Reviewed,
UniProtKB/Swiss-Prot P12785 (FAS_RAT)
Last modified
November 25, 2008.
Version 94.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Fatty acid synthase EC=2.3.1.85 Including the following 7 domains: 1- Recommended name: [Acyl-carrier-protein] S-acetyltransferase EC=2.3.1.38 2- Recommended name: [Acyl-carrier-protein] S-malonyltransferase EC=2.3.1.39 3- Recommended name: 3-oxoacyl-[acyl-carrier-protein] synthase EC=2.3.1.41 4- Recommended name: 3-oxoacyl-[acyl-carrier-protein] reductase EC=1.1.1.100 5- Recommended name: 3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase EC=4.2.1.61 6- Recommended name: Enoyl-[acyl-carrier-protein] reductase EC=1.3.1.10 7- Recommended name: Oleoyl-[acyl-carrier-protein] hydrolase EC=3.1.2.14 | ||
| Gene names |
| ||
| Organism | Rattus norvegicus (Rat) | ||
| Taxonomic identifier | 10116 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus |
Protein attributes
| Sequence length | 2505 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| 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 CO(2) + 2n NADP(+). Acetyl-CoA + [acyl-carrier-protein] = CoA + acetyl-[acyl-carrier-protein]. Malonyl-CoA + [acyl-carrier-protein] = CoA + malonyl-[acyl-carrier-protein]. Acyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = 3-oxoacyl-[acyl-carrier-protein] + CO(2) + [acyl-carrier-protein]. (3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP(+) = 3-oxoacyl-[acyl-carrier-protein] + NADPH. (3R)-3-hydroxypalmitoyl-[acyl-carrier-protein] = hexadec-2-enoyl-[acyl-carrier-protein] + H(2)O. Acyl-[acyl-carrier-protein] + NADP(+) = trans-2,3-dehydroacyl-[acyl-carrier-protein] + NADPH. Oleoyl-[acyl-carrier-protein] + H(2)O = [acyl-carrier-protein] + oleate. |
| Subunit structure | Homodimer which is arranged in a head to tail fashion. |
| Subcellular location | CytoplasmBy similarity. MelanosomeBy similarity. |
| Induction | Up-regulated in livers of rats fed on a high carbohydrate diet. |
| Sequence similarities | Contains 1 acyl carrier domain. |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 2505 | 2505 | Fatty acid synthase | PRO_0000180279 | |||||||||||||||||||||||
Regions | |||||||||||||||||||||||||||
| Domain | 2118 – 2174 | 57 | Acyl carrier | ||||||||||||||||||||||||
| Nucleotide binding | 1665 – 1682 | 18 | NADP (ER) | ||||||||||||||||||||||||
| Nucleotide binding | 1765 – 1780 | 16 | NADP (KR) | ||||||||||||||||||||||||
| Region | 1 – 413 | 413 | Beta-ketoacyl synthase | ||||||||||||||||||||||||
| Region | 429 – 817 | 389 | Acyl and malonyl transferases | ||||||||||||||||||||||||
| Region | 1629 – 1857 | 229 | Enoyl reductase | ||||||||||||||||||||||||
| Region | 1858 – 2113 | 256 | Beta-ketoacyl reductase | ||||||||||||||||||||||||
| Region | 2202 – 2505 | 304 | Thioesterase | ||||||||||||||||||||||||
Sites | |||||||||||||||||||||||||||
| Active site | 161 | 1 | For beta-ketoacyl synthase activity By similarity | ||||||||||||||||||||||||
| Active site | 581 | 1 | For malonyltransferase activity By similarity | ||||||||||||||||||||||||
| Active site | 878 | 1 | For beta-hydroxyacyl dehydratase activity By similarity | ||||||||||||||||||||||||
| Active site | 2302 | 1 | For thioesterase activity By similarity | ||||||||||||||||||||||||
| Active site | 2475 | 1 | For thioesterase activity By similarity | ||||||||||||||||||||||||
