Q5SWU9 (ACACA_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 92.
History...
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Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended 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:
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| Gene names |
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| Organism | Mus musculus (Mouse) [Reference proteome] | ||||
| Taxonomic identifier | 10090 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus |
Protein attributes
| Sequence length | 2345 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence 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.13 UniProtKB P11497 |
| Catalytic activity | ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA. Ref.13 UniProtKB P11497 ATP + biotin-[carboxyl-carrier-protein] + CO2 = ADP + phosphate + carboxy-biotin-[carboxyl-carrier-protein]. Ref.13 |
| 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.13 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.13 |
| Subcellular location | |
| 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
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 key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 2345 | 2345 | Acetyl-CoA carboxylase 1 | PRO_0000258040 | |||||
Regions | |||||||||
| Domain | 116 – 617 | 502 | Biotin carboxylation | ||||||
| Domain | 274 – 465 | 192 | ATP-grasp | ||||||
| Domain | 751 – 817 | 67 | Biotinyl-binding | ||||||
| Domain | 1697 – 2193 | 497 | Carboxyltransferase | ||||||
| Nucleotide binding | 300 – 357 | 58 | ATP Potential | ||||||
Sites | |||||||||
| Active site | 440 | 1 | By similarity | ||||||
| Metal binding | 423 | 1 | Manganese 1 By similarity | ||||||
| Metal binding | 436 | 1 | Manganese 1 By similarity | ||||||
| Metal binding | 436 | 1 | Manganese 2 By similarity | ||||||
| Metal binding | 438 | 1 | Manganese 2 By similarity | ||||||
| Binding site | 1822 | 1 | Coenzyme A By similarity UniProtKB Q00955 | ||||||
| Binding site | 2126 | 1 | Coenzyme A By similarity UniProtKB Q00955 | ||||||
| Binding site | 2128 | 1 | Coenzyme A By similarity UniProtKB Q00955 | ||||||
Amino acid modifications | |||||||||
| Modified residue | 1 | 1 | N-acetylmethionine By similarity | ||||||
| Modified residue | 5 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 23 | 1 | Phosphoserine Ref.9 | ||||||
| Modified residue | 25 | 1 | Phosphoserine Ref.9 | ||||||
| Modified residue | 29 | 1 | Phosphoserine Ref.7 Ref.9 Ref.10 Ref.11 UniProtKB Q13085 | ||||||
| Modified residue | 47 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 52 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 77 | 1 | Phosphoserine By similarity UniProtKB P11497 | ||||||
| Modified residue | 79 | 1 | Phosphoserine; by AMPK Probable UniProtKB P11497 | ||||||
| Modified residue | 785 | 1 | N6-biotinyllysine By similarity | ||||||
| Modified residue | 1200 | 1 | Phosphoserine By similarity UniProtKB P11497 | ||||||
| Modified residue | 1215 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1262 | 1 | Phosphoserine By similarity UniProtKB Q13085 | ||||||
| Modified residue | 1333 | 1 | N6-acetyllysine By similarity | ||||||
Natural variations | |||||||||
| Alternative sequence | 1 | 1 | M → MMWWSTLMSLLRASSFWRRI SAETIRIIRALRAYFERIM in isoform 2. | VSP_026101 | |||||
Experimental info | |||||||||
| Sequence conflict | 623 | 1 | E → G in AAS13685. Ref.1 | ||||||
| Sequence conflict | 906 | 1 | S → P in AAS13685. Ref.1 | ||||||
| Sequence conflict | 933 | 1 | C → Y in AAS13685. Ref.1 | ||||||
| Sequence conflict | 1456 | 1 | L → S in AAS13685. Ref.1 | ||||||
| Sequence conflict | 1995 | 1 | S → G in AAS13685. Ref.1 | ||||||
| Sequence conflict | 2077 | 1 | V → I in AAS13685. Ref.1 | ||||||
