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Protein

Fatty acid synthase

Gene

FASN

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

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.

Catalytic activityi

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

GO - Molecular functioni

  1. fatty acid synthase activity Source: UniProtKB-EC

GO - Biological processi

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

Keywords - Molecular functioni

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
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
ProteomesiUP000001811: Unplaced

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 – ›64›64Fatty acid synthasePRO_0000180278Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei38 – 381O-(pantetheine 4'-phosphoryl)serine1 PublicationPROSITE-ProRule annotation

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

Interactioni

Subunit structurei

Homodimer which is arranged in a head to tail fashion.

Structurei

3D structure databases

ProteinModelPortaliP07855.
SMRiP07855. Positions 1-64.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 6460Acyl carrierPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 acyl carrier domain.PROSITE-ProRule annotation

Phylogenomic databases

InParanoidiP07855.

Family and domain databases

Gene3Di1.10.1200.10. 1 hit.
InterProiIPR009081. Acyl_carrier_prot-like.
IPR006162. Ppantetheine_attach_site.
[Graphical view]
PfamiPF00550. PP-binding. 1 hit.
[Graphical view]
SUPFAMiSSF47336. SSF47336. 1 hit.
PROSITEiPS50075. ACP_DOMAIN. 1 hit.
PS00012. PHOSPHOPANTETHEINE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

P07855-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
AEGEGQRDLL KAVAHILGIR DLAGINLDSS LADLGLDSLM GVEVRQTLER
60
EHDLVLSMRE VRQL
Length:64
Mass (Da):7,037
Last modified:August 1, 1988 - v1
Checksum:i7CECE99D8A76B42D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11
Non-terminal residuei64 – 641

Sequence databases

PIRiS07221.

Cross-referencesi

Sequence databases

PIRiS07221.

3D structure databases

ProteinModelPortaliP07855.
SMRiP07855. Positions 1-64.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

InParanoidiP07855.

Family and domain databases

Gene3Di1.10.1200.10. 1 hit.
InterProiIPR009081. Acyl_carrier_prot-like.
IPR006162. Ppantetheine_attach_site.
[Graphical view]
PfamiPF00550. PP-binding. 1 hit.
[Graphical view]
SUPFAMiSSF47336. SSF47336. 1 hit.
PROSITEiPS50075. ACP_DOMAIN. 1 hit.
PS00012. PHOSPHOPANTETHEINE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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, PHOSPHOPANTETHEINYLATION AT SER-38.

Entry informationi

Entry nameiFAS_RABIT
AccessioniPrimary (citable) accession number: P07855
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: January 7, 2015
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Multifunctional enzyme, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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.