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P07855

- FAS_RABIT

UniProt

P07855 - FAS_RABIT

Protein

Fatty acid synthase

Gene

FASN

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

    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

    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

    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

    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

    AEGEGQRDLL KAVAHILGIR DLAGINLDSS LADLGLDSLM GVEVRQTLER   50
    EHDLVLSMRE VRQL 64
    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

    PIRi S07221.

    3D structure databases

    ProteinModelPortali P07855.
    SMRi P07855. Positions 1-64.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 1.10.1200.10. 1 hit.
    InterProi IPR009081. Acyl_carrier_prot-like.
    IPR006162. PPantetheine_attach_site.
    [Graphical view ]
    Pfami PF00550. PP-binding. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47336. SSF47336. 1 hit.
    PROSITEi PS50075. ACP_DOMAIN. 1 hit.
    PS00012. PHOSPHOPANTETHEINE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    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: October 1, 2014
    This is version 84 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