| Sequence conflict | 2169 | 1 | E → K in AAS13685. Ref.1 | ||||||
| Sequence conflict | 2251 | 1 | F → S in AAS13685. Ref.1 | ||||||
| Sequence conflict | 2257 | 1 | T → A in AAS13685. Ref.1 | ||||||
Sequences
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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.  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] | "Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry." Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R. J. Proteome Res. 6:250-262(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29, MASS SPECTROMETRY. Tissue: Liver. |
| [8] | "Mitochondrial phosphoproteome revealed by an improved IMAC method and MS/MS/MS." Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y. Mol. Cell. Proteomics 6:669-676(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, MASS SPECTROMETRY. Tissue: Liver. |
| [9] | "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-23; SER-25 AND SER-29, MASS SPECTROMETRY. Tissue: Liver. |
| [10] | "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, MASS SPECTROMETRY. Tissue: Liver. |
| [11] | "Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29 AND SER-79, MASS SPECTROMETRY. Tissue: Melanoma. |
| [12] | "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, MASS SPECTROMETRY. Tissue: Embryonic fibroblast. |
| [13] | "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. |
| IPI | IPI00474783. IPI00848443. |
| RefSeq | NP_579938.2. NM_133360.2. |
| UniGene | Mm.31374. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1W96 based on UniProtKB Q00955. |
| ProteinModelPortal | Q5SWU9. |
| SMR | Q5SWU9. Positions 101-615, 747-816, 1580-2337. |
| ModBase | Search... |
Protein-protein interaction databases | |
| DIP | DIP-32276N. |
| IntAct | Q5SWU9. 5 interactions. |
PTM databases | |
| PhosphoSite | Q5SWU9. |
Proteomic databases | |
| PaxDb | Q5SWU9. |
| PRIDE | Q5SWU9. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSMUST00000020843; ENSMUSP00000020843; ENSMUSG00000020532. ENSMUST00000103201; ENSMUSP00000099490; ENSMUSG00000020532. ENSMUST00000130012; ENSMUSP00000117972; ENSMUSG00000020532. ENSMUST00000133811; ENSMUSP00000116174; ENSMUSG00000020532. ENSMUST00000136463; ENSMUSP00000116295; ENSMUSG00000020532. ENSMUST00000137500; ENSMUSP00000121274; ENSMUSG00000020532. |
| GeneID | 107476. |
| KEGG | mmu:107476. |
| UCSC | uc007kql.1. mouse. |
Organism-specific databases | |
| CTD | 31. |
| MGI | MGI:108451. Acaca. |
Phylogenomic databases | |
| eggNOG | COG0511. |
| GeneTree | ENSGT00550000074703. |
| HOVERGEN | HBG005371. |
| InParanoid | Q5SWU9. |
| KO | K11262. |
| OMA | ETESFQM. |
| OrthoDB | EOG4X0MRD. |
Enzyme and pathway databases | |
| UniPathway | UPA00655; UER00711. |
Gene expression databases | |
| ArrayExpress | Q5SWU9. |
| Bgee | Q5SWU9. |
| CleanEx | MM_ACACA. |
| Genevestigator | Q5SWU9. |
| GermOnline | ENSMUSG00000020532. Mus musculus. |
Family and domain databases | |
| Gene3D | 3.30.1490.20. 1 hit. 3.30.470.20. 1 hit. 3.40.50.20. 1 hit. |
| InterPro | IPR013537. 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] |
| Pfam | PF08326. 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] |
| SMART | SM00878. Biotin_carb_C. 1 hit. [Graphical view] |
| SUPFAM | SSF51230. Hybrid_motif. 1 hit. SSF52440. PreATP-grasp-like. 1 hit. SSF51246. Rudmnt_hyb_motif. 1 hit. |
| 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. [Graphical view] |
| ProtoNet | Search... |
Other | |
| ChEMBL | CHEMBL3086. |
| NextBio | 358872. |
| SOURCE | Search... |
Entry information
| Entry name | ACACA_MOUSE | ||||||||
| Accession | Primary (citable) accession number: Q5SWU9 Secondary accession number(s): A2A6H4 Q925C5 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |