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Q2KIA4

- SCD5_BOVIN

UniProt

Q2KIA4 - SCD5_BOVIN

Protein

Stearoyl-CoA desaturase 5

Gene

SCD5

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 65 (01 Oct 2014)
      Sequence version 1 (07 Mar 2006)
      Previous versions | rss
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    Functioni

    Fatty acid delta(9)-desaturase that introduces a double bond in fatty acyl-coenzyme A at the delta 9 position.By similarity

    Catalytic activityi

    Stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O.

    Cofactori

    Iron.By similarity

    GO - Molecular functioni

    1. iron ion binding Source: InterPro
    2. stearoyl-CoA 9-desaturase activity Source: UniProtKB-EC

    GO - Biological processi

    1. fatty acid biosynthetic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

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

    Keywords - Ligandi

    Iron, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Stearoyl-CoA desaturase 5 (EC:1.14.19.1)
    Alternative name(s):
    Acyl-CoA-desaturase 4
    Stearoyl-CoA 9-desaturase
    Gene namesi
    Name:SCD5
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Chromosome 6

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    2. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 335335Stearoyl-CoA desaturase 5PRO_0000312652Add
    BLAST

    Proteomic databases

    PRIDEiQ2KIA4.

    Expressioni

    Tissue specificityi

    Detected in brain.1 Publication

    Interactioni

    Protein-protein interaction databases

    STRINGi9913.ENSBTAP00000025820.

    Structurei

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei55 – 7521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei78 – 9821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei199 – 21921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei228 – 24720HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi99 – 1046Histidine box-1By similarity
    Motifi136 – 1405Histidine box-2By similarity
    Motifi277 – 2815Histidine box-3By similarity

    Domaini

    The histidine box domains may contain the active site and/or be involved in metal ion binding.By similarity

    Sequence similaritiesi

    Belongs to the fatty acid desaturase family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG1398.
    GeneTreeiENSGT00530000063158.
    HOGENOMiHOG000270352.
    HOVERGENiHBG003367.
    InParanoidiQ2KIA4.
    KOiK00507.
    OMAiAAYFCFL.
    OrthoDBiEOG7ZPNKS.
    TreeFamiTF313251.

    Family and domain databases

    InterProiIPR005804. Fatty_acid_desaturase-1.
    IPR001522. Fatty_acid_desaturase-1_C.
    IPR015876. Fatty_acid_desaturase-1_core.
    [Graphical view]
    PfamiPF00487. FA_desaturase. 1 hit.
    [Graphical view]
    PRINTSiPR00075. FACDDSATRASE.
    PROSITEiPS00476. FATTY_ACID_DESATUR_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q2KIA4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPGPAVDAEK VPFRSAKEEI RAGVGVEGSE GGGGGGGRER PGARGHRQDI    50
    VWRNVFLMSL LHLAAVYSLV LIPKAQPLTL LWAYFCFLLT ALGVTAGAHR 100
    LWSHRSYKAK LPLRIFLAAA NSMAFQNDIF EWSRDHRVHH KYSETDADPH 150
    NARRGFFFSH IGWLFVRKHR DVIEKGRKLD VTDLLADPVV RFQRKYYKIT 200
    VVLMCFVVPT LVPWYIWGES LWNSYFLASI LRYTISLNVT WLVNSVAHMY 250
    GNRPYDKHIS PRQNPLVTLG AIGEGFHNYH HTFPFDYSAS EFGLNFNPTT 300
    WFIDFMCWLG LATDRKRATK QMIEARKART GDGSA 335
    Length:335
    Mass (Da):38,215
    Last modified:March 7, 2006 - v1
    Checksum:i32F8B2C60533AB31
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    EF014951 mRNA. Translation: ABJ99757.1.
    BC112711 mRNA. Translation: AAI12712.1.
    RefSeqiNP_001070413.1. NM_001076945.1.
    UniGeneiBt.13249.

    Genome annotation databases

    EnsembliENSBTAT00000025820; ENSBTAP00000025820; ENSBTAG00000022449.
    GeneIDi617419.
    KEGGibta:617419.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    EF014951 mRNA. Translation: ABJ99757.1 .
    BC112711 mRNA. Translation: AAI12712.1 .
    RefSeqi NP_001070413.1. NM_001076945.1.
    UniGenei Bt.13249.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9913.ENSBTAP00000025820.

    Proteomic databases

    PRIDEi Q2KIA4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSBTAT00000025820 ; ENSBTAP00000025820 ; ENSBTAG00000022449 .
    GeneIDi 617419.
    KEGGi bta:617419.

    Organism-specific databases

    CTDi 79966.

    Phylogenomic databases

    eggNOGi COG1398.
    GeneTreei ENSGT00530000063158.
    HOGENOMi HOG000270352.
    HOVERGENi HBG003367.
    InParanoidi Q2KIA4.
    KOi K00507.
    OMAi AAYFCFL.
    OrthoDBi EOG7ZPNKS.
    TreeFami TF313251.

    Miscellaneous databases

    NextBioi 20900654.

    Family and domain databases

    InterProi IPR005804. Fatty_acid_desaturase-1.
    IPR001522. Fatty_acid_desaturase-1_C.
    IPR015876. Fatty_acid_desaturase-1_core.
    [Graphical view ]
    Pfami PF00487. FA_desaturase. 1 hit.
    [Graphical view ]
    PRINTSi PR00075. FACDDSATRASE.
    PROSITEi PS00476. FATTY_ACID_DESATUR_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification and characterization of a novel bovine stearoyl-CoA desaturase isoform with homology to human SCD5."
      Lengi A.J., Corl B.A.
      Lipids 42:499-508(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    2. NIH - Mammalian Gene Collection (MGC) project
      Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Hereford.
      Tissue: Hypothalamus.

    Entry informationi

    Entry nameiSCD5_BOVIN
    AccessioniPrimary (citable) accession number: Q2KIA4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 4, 2007
    Last sequence update: March 7, 2006
    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

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3