P07855 (FAS_RABIT) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 80.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Fatty acid synthase EC=2.3.1.85 | ||
| Gene names |
| ||
| Organism | Oryctolagus cuniculus (Rabbit) [Reference proteome] | ||
| Taxonomic identifier | 9986 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus![]() |
Protein attributes
| Sequence length | 64 AA. |
| Sequence status | Fragment. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. This multifunctional protein has 7 catalytic activities and an acyl carrier protein. |
| Catalytic activity | Acetyl-CoA + n malonyl-CoA + 2n NADPH = a long-chain fatty acid + (n+1) CoA + n CO2 + 2n NADP+. |
| Subunit structure | Homodimer which is arranged in a head to tail fashion. |
| Subcellular location | Cytoplasm By similarity. Melanosome By similarity. |
| Sequence similarities | Contains 1 acyl carrier domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Fatty acid biosynthesis Fatty acid metabolism Lipid biosynthesis Lipid metabolism |
| Cellular component | Cytoplasm |
| Ligand | NAD NADP Phosphopantetheine |
| Molecular function | Transferase |
| Technical term | Complete proteome Direct protein sequencing Multifunctional enzyme Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | fatty acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular_component | melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | fatty acid synthase activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | ‹1 – ›64 | ›64 | Fatty acid synthase | PRO_0000180278 | |||||
Regions | |||||||||
| Domain | 5 – 64 | 60 | Acyl carrier | ||||||
Amino acid modifications | |||||||||
| Modified residue | 38 | 1 | O-(pantetheine 4'-phosphoryl)serine Ref.1 | ||||||
Experimental info | |||||||||
| Non-terminal residue | 1 | 1 | |||||||
| Non-terminal residue | 64 | 1 | |||||||
Sequences
References
| [1] | "The multifunctional polypeptide chain of rabbit mammary fatty acid synthase contains a domain homologous with the acyl carrier protein of Escherichia coli." McCarthy A.D., Aitken A., Hardie D.G. Eur. J. Biochem. 136:501-508(1983) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE. |
Cross-references
Sequence databases | |
|---|---|
| PIR | S07221. |
3D structure databases | |
| ProteinModelPortal | P07855. |
| SMR | P07855. Positions 1-64. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| Gene3D | 1.10.1200.10. 1 hit. |
| InterPro | IPR009081. Acyl_carrier_prot-like. IPR006162. PPantetheine_attach_site. [Graphical view] |
| Pfam | PF00550. PP-binding. 1 hit. [Graphical view] |
| SUPFAM | SSF47336. ACP_like. 1 hit. |
| PROSITE | PS50075. ACP_DOMAIN. 1 hit. PS00606. B_KETOACYL_SYNTHASE. Partial match. PS00012. PHOSPHOPANTETHEINE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | FAS_RABIT | ||||||||
| Accession | Primary (citable) accession number: P07855 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