| Binding site | 1698 | 1 | Pyridoxal phosphate (covalent) By similarity | ||||||||||||||||||||||||
| Binding site | 2151 | 1 | Phosphopantetheine (covalent) By similarity | ||||||||||||||||||||||||
Amino acid modifications | |||||||||||||||||||||||||||
| Modified residue | 1 | 1 | N-acetylmethionine By similarity | ||||||||||||||||||||||||
| Modified residue | 207 | 1 | Phosphoserine By similarity | ||||||||||||||||||||||||
| Modified residue | 2230 | 1 | Phosphoserine By similarity | ||||||||||||||||||||||||
Experimental info | |||||||||||||||||||||||||||
| Sequence conflict | 184 | 1 | I → T in AAA41145. Ref.3 | ||||||||||||||||||||||||
| Sequence conflict | 871 | 1 | S → P in CAA31780. Ref.4 | ||||||||||||||||||||||||
| Sequence conflict | 1967 – 1968 | 2 | MV → IL Ref.6 | ||||||||||||||||||||||||
| Sequence conflict | 2085 | 1 | C → P in AAA41144. Ref.5 | ||||||||||||||||||||||||
| Sequence conflict | 2106 | 1 | A → V Ref.1 Ref.3 Ref.6 | ||||||||||||||||||||||||
| Sequence conflict | 2296 | 1 | Y → H Ref.1 Ref.6 | ||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||
| Helix | 2122 – 2124 | 3 | |||||||||||||||||||||||||
| Helix | 2126 – 2130 | 5 | |||||||||||||||||||||||||
| Beta strand | 2140 – 2142 | 3 | |||||||||||||||||||||||||
| Helix | 2144 – 2147 | 4 | |||||||||||||||||||||||||
| Helix | 2152 – 2164 | 13 | |||||||||||||||||||||||||
| Helix | 2171 – 2174 | 4 | |||||||||||||||||||||||||
| Helix | 2180 – 2184 | 5 | |||||||||||||||||||||||||
| Beta strand | 2188 – 2190 | 3 | |||||||||||||||||||||||||
| Beta strand | 2192 – 2194 | 3 | |||||||||||||||||||||||||
Sequences
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References
| [1] | "Molecular cloning and sequencing of cDNAs encoding the entire rat fatty acid synthase." Amy C.M., Witkowski A., Naggert J., Williams B., Randhawa Z., Smith S. Proc. Natl. Acad. Sci. U.S.A. 86:3114-3118(1989) [PubMed: 2717611] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. |
| [2] | "The fatty acid synthase (FAS) gene and its promoter in Rattus norvegicus." Beck K.F., Schreglmann R., Stathopulos I., Klein H., Hoch J., Schweizer M. DNA Seq. 2:359-386(1992) [PubMed: 1339331] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: Sprague-Dawley. Tissue: Liver. |
| [3] | "Intron-exon organization of the gene for the multifunctional animal fatty acid synthase." Amy C.M., Williams-Ahlf B., Naggert J., Smith S. Proc. Natl. Acad. Sci. U.S.A. 89:1105-1108(1992) [PubMed: 1736293] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [4] | "Rat mammary gland fatty acid synthase: localization of the constituent domains and two functional polyadenylation/termination signals in the cDNA." Schweizer M., Takabeyashi K., Beck K.F., Schreglmann R. Nucleic Acids Res. 17:567-586(1989) [PubMed: 2915923] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 75-2505. Strain: Sprague-Dawley. Tissue: Mammary gland. |
| [5] | "Molecular cloning and sequencing of a cDNA encoding the thioesterase domain of the rat fatty acid synthetase." Naggert J., Witkowski A., Mikkelsen J., Smith S. J. Biol. Chem. 263:1146-1150(1988) [PubMed: 2891707] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2085-2505. Tissue: Mammary gland. |
| [6] | "Molecular cloning and sequencing of a cDNA encoding the acyl carrier protein and its flanking domains in the mammalian fatty acid synthetase." Witlowski A., Naggert J., Mikkelsen J., Smith S. Eur. J. Biochem. 165:601-606(1987) [PubMed: 3109907] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 1921-2324. Tissue: Mammary gland. |
