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Protein

Fatty acid synthase

Gene

FASN

Organism
Capra hircus (Goat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

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 activityi

Acetyl-CoA + n malonyl-CoA + 2n NADPH = a long-chain fatty acid + (n+1) CoA + n CO2 + 2n NADP+.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei12 – 121

GO - Molecular functioni

  1. fatty acid synthase activity Source: UniProtKB-EC
  2. hydrolase activity Source: UniProtKB-KW

GO - Biological processi

  1. fatty acid biosynthetic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Transferase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Keywords - Ligandi

NAD, NADP

Names & Taxonomyi

Protein namesi
Recommended name:
Fatty acid synthase (EC:2.3.1.85)
Gene namesi
Name:FASN
Synonyms:FAS
OrganismiCapra hircus (Goat)
Taxonomic identifieri9925 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeCaprinaeCapra

Subcellular locationi

Cytoplasm By similarity. Melanosome By similarity

GO - Cellular componenti

  1. melanosome Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – ›35›35Fatty acid synthasePRO_0000180275Add
BLAST

Interactioni

Subunit structurei

Homodimer which is arranged in a head to tail fashion.

Structurei

3D structure databases

ProteinModelPortaliP08757.
SMRiP08757. Positions 1-35.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Family and domain databases

Gene3Di3.40.366.10. 1 hit.
InterProiIPR001227. Ac_transferase_dom.
IPR014043. Acyl_transferase.
IPR016035. Acyl_Trfase/lysoPLipase.
[Graphical view]
PfamiPF00698. Acyl_transf_1. 1 hit.
[Graphical view]
SUPFAMiSSF52151. SSF52151. 1 hit.

Sequencei

Sequence statusi: Fragment.

P08757-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30 
MGLRPDGIIG HSLGEVARAY YNGRISQEEA ILSAY
Length:35
Mass (Da):3,808
Last modified:October 1, 1993 - v2
Checksum:i401BEF8B4ABE562D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11
Non-terminal residuei35 – 351

Sequence databases

PIRiS07131.

Cross-referencesi

Sequence databases

PIRiS07131.

3D structure databases

ProteinModelPortaliP08757.
SMRiP08757. Positions 1-35.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di3.40.366.10. 1 hit.
InterProiIPR001227. Ac_transferase_dom.
IPR014043. Acyl_transferase.
IPR016035. Acyl_Trfase/lysoPLipase.
[Graphical view]
PfamiPF00698. Acyl_transf_1. 1 hit.
[Graphical view]
SUPFAMiSSF52151. SSF52151. 1 hit.
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiFAS_CAPHI
AccessioniPrimary (citable) accession number: P08757
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: October 1, 1993
Last modified: January 7, 2015
This is version 73 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Multifunctional enzyme

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.