProtKB Q13085
Modified residue521Phosphoserine By similarity
Modified residue771Phosphoserine By similarity UniProtKB P11497
Modified residue791Phosphoserine; alternate Ref.8 Ref.9 Ref.10 UniProtKB P11497
Modified residue791Phosphoserine; by AMPK; alternate Probable
Modified residue7851N6-biotinyllysine By similarity
Modified residue12001Phosphoserine By similarity UniProtKB P11497
Modified residue12151Phosphoserine By similarity
Modified residue12621Phosphoserine By similarity UniProtKB Q13085
Modified residue13331N6-acetyllysine By similarity

Natural variations

Alternative sequence11M → MMWWSTLMSLLRASSFWRRI SAETIRIIRALRAYFERIM in isoform 2.
VSP_026101

Experimental info

Sequence conflict6231E → G in AAS13685. Ref.1
Sequence conflict9061S → P in AAS13685. Ref.1
Sequence conflict9331C → Y in AAS13685. Ref.1
Sequence conflict14561L → S in AAS13685. Ref.1
Sequence conflict19951S → G in AAS13685. Ref.1
Sequence conflict20771V → I in AAS13685. Ref.1
Sequence conflict21691E → K in AAS13685. Ref.1
Sequence conflict22511F → S in AAS13685. Ref.1
Sequence conflict22571T → A in AAS13685. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 6995C534B054FE02

FASTA2,345265,257
        10         20         30         40         50         60 
MDEPSPLAKT LELNQHSRFI IGSVSEDNSE DEISNLVKLD LEEKEGSLSP ASVSSDTLSD 

        70         80         90        100        110        120 
LGISGLQDGL AFHMRSSMSG LHLVKQGRDR KKIDSQRDFT VASPAEFVTR FGGNKVIEKV 

       130        140        150        160        170        180 
LIANNGIAAV KCMRSIRRWS YEMFRNERAI RFVVMVTPED LKANAEYIKM ADHYVPVPGG 

       190        200        210        220        230        240 
PNNNNYANVE LILDIAKRIP VQAVWAGWGH ASENPKLPEL LLKNGIAFMG PPSQAMWALG 

       250        260        270        280        290        300 
DKIASSIVAQ TAGIPTLPWS GSGLRVDWQE NDFSKRILNV PQDLYEKGYV KDVDDGLKAA 

       310        320        330        340        350        360 
EEVGYPVMIK ASEGGGGKGI RKVNNADDFP NLFRQVQAEV PGSPIFVMRL AKQSRHLEVQ 

       370        380        390        400        410        420 
ILADQYGNAI SLFGRDCSVQ RRHQKIIEEA PAAIATPAVF EHMEQCAVKL AKMVGYVSAG 

       430        440        450        460        470        480 
TVEYLYSQDG SFYFLELNPR LQVEHPCTEM VADVNLPAAQ LQIAMGIPLF RIKDIRMMYG 

       490        500        510        520        530        540 
VSPWGDAPID FENSAHVPCP RGHVIAARIT SENPDEGFKP SSGTVQELNF RSNKNVWGYF 

       550        560        570        580        590        600 
SVAAAGGLHE FADSQFGHCF SWGENREEAI SNMVVALKEL SIRGDFRTTV EYLIKLLETE 

       610        620        630        640        650        660 
SFQLNRIDTG WLDRLIAEKV QAERPDTMLG VVCGALHVAD VSLRNSISNF LHSLERGQVL 

       670        680        690        700        710        720 
PAHTLLNTVD VELIYEGIKY VLKVTRQSPN SYVVIMNGSC VEVDVHRLSD GGLLLSYDGS 

       730        740        750        760        770        780 
SYTTYMKEEV DRYRITIGNK TCVFEKENDP SVMRSPSAGK LIQYIVEDGG HVFAGQCYAE 

       790        800        810        820        830        840 
IEVMKMVMTL TAVESGCIHY VKRPGAALDP GCVIAKMQLD NPSKVQQAEL HTGSLPQIQS 

       850        860        870        880        890        900 
TALRGEKLHR VFHYVLDNLV NVMNGYCLPD PFFSSRVKDW VERLMKTLRD PSLPLLELQD 

       910        920        930        940        950        960 
IMTSVSGRIP LNVEKSIKKE MAQYASNITS VLCQFPSQQI ANILDSHAAT LNRKSEREVF 

       970        980        990       1000       1010       1020 
FMNTQSIVQL VQRYRSGIRG HMKAVVMDLL RQYLRVETQF QNGHYDKCVF ALREENKSDM 

      1030       1040       1050       1060       1070       1080 
NTVLNYIFSH AQVTKKNLLV TMLIDQLCGR DPTLTDELLN ILTELTQLSK TTNAKVALRA 

      1090       1100       1110       1120       1130       1140 
RQVLIASHLP SYELRHNQVE SIFLSAIDMY GHQFCIENLQ KLILSETSIF DVLPNFFYHS 

