Reviewed,
UniProtKB/Swiss-Prot Q28559 (ACACA_SHEEP)
Last modified
June 16, 2009.
Version 76.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Acetyl-CoA carboxylase 1 EC=6.4.1.2 Alternative name(s): ACC-alpha Including the following 1 domains: 1- Recommended name: Biotin carboxylase EC=6.3.4.14 | ||||
| Gene names |
| ||||
| Organism | Ovis aries (Sheep) | ||||
| Taxonomic identifier | 9940 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Caprinae › Ovis |
Protein attributes
| Sequence length | 2346 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at transcript 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. |
| Catalytic activity | ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA. ATP + biotin-carboxyl-carrier protein + CO2 = ADP + phosphate + carboxybiotin-carboxyl-carrier protein. |
| Cofactor | Biotin By similarity. Binds 2 manganese ions per subunit By similarity. |
| Enzyme regulation | By phosphorylation By similarity. |
| Pathway | Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. |
| Subunit structure | Interacts in its inactive phosphorylated form with the BRCT domains of BRCA1 which prevents ACACA dephosphorylation and inhibits lipid synthesis By similarity. |
| Subcellular location | |
| Tissue specificity | Isoform 2 is expressed at high levels in mammary gland. Ref.2 |
| Induction | Isoform 2 is induced in mammary gland during lactation. Ref.2 |
| Post-translational modification | Phosphorylation on Ser-1263 is required for interaction with BRCA1 By similarity. |
| Sequence similarities | Contains 1 ATP-grasp domain. Contains 1 biotin carboxylation domain. Contains 1 biotinyl-binding domain. Contains 1 carboxyltransferase domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Fatty acid biosynthesis Lipid synthesis |
| Cellular component | Cytoplasm |
| Coding sequence diversity | Alternative promoter usage |
| Ligand | ATP-binding Biotin Manganese Metal-binding Nucleotide-binding |
| Molecular function | Ligase |
| PTM | Acetylation Phosphoprotein |
| Technical term | Multifunctional enzyme |
| Gene Ontology (GO) | |
| Biological process | fatty acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW acetyl-CoA carboxylase activityInferred from electronic annotation. Source: EC biotin bindingInferred from electronic annotation. Source: InterPro biotin carboxylase activityInferred from electronic annotation. Source: EC manganese ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Alternative products
| This entry describes 3 isoforms produced by alternative promoter usage. [Align] [Select] | ||||||
| Isoform 1 (identifier: Q28559-1) 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: Q28559-2) Also known as: E5A; The sequence of this isoform differs from the canonical sequence as follows: 1-75: MGEPSSLAKP...SLQDGLALHM → MEGSAEESKEMRYYMLQ | ||||||
| Isoform 3 (identifier: Q28559-3) The sequence of this isoform differs from the canonical sequence as follows: 1-1: M → MWWSTLMSILRASSFWKWISAQTIRIIRALRARFEGTM |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 2346 | 2346 | Acetyl-CoA carboxylase 1 | PRO_0000146766 | |||||
Regions | |||||||||
| Domain | 117 – 618 | 502 | Biotin carboxylation | ||||||
| Domain | 275 – 466 | 192 | ATP-grasp | ||||||
| Domain | 752 – 818 | 67 | Biotinyl-binding | ||||||
| Domain | 1698 – 2194 | 497 | Carboxyltransferase | ||||||
| Nucleotide binding | 315 – 320 | 6 | ATP Potential | ||||||
Sites | |||||||||
| Active site | 441 | 1 | By similarity | ||||||
| Metal binding | 424 | 1 | Manganese 1 By similarity | ||||||
| Metal binding | 437 | 1 | Manganese 1 By similarity | ||||||
| Metal binding | 437 | 1 | Manganese 2 By similarity | ||||||
| Metal binding | 439 | 1 | Manganese 2 By similarity | ||||||
| Binding site | 1823 | 1 | Coenzyme A By similarity | ||||||
| Binding site | 2127 | 1 | Coenzyme A By similarity | ||||||
| Binding site | 2129 | 1 | Coenzyme A By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 1 | 1 | N-acetylmethionine By similarity | ||||||
| Modified residue | 5 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 23 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 25 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 29 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 48 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 50 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 53 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 56 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 58 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 60 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 78 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 80 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 786 | 1 | N6-biotinyllysine By similarity | ||||||
| Modified residue | 1042 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 1201 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1263 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1844 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 2108 | 1 | Phosphotyrosine By similarity | ||||||
Natural variations | |||||||||
| Alternative sequence | 1 – 75 | 75 | MGEPS…LALHM → MEGSAEESKEMRYYMLQ in isoform 2. | VSP_026102 | |||||
| Alternative sequence | 1 | 1 | M → MWWSTLMSILRASSFWKWIS AQTIRIIRALRARFEGTM in isoform 3. | VSP_026103 | |||||
Sequences
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References
| [1] | "Cloning and characterisation of multiple acetyl-CoA carboxylase transcripts in ovine adipose tissue." Barber M.C., Travers M.T. Gene 154:271-275(1995) [PubMed: 7890176] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Strain: Finn-Dorset. Tissue: Adipose tissue. |
| [2] | "Elucidation of a promoter activity that directs the expression of acetyl-CoA carboxylase alpha with an alternative N-terminus in a tissue-restricted fashion." Barber M.C., Travers M.T. Biochem. J. 333:17-25(1998) [PubMed: 9639557] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-144 (ISOFORM 2), TISSUE SPECIFICITY, INDUCTION BY LACTATION. Strain: Finn-Dorset. Tissue: Mammary gland. |
| [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: 15607423] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-93 (ISOFORM 3). Tissue: Brain. |
Cross-references
Sequence databases | |
|---|---|
| X80045 mRNA. Translation: CAA56352.1. AJ001056 mRNA. Translation: CAA04506.1. AJ564445 mRNA. Translation: CAD92090.1. | |
| RefSeq | NP_001009256.1. |
| UniGene | Oar.17311 Oar.994 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1OD4 based on UniProtKB Q00955. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 443186. |
Phylogenomic databases | |
| HOVERGEN | Q28559. |
Enzyme and pathway databases | |
| BRENDA | 6.3.4.14. 271. 6.4.1.2. 271. |
Family and domain databases | |
| InterPro | IPR013537. AcCoA_COase_cen. IPR011761. ATP-grasp. IPR013816. ATP_grasp_subdomain_2. IPR011764. BC. IPR001882. Biotin_BS. IPR005482. Biotin_COase_C. IPR000089. Biotin_lipoyl. IPR005479. CarbamoylP_synth_lsu_ATP-bd. IPR005481. CarbamoylP_synth_lsu_N. IPR000022. Carboxyl_trans. IPR011763. COA_CT_C. IPR011762. COA_CT_N. IPR013817. Pre-ATP_grasp. [Graphical view] |
| Gene3D | G3DSA:3.30.470.20. ATP_grasp_subdomain_2. 1 hit. G3DSA:3.40.50.20. Pre-ATP_grasp. 1 hit. |
| 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] |
| 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... |
Entry information
| Entry name | ACACA_SHEEP | ||||||||
| Accession | Primary (citable) accession number: Q28559 Secondary accession number(s): O62847, Q6KEV5 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


