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P08757

- FAS_CAPHI

UniProt

P08757 - FAS_CAPHI

Protein

Fatty acid synthase

Gene

FASN

Organism
Capra hircus (Goat)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
  1. 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

    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

    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

    MGLRPDGIIG HSLGEVARAY YNGRISQEEA ILSAY                   35
    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

    PIRi S07131.

    3D structure databases

    ProteinModelPortali P08757.
    SMRi P08757. Positions 1-35.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 3.40.366.10. 1 hit.
    InterProi IPR001227. Ac_transferase_dom.
    IPR014043. Acyl_transferase.
    IPR016035. Acyl_Trfase/lysoPLipase.
    [Graphical view ]
    Pfami PF00698. Acyl_transf_1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52151. SSF52151. 1 hit.
    ProtoNeti Search...

    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: October 1, 2014
    This is version 71 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