      1150       1160       1170       1180       1190       1200 
NQVVRMAALE VYVRRAYIAY ELNSVQHRQL KDNTCVVEFQ FMLPTSHPNR GNIPTLNRMS 

      1210       1220       1230       1240       1250       1260 
FASNLNHYGM THVASVSDVL LDNAFTPPCQ RMGGMVSFRT FEDFVRIFDE IMGCFCDSPP 

      1270       1280       1290       1300       1310       1320 
QSPTFPESGH TSLYDEDKVP RDEPIHILNV AIKTDGDIED DRLAAMFREF TQQNKATLVE 

      1330       1340       1350       1360       1370       1380 
HGIRRLTFLV AQKDFRKQVN CEVDQRFHRE FPKFFTFRAR DKFEEDRIYR HLEPALAFQL 

      1390       1400       1410       1420       1430       1440 
ELNRMRNFDL TAIPCANHKM HLYLGAAKVE VGTEVTDYRF FVRAIIRHSD LVTKEASFEY 

      1450       1460       1470       1480       1490       1500 
LQNEGERLLL EAMDELEVAF NNTNVRTDCN HIFLNFVPTV IMDPSKIEES VRSMVMRYGS 

      1510       1520       1530       1540       1550       1560 
RLWKLRVLQA ELKINIRLTT TGKAIPIRLF LTNESGYYLD ISLYKEVTDS RTAQIMFQAY 

      1570       1580       1590       1600       1610       1620 
GDKQGPLHGM LINTPYVTKD LLQSKRFQAQ SLGTTYIYDI PEMFRQSLIK LWESMSTQAF 

      1630       1640       1650       1660       1670       1680 
LPSPPLPSDI LTYTELVLDD QGQLVHMNRL PGGNEIGMVA WKMSLKSPEY PDGRDIIVIG 

      1690       1700       1710       1720       1730       1740 
NDITYRIGSF GPQEDLLFLR ASELARAEGI PRIYVAANSG ARIGLAEEIR HMFHVAWVDP 

      1750       1760       1770       1780       1790       1800 
EDPYKGYKYL YLTPQDYKRV SALNSVHCEH VEDEGESRYK ITDIIGKEEG LGAENLRGSG 

      1810       1820       1830       1840       1850       1860 
MIAGESSLAY DEVITISLVT CRAIGIGAYL VRLGQRTIQV ENSHLILTGA GALNKVLGRE 

      1870       1880       1890       1900       1910       1920 
VYTSNNQLGG IQIMHNNGVT HSTVCDDFEG VFTVLHWLSY MPKSVHSSVP LLNSKDPIDR 

      1930       1940       1950       1960       1970       1980 
IIEFVPTKAP YDPRWMLAGR PHPTQKGQWL SGFFDYGSFS EIMQPWAQTV VVGRARLGGI 

      1990       2000       2010       2020       2030       2040 
PVGVVAVETR TVELSIPADP ANLDSEAKII QQAGQVWFPD SAFKTYQAIK DFNREGLPLM 

      2050       2060       2070       2080       2090       2100 
VFANWRGFSG GMKDMYDQVL KFGAYIVDGL RECSQPVMVY IPPQAELRGG SWVVIDPTIN 

      2110       2120       2130       2140       2150       2160 
PRHMEMYADR ESRGSVLEPE GTVEIKFRKK DLVKTMRRVD PVYIRLAERL GTPELSPTER 

      2170       2180       2190       2200       2210       2220 
KELESKLKER EEFLIPIYHQ VAVQFADLHD TPGRMQEKGV INDILDWKTS RTFFYWRLRR 

      2230       2240       2250       2260       2270       2280 
LLLEDLVKKK IHNANPELTD GQIQAMLRRW FVEVEGTVKA YVWDNNKDLV EWLEKQLTEE 

      2290       2300       2310       2320       2330       2340 
DGVRSVIEEN IKYISRDYVL KQIRSLVQAN PEVAMDSIVH MTQHISPTQR AEVVRILSTM 


DSPST 

« Hide

Isoform 2 [UniParc].

