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O02858

- ACOD_PIG

UniProt

O02858 - ACOD_PIG

Protein

Acyl-CoA desaturase

Gene

SCD

Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 87 (01 Oct 2014)
      Sequence version 1 (01 Jul 1997)
      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.

    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
    OrganismiSus scrofa (Pig)
    Taxonomic identifieri9823 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
    ProteomesiUP000008227: Unplaced

    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
    Chaini‹1 – ›334›334Acyl-CoA desaturasePRO_0000185399Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei192 – 1921PhosphoserineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Structurei

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini‹1 – 60›60CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini83 – 919LumenalSequence Analysis
    Topological domaini109 – 20597CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini225 – 23915LumenalSequence AnalysisAdd
    BLAST
    Topological domaini263 – ›334›72CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei61 – 8222HelicalSequence AnalysisAdd
    BLAST
    Transmembranei92 – 10817HelicalSequence AnalysisAdd
    BLAST
    Transmembranei206 – 22419HelicalSequence AnalysisAdd
    BLAST
    Transmembranei240 – 26223HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi109 – 1146Histidine box-1
    Motifi146 – 1505Histidine box-2
    Motifi287 – 2915Histidine 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

    eggNOGiCOG1398.
    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: Fragment.

    O02858-1 [UniParc]FASTAAdd to Basket

    « Hide

    SSYTTTTTIT APSSRVLQNG GGKSEKTPQY VEEDIRPEMK DDIYDPTYQD    50
    KEGPQGKLEY VWRNIILMSL LHLGALYGII LIPTCKIYTL LWAFAYYLLS 100
    AVGVTAGAHR LWSHRTYKAR LPLRVFLIIA NTMAFQNDVY EWARDHRAHH 150
    KFSETDADPH NSRRGFFFSH VGWLLVRKHP AVKEKGGLLN MSDLKAEKLV 200
    MFQRRYYKPG ILLMCFILPT IVPWYCWGEA FPQSLFVATF LRYAIVLNAT 250
    WLVNSAAHLY GYRPYDKTIS PRENILVSLG AVGEGFHNYH HTFPYDYSAS 300
    EYRWHINLTT FFIDCMAALG LAYDRKKVSK AAIL 334
    Length:334
    Mass (Da):38,482
    Last modified:July 1, 1997 - v1
    Checksum:i79183E3918469977
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei1 – 11
    Non-terminal residuei334 – 3341

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z97186 mRNA. Translation: CAB10004.1.
    UniGeneiSsc.16159.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z97186 mRNA. Translation: CAB10004.1 .
    UniGenei Ssc.16159.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi COG1398.
    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. Fumiere O.
      Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].

    Entry informationi

    Entry nameiACOD_PIG
    AccessioniPrimary (citable) accession number: O02858
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: July 1, 1997
    Last modified: October 1, 2014
    This is version 87 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