| [7] | "Nutritional control of rat liver fatty acid synthase and S14 mRNA abundance." Clarke S.D., Armstrong M.K., Jump D.B. J. Nutr. 120:218-224(1990) [PubMed: 2313386] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 2377-2413, INDUCTION. |
| [8] | "The type I rat fatty acid synthase ACP shows structural homology and analogous biochemical properties to type II ACPs." Reed M.A.C., Schweizer M., Szafranska A.E., Arthur C., Nicholson T.P., Cox R.J., Crosby J., Crump M.P., Simpson T.J. Org. Biomol. Chem. 1:463-471(2003) [PubMed: 12926246] [Abstract] Cited for: STRUCTURE BY NMR OF 2114-2202. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| M76767 mRNA. Translation: AAA57219.1. X62888 mRNA. Translation: CAA44679.1. X62889 Genomic DNA. Translation: CAA44680.1. M84761 Genomic DNA. Translation: AAA41145.1. X13415 mRNA. Translation: CAA31780.1. X13527 mRNA. Translation: CAA31882.1. J03514 mRNA. Translation: AAA41144.1. | |||||||||||||||||||
| PIR | XYRTFA. A30313. | ||||||||||||||||||
| RefSeq | NP_059028.1. | ||||||||||||||||||
| UniGene | Rn.9486 | ||||||||||||||||||
3D structure databases | |||||||||||||||||||
| |||||||||||||||||||
| SMR | P12785. Positions 2211-2496. | ||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||
| IntAct | P12785. | ||||||||||||||||||
Genome annotation databases | |||||||||||||||||||
| GeneID | 50671. | ||||||||||||||||||
| KEGG | rno:50671. | ||||||||||||||||||
Organism-specific databases | |||||||||||||||||||
| RGD | 620665. Fasn. | ||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||
| HOVERGEN | P12785. | ||||||||||||||||||
Family and domain databases | |||||||||||||||||||
| InterPro | IPR001227. Ac_transferase_reg. IPR009081. ACP_like. IPR014043. Acyl_transferase. IPR013149. AlcDHase_Zn-bd. IPR002198. DHase_sc/Rdtase_SDR. IPR000794. Ketoacyl_synth. IPR014031. Ketoacyl_synth_C. IPR014030. Ketoacyl_synth_N. IPR013217. Methyltransf_12. IPR016040. NAD(P)-bd. IPR006163. Phsphopanteth_bd. IPR006162. Ppantne_S. IPR001031. Thioesterase. IPR016038. Thiolase-like_subgr. [Graphical view] | ||||||||||||||||||
| Gene3D | G3DSA:3.40.366.10. Ac_transferase_reg. 1 hit. G3DSA:1.10.1200.10. ACP_like. 1 hit. G3DSA:3.40.50.720. NAD(P)-bd. 2 hits. G3DSA:3.40.47.10. Thiolase-like_subgr. 2 hits. | ||||||||||||||||||
| PANTHER | PTHR11712. Ketoacyl_synth. 1 hit. | ||||||||||||||||||
| Pfam | PF00698. Acyl_transf_1. 1 hit. PF00106. adh_short. 1 hit. PF00107. ADH_zinc_N. 1 hit. PF00109. ketoacyl-synt. 1 hit. PF02801. Ketoacyl-synt_C. 1 hit. PF08242. Methyltransf_12. 1 hit. PF00550. PP-binding. 1 hit. PF00975. Thioesterase. 1 hit. [Graphical view] | ||||||||||||||||||
| PROSITE | PS50075. ACP_DOMAIN. 1 hit. PS00606. B_KETOACYL_SYNTHASE. 1 hit. PS00012. PHOSPHOPANTETHEINE. 1 hit. [Graphical view] | ||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||
Other Resources | |||||||||||||||||||
| NextBio | 610498. | ||||||||||||||||||
Entry information
| Entry name | FAS_RAT | ||||||||
| Accession | Primary (citable) accession number: P12785 Secondary accession number(s): O09187 Q64717 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| UniProtKB secondary accession numbers Index of UniProtKB secondary accession numbers |
| SIMILARITY comments Index of protein domains and families |

Clusters with


