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Q95MI7

- ACOD_CAPHI

UniProt

Q95MI7 - ACOD_CAPHI

Protein

Acyl-CoA desaturase

Gene

SCD

Organism
Capra hircus (Goat)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 58 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      Previous versions | rss
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    Functioni

    Terminal component of the liver microsomal stearyl-CoA desaturase system, that utilizes O2 and electrons from reduced cytochrome b5 to catalyze the insertion of a double bond into a spectrum of fatty acyl-CoA substrates including palmitoyl-CoA and stearoyl-CoA.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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acyl-CoA desaturase (EC:1.14.19.1)
    Alternative name(s):
    Delta(9)-desaturase
    Short name:
    Delta-9 desaturase
    Fatty acid desaturase
    Stearoyl-CoA desaturase
    Gene namesi
    Name:SCD
    OrganismiCapra hircus (Goat)
    Taxonomic identifieri9925 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeCaprinaeCapra

    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 – 359359Acyl-CoA desaturasePRO_0000232709Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei203 – 2031PhosphoserineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Structurei

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 7171CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini94 – 1029LumenalSequence Analysis
    Topological domaini120 – 21697CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini236 – 25015LumenalSequence AnalysisAdd
    BLAST
    Topological domaini274 – 35986CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei72 – 9322HelicalSequence AnalysisAdd
    BLAST
    Transmembranei103 – 11917HelicalSequence AnalysisAdd
    BLAST
    Transmembranei217 – 23519HelicalSequence AnalysisAdd
    BLAST
    Transmembranei251 – 27323HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi120 – 1256Histidine box-1
    Motifi157 – 1615Histidine box-2
    Motifi298 – 3025Histidine box-3

    Domaini

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

    Sequence similaritiesi

    Belongs to the fatty acid desaturase family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    HOVERGENiHBG003367.

    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.

    Q95MI7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPAHLLQEEI SSSYTTTTTI TAPPSKVLQN GGGKLEKTPL YLEEDIRPEM    50
    RDDIYDPTYQ DKEGPKPKLE YVWRNIILMG LLHLGALYGI TLIPTCKIYT 100
    FLWVLFYYMM SALGITAGVH RLWSHRTYKA RLPLRVFLII ANTMAFQNDV 150
    FEWSRDHRAH HKFSETDADP HNSRRGFFFS HVGWLLVRKH PAVREKGATL 200
    DLSDLRAEKL VMFQRRYYKP GVLLLCFILP TLVPWYLWGE TFQNSLFFAT 250
    LLRYAVVLNA TWLVNSAAHM YGYRPYDKTI NPRENILVSL GAVGEGFHNY 300
    HHTFPYDYSA SEYRWHINFT TFFIDCMAAI GLAYDRKKVS KAAALARMKR 350
    TGEESCKSG 359
    Length:359
    Mass (Da):41,586
    Last modified:December 1, 2001 - v1
    Checksum:i052E5BE2B4463F88
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF339909 mRNA. Translation: AAK61862.1.
    AF422171
    , AF422167, AF422166, AF422168, AF422170, AF422169 Genomic DNA. Translation: AAL29305.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF339909 mRNA. Translation: AAK61862.1 .
    AF422171
    , AF422167 , AF422166 , AF422168 , AF422170 , AF422169 Genomic DNA. Translation: AAL29305.1 .

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    HOVERGENi HBG003367.

    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. "Partial nucleotide sequence of the goat stearoyl coenzyme A desaturase cDNA and gene structure."
      Yahyaoui M.H., Sanchez A., Folch J.M.
      J. Anim. Sci. 80:866-867(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].

    Entry informationi

    Entry nameiACOD_CAPHI
    AccessioniPrimary (citable) accession number: Q95MI7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 18, 2006
    Last sequence update: December 1, 2001
    Last modified: October 1, 2014
    This is version 58 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3