Checksum: 57B7FB88C694692E
Show »

FASTA2,383269,958

References

« Hide 'large scale' references
[1]"Characterization of the mouse acetyl-CoA carboxylase 1 (ACC1) gene and identification of an intronless pseudogene."
Mao J., Wakil S.J.
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Strain: C57BL/6J.
Tissue: Liver.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]"Asymmetric expression of transcripts derived from the shared promoter between the divergently oriented ACACA and TADA2L genes."
Travers M.T., Cambot M., Kennedy H.T., Lenoir G.M., Barber M.C., Joulin V.
Genomics 85:71-84(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1-119 (ISOFORM 2).
Strain: Swiss.
Tissue: Brain.
[4]"Acetyl-CoA carboxylase and SREBP expression during peripheral nervous system myelination."
Salles J., Sargueil F., Knoll-Gellida A., Witters L.A., Cassagne C., Garbay B.
Biochim. Biophys. Acta 1631:229-238(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-38; 1221-1348 AND 1681-1891.
Strain: C57BL/6.
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1501-2345.
Strain: C57BL/6.
Tissue: Brain.
[6]"BRCA1 interacts with acetyl-CoA carboxylase through its tandem of BRCT domains."
Magnard C., Bachelier R., Vincent A., Jaquinod M., Kieffer S., Lenoir G.M., Venezia N.D.
Oncogene 21:6729-6739(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 298-306 AND 2267-2275, INTERACTION WITH BRCA1, SUBCELLULAR LOCATION.
[7]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25 AND SER-29, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[8]"Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29 AND SER-79, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[9]"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
[10]"Crystal structure of Spot 14, a modulator of fatty acid synthesis."
Colbert C.L., Kim C.W., Moon Y.A., Henry L., Palnitkar M., McKean W.B., Fitzgerald K., Deisenhofer J., Horton J.D., Kwon H.J.
Proc. Natl. Acad. Sci. U.S.A. 107:18820-18825(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, ENZYME REGULATION, INTERACTION WITH MID1IP1, PHOSPHORYLATION AT SER-79, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_579938.2. NM_133360.2.
XP_006532016.1. XM_006531953.1.
XP_006532017.1. XM_006531954.1.
XP_006532018.1. XM_006531955.1.
XP_006532019.1. XM_006531956.1.
XP_006532020.1. XM_006531957.1.
UniGeneMm.31374.

3D structure databases

ProteinModelPortalQ5SWU9.
SMRQ5SWU9. Positions 101-615, 747-816, 1580-2337.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid223322. 1 interaction.
DIPDIP-32276N.
IntActQ5SWU9. 8 interactions.
MINTMINT-4091386.

Chemistry

ChEMBLCHEMBL3086.

PTM databases

PhosphoSiteQ5SWU9.

Proteomic databases

PaxDbQ5SWU9.
PRIDEQ5SWU9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000020843; ENSMUSP00000020843; ENSMUSG00000020532. [Q5SWU9-1]
ENSMUST00000103201; ENSMUSP00000099490; ENSMUSG00000020532. [Q5SWU9-1]
ENSMUST00000133811; ENSMUSP00000116174; ENSMUSG00000020532.
GeneID107476.
KEGGmmu:107476.
UCSCuc007kql.1. mouse. [Q5SWU9-1]

Organism-specific databases

CTD31.
MGIMGI:108451. Acaca.

Phylogenomic databases

eggNOGCOG0511.
GeneTreeENSGT00550000074703.
HOVERGENHBG005371.
InParanoidQ5SWU9.
KOK11262.
OMAETESFQM.
OrthoDBEOG7HXCPW.
PhylomeDBQ5SWU9.
TreeFamTF300061.

Enzyme and pathway databases

UniPathwayUPA00655; UER00711.

Gene expression databases

ArrayExpressQ5SWU9.
BgeeQ5SWU9.
CleanExMM_ACACA.
GenevestigatorQ5SWU9.

Family and domain databases

Gene3D3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
InterProIPR013537. AcCoA_COase_cen.
IPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR001882. Biotin_BS.
IPR011764. Biotin_carboxylation_dom.
IPR005482. Biotin_COase_C.
IPR000089. Biotin_lipoyl.
IPR005481. CarbamoylP_synth_lsu_N.
IPR000022. Carboxyl_trans.
IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
IPR011763. COA_CT_C.
IPR011762. COA_CT_N.
IPR016185. PreATP-grasp_dom.
IPR011054. Rudment_hybrid_motif.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamPF08326. ACC_central. 1 hit.
PF02785. Biotin_carb_C. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF01039. Carboxyl_trans. 1 hit.
PF00289. CPSase_L_chain. 1 hit.
PF02786. CPSase_L_D2. 1 hit.
[Graphical view]
SMARTSM00878. Biotin_carb_C. 1 hit.
[Graphical view]
SUPFAMSSF51230. SSF51230. 1 hit.
SSF51246. SSF51246. 1 hit.
SSF52440. SSF52440. 1 hit.
PROSITEPS50975. 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.
[Graphical view]
ProtoNetSearch...

Other

NextBio358872.
PROQ5SWU9.
SOURCESearch...

Entry information

Entry nameACACA_MOUSE
AccessionPrimary (citable) accession number: Q5SWU9
Secondary accession number(s): A2A6H4 expand/collapse secondary AC list , Q5SWU6, Q5SWU7, Q5SWU8, Q6JIZ1, Q6PHL9, Q705X8, Q705X9, Q91VC8, Q925C4, Q925C5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: December 21, 2004
Last modified: April 16, 2014
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot