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P36189

- FAS_ANSAN

UniProt

P36189 - FAS_ANSAN

Protein

Fatty acid synthase

Gene

FASN

Organism
Anser anser anser (Western graylag goose)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 65 (01 Oct 2014)
      Sequence version 1 (01 Jun 1994)
      Previous versions | rss
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    Functioni

    Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. This multifunctional protein has seven 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+.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei161 – 1611For beta-ketoacyl synthase activityPROSITE-ProRule annotation

    GO - Molecular functioni

    1. fatty acid synthase activity Source: UniProtKB-EC
    2. hydrolase activity Source: UniProtKB-KW
    3. ligase activity Source: UniProtKB-KW
    4. oxidoreductase activity Source: UniProtKB-KW

    GO - Biological processi

    1. fatty acid biosynthetic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase, Ligase, Oxidoreductase, 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
    OrganismiAnser anser anser (Western graylag goose)
    Taxonomic identifieri8844 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeAnseriformesAnatidaeAnser

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – ›352›352Fatty acid synthasePRO_0000180272Add
    BLAST

    Keywords - PTMi

    Phosphopantetheine

    Proteomic databases

    PRIDEiP36189.

    Expressioni

    Inductioni

    By triiodothyronine.

    Interactioni

    Subunit structurei

    Homodimer which monomers are arranged in a head to tail fashion.

    Structurei

    3D structure databases

    ProteinModelPortaliP36189.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – ›352›352Beta-ketoacyl synthaseAdd
    BLAST

    Family and domain databases

    Gene3Di3.40.47.10. 2 hits.
    InterProiIPR018201. Ketoacyl_synth_AS.
    IPR014031. Ketoacyl_synth_C.
    IPR014030. Ketoacyl_synth_N.
    IPR016039. Thiolase-like.
    IPR016038. Thiolase-like_subgr.
    [Graphical view]
    PfamiPF00109. ketoacyl-synt. 1 hit.
    PF02801. Ketoacyl-synt_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF53901. SSF53901. 1 hit.
    PROSITEiPS00606. B_KETOACYL_SYNTHASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Fragment.

    P36189-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEDVVIAGIA GKLPESENLQ EFWEKLLNGV DMVTEDDRRW KPGMYGLPKR    50
    NGKLKDISKF DASFFGVHPK QAHTMDPQLR LLLEVSYEAI LDGGINPATL 100
    RGTDTGVWVG ASGSEAGEAF SQDPEQLLGY SMIGCQRAMF ANRISYFYDF 150
    KGPSLSIDTA CSSSLMALEN AYKAIRNGRC SAAVVGGVNL LLKPNTSVQF 200
    MKLGMLSPDG ACKVFDASGD GYCRSEAVVV VLLTKKSMAK RIYATIVNAG 250
    SNTDGFKEQG VTFPSGDMQR QLVSSLHREC GIKPGDIEYV ETHGTGTKVG 300
    DPQEVNGLAD LFCQCEREPL LIGSTKSNMG HPEPASGLAA LAKVVLSLEH 350
    GL 352
    Length:352
    Mass (Da):37,912
    Last modified:June 1, 1994 - v1
    Checksum:i908530BF76762335
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei352 – 3521

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M60622 mRNA. Translation: AAA49316.1.
    PIRiA39042.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M60622 mRNA. Translation: AAA49316.1 .
    PIRi A39042.

    3D structure databases

    ProteinModelPortali P36189.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi P36189.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 3.40.47.10. 2 hits.
    InterProi IPR018201. Ketoacyl_synth_AS.
    IPR014031. Ketoacyl_synth_C.
    IPR014030. Ketoacyl_synth_N.
    IPR016039. Thiolase-like.
    IPR016038. Thiolase-like_subgr.
    [Graphical view ]
    Pfami PF00109. ketoacyl-synt. 1 hit.
    PF02801. Ketoacyl-synt_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53901. SSF53901. 1 hit.
    PROSITEi PS00606. B_KETOACYL_SYNTHASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and partial characterization of the gene for goose fatty acid synthase."
      Kameda K., Goodridge A.G.
      J. Biol. Chem. 266:419-426(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    2. "Specific modification of the condensation domain of fatty acid synthase and the determination of the primary structure of the modified active site peptides."
      Pouloe A.J., Bonsall R.F., Kolattukudy P.E.
      Arch. Biochem. Biophys. 230:117-128(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 152-173.

    Entry informationi

    Entry nameiFAS_ANSAN
    AccessioniPrimary (citable) accession number: P36189
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: June 1, 1994
    Last modified: October 1, 2014
    This is version 65 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

    Direct protein sequencing, Multifunctional enzyme

    External Data

    Dasty 3