Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P08757 (FAS_CAPHI) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
Fatty acid synthase

EC=2.3.1.85
Gene names
Name:FASN
Synonyms:FAS
OrganismCapra hircus (Goat)
Taxonomic identifier9925 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeCaprinaeCapra

Protein attributes

Sequence length35 AA.
Sequence statusFragment.
Protein existenceInferred from homology

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.

This fragment is from the acyltransferase domain of the fatty acid synthetase.

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.

Ontologies

Keywords
   Biological processFatty acid biosynthesis
Fatty acid metabolism
Lipid biosynthesis
Lipid metabolism
   Cellular componentCytoplasm
   LigandNAD
NADP
   Molecular functionHydrolase
Transferase
   Technical termMultifunctional enzyme
Gene Ontology (GO)
   Biological_processfatty acid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentmelanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionfatty acid synthase activity

Inferred from electronic annotation. Source: UniProtKB-EC

hydrolase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – ›35›35Fatty acid synthase
PRO_0000180275

Sites

Active site121

Experimental info

Non-terminal residue11
Non-terminal residue351

Sequences

Sequence LengthMass (Da)Tools
P08757 [UniParc].

Last modified October 1, 1993. Version 2.
Checksum: 401BEF8B4ABE562D

FASTA353,808
        10         20         30 
MGLRPDGIIG HSLGEVARAY YNGRISQEEA ILSAY 

« Hide

References

[1]"Amino acid sequence around the active-site serine residue in the acyltransferase domain of goat mammary fatty acid synthetase."
Mikkelsen J., Hoejrup P., Rasmussen M.M., Roepstorff P., Knudsen J.
Biochem. J. 227:21-27(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.

Cross-references

Sequence databases

PIRS07131.

3D structure databases

ProteinModelPortalP08757.
SMRP08757. Positions 1-35.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.40.366.10. 1 hit.
InterProIPR001227. Ac_transferase_dom.
IPR014043. Acyl_transferase.
IPR016035. Acyl_Trfase/lysoPLipase.
[Graphical view]
PfamPF00698. Acyl_transf_1. 1 hit.
[Graphical view]
SUPFAMSSF52151. SSF52151. 1 hit.
ProtoNetSearch...

Entry information

Entry nameFAS_CAPHI
AccessionPrimary (citable) accession number: P08757
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: October 1, 1993
Last modified: February 19, 2014
This is version 70 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program