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P07308

- ACOD1_RAT

UniProt

P07308 - ACOD1_RAT

Protein

Acyl-CoA desaturase 1

Gene

Scd1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 2 (23 Nov 2004)
      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.

    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: RGD

    GO - Biological processi

    1. brown fat cell differentiation Source: Ensembl
    2. cholesterol esterification Source: Ensembl
    3. defense response to Gram-positive bacterium Source: Ensembl
    4. fatty acid biosynthetic process Source: RGD
    5. lipid biosynthetic process Source: RGD
    6. negative regulation of growth of symbiont in host Source: Ensembl
    7. white fat cell differentiation Source: Ensembl

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

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

    Keywords - Ligandi

    Iron

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-14123.
    BRENDAi1.14.19.1. 5301.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acyl-CoA desaturase 1 (EC:1.14.19.1)
    Alternative name(s):
    Delta(9)-desaturase 1
    Short name:
    Delta-9 desaturase 1
    Fatty acid desaturase 1
    Stearoyl-CoA desaturase 1
    Gene namesi
    Name:Scd1
    Synonyms:Scd
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 1

    Organism-specific databases

    RGDi621176. Scd1.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of endoplasmic reticulum membrane Source: RGD
    2. intracellular membrane-bounded organelle Source: RGD

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 358358Acyl-CoA desaturase 1PRO_0000185400Add
    BLAST

    Proteomic databases

    PaxDbiP07308.
    PRIDEiP07308.

    PTM databases

    PhosphoSiteiP07308.

    Expressioni

    Inductioni

    This protein is the only inducible component of this fatty acyl-CoA desaturase system.

    Gene expression databases

    ArrayExpressiP07308.
    GenevestigatoriP07308.

    Interactioni

    Protein-protein interaction databases

    BioGridi251497. 1 interaction.
    STRINGi10116.ENSRNOP00000018447.

    Structurei

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 7070CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini93 – 1019LumenalSequence Analysis
    Topological domaini119 – 21597CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini235 – 24915LumenalSequence AnalysisAdd
    BLAST
    Topological domaini273 – 35886CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei71 – 9222HelicalSequence AnalysisAdd
    BLAST
    Transmembranei102 – 11817HelicalSequence AnalysisAdd
    BLAST
    Transmembranei216 – 23419HelicalSequence AnalysisAdd
    BLAST
    Transmembranei250 – 27223HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi119 – 1246Histidine box-1
    Motifi156 – 1605Histidine box-2
    Motifi297 – 3015Histidine 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.
    GeneTreeiENSGT00530000063158.
    HOGENOMiHOG000270352.
    HOVERGENiHBG003367.
    InParanoidiP07308.
    KOiK00507.
    OMAiLARCSRT.
    OrthoDBiEOG7ZPNKS.

    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.

    P07308-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPAHMLQEIS SSYTTTTTIT EPPSGNLQNG REKMKKVPLY LEEDIRPEMR    50
    EDIHDPSYQD EEGPPPKLEY VWRNIILMAL LHVGALYGIT LIPSSKVYTL 100
    LWGIFYYLIS ALGITAGAHR LWSHRTYKAR LPLRIFLIIA NTMAFQNDVY 150
    EWARDHRAHH KFSETHADPH NSRRGFFFSH VGWLLVRKHP AVKEKGGKLD 200
    MSDLKAEKLV MFQRRYYKPG LLLMCFILPT LVPWYCWGET FLHSLFVSTF 250
    LRYTLVLNAT WLVNSAAHLY GYRPYDKNIQ SRENILVSLG AVGEGFHNYH 300
    HAFPYDYSAS EYRWHINFTT FFIDCMAALG LAYDRKKVSK AAVLARIKRT 350
    GDGSHKSS 358
    Length:358
    Mass (Da):41,467
    Last modified:November 23, 2004 - v2
    Checksum:iB4C960A969B63774
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti291 – 2911A → S in AAA42116. (PubMed:2428815)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02585 mRNA. Translation: AAA42116.1.
    AF509568 mRNA. Translation: AAM34745.1.
    AF509569 mRNA. Translation: AAM34746.1.
    PIRiA24699.
    RefSeqiNP_631931.2. NM_139192.2.
    XP_006231495.1. XM_006231433.1.
    UniGeneiRn.1023.

    Genome annotation databases

    EnsembliENSRNOT00000018447; ENSRNOP00000018447; ENSRNOG00000013552.
    GeneIDi246074.
    KEGGirno:246074.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02585 mRNA. Translation: AAA42116.1 .
    AF509568 mRNA. Translation: AAM34745.1 .
    AF509569 mRNA. Translation: AAM34746.1 .
    PIRi A24699.
    RefSeqi NP_631931.2. NM_139192.2.
    XP_006231495.1. XM_006231433.1.
    UniGenei Rn.1023.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 251497. 1 interaction.
    STRINGi 10116.ENSRNOP00000018447.

    Chemistry

    BindingDBi P07308.
    ChEMBLi CHEMBL5424.

    PTM databases

    PhosphoSitei P07308.

    Proteomic databases

    PaxDbi P07308.
    PRIDEi P07308.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000018447 ; ENSRNOP00000018447 ; ENSRNOG00000013552 .
    GeneIDi 246074.
    KEGGi rno:246074.

    Organism-specific databases

    CTDi 20249.
    RGDi 621176. Scd1.

    Phylogenomic databases

    eggNOGi COG1398.
    GeneTreei ENSGT00530000063158.
    HOGENOMi HOG000270352.
    HOVERGENi HBG003367.
    InParanoidi P07308.
    KOi K00507.
    OMAi LARCSRT.
    OrthoDBi EOG7ZPNKS.

    Enzyme and pathway databases

    BioCyci MetaCyc:MONOMER-14123.
    BRENDAi 1.14.19.1. 5301.

    Miscellaneous databases

    NextBioi 623356.
    PROi P07308.

    Gene expression databases

    ArrayExpressi P07308.
    Genevestigatori P07308.

    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. "Construction and sequence of cDNA for rat liver stearyl coenzyme A desaturase."
      Thiede M.A., Ozols J., Strittmatter P.
      J. Biol. Chem. 261:13230-13235(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Structure and regulation of rat liver microsomal stearoyl-CoA desaturase gene."
      Mihara K.
      J. Biochem. 108:1022-1029(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Stearoyl-CoA desaturase 1 (Scd1) gene overexpression is associated with genetic predisposition to hepatocarcinogenesis in mice and rats."
      Falvella F.S., Pascale R.M., Gariboldi M., Manenti G., De Miglio M.R., Simile M.M., Dragani T.A., Feo F.
      Carcinogenesis 23:1933-1936(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Brown Norway and Fischer 344.

    Entry informationi

    Entry nameiACOD1_RAT
    AccessioniPrimary (citable) accession number: P07308
    Secondary accession number(s): Q8JZL5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: November 23, 2004
    Last modified: October 1, 2014
    This is version 128 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Desaturase has a half-life of only 4 hours.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3