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Q92038

- ACOD_CYPCA

UniProt

Q92038 - ACOD_CYPCA

Protein

Acyl-CoA desaturase

Gene
N/A
Organism
Cyprinus carpio (Common carp)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 75 (01 Oct 2014)
      Sequence version 2 (01 May 2000)
      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
    2. response to stress Source: UniProtKB-KW

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism, Stress response

    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
    OrganismiCyprinus carpio (Common carp)
    Taxonomic identifieri7962 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeCyprinus

    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 – 327327Acyl-CoA desaturasePRO_0000185403Add
    BLAST

    Expressioni

    Inductioni

    By cold. A 10-fold increase in transcript levels is observed 48-60 hours after cooling.1 Publication

    Structurei

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini2 – 3837CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini61 – 699LumenalSequence Analysis
    Topological domaini87 – 18397CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini203 – 21715LumenalSequence AnalysisAdd
    BLAST
    Topological domaini241 – 32787CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei39 – 6022HelicalSequence AnalysisAdd
    BLAST
    Transmembranei70 – 8617HelicalSequence AnalysisAdd
    BLAST
    Transmembranei184 – 20219HelicalSequence AnalysisAdd
    BLAST
    Transmembranei218 – 24023HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi87 – 926Histidine box-1
    Motifi124 – 1285Histidine box-2
    Motifi265 – 2695Histidine 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.

    Q92038-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPDREIKSPI WHPEPGTVED VFDHTYKEKE GPKPPTVIVW RNVILMSLLH    50
    LGALYGLFLF PSARALTWIW FFGCLLFSAL GITAGAHRLW SHRSYKASLP 100
    LQIFLALGNS MAFQNDIYEW SRDHRVHHKY SETDADPHNA VRGFFFSHVG 150
    WLLVRKHPDV IEKGRKLELS DLKADKVVMF QRRFYKPSVL LMCFFVPTFV 200
    PWYVWGESLW VAYFVPALLR YALVLNATWL VNSAAHMWGN RPYDSSINPR 250
    ENRFVTFSAI GEGFHNYHHT FPFDYATSEF GCKLNLTTCC FIDLMCFLGL 300
    AREPKRVSRE AVLARAQRTG DGSHWSG 327
    Length:327
    Mass (Da):37,820
    Last modified:May 1, 2000 - v2
    Checksum:i3E794CB408D33089
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U31864 mRNA. Translation: AAB03857.2.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U31864 mRNA. Translation: AAB03857.2 .

    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. "Cold-induced expression of delta 9-desaturase in carp by transcriptional and posttranslational mechanisms."
      Tiku P.E., Gracey A.Y., Macartney A.I., Beynon R.J., Cossins A.R.
      Science 271:815-818(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION.
      Tissue: Liver.
    2. Tiku P.E.
      Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO 11-25 AND C-TERMINUS.

    Entry informationi

    Entry nameiACOD_CYPCA
    AccessioniPrimary (citable) accession number: Q92038
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 19, 2003
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 75 of the entry and version 2 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