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Q92038

- ACOD_CYPCA

UniProt

Q92038 - ACOD_CYPCA

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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

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

Fe cationBy 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
Complete GO annotation...

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 3838CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei39 – 6022HelicalSequence AnalysisAdd
BLAST
Topological domaini61 – 699LumenalSequence Analysis
Transmembranei70 – 8617HelicalSequence AnalysisAdd
BLAST
Topological domaini87 – 18397CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei184 – 20219HelicalSequence AnalysisAdd
BLAST
Topological domaini203 – 21715LumenalSequence AnalysisAdd
BLAST
Transmembranei218 – 24023HelicalSequence AnalysisAdd
BLAST
Topological domaini241 – 32787CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB-KW
  2. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

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

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

        10         20         30         40         50
MPDREIKSPI WHPEPGTVED VFDHTYKEKE GPKPPTVIVW RNVILMSLLH
60 70 80 90 100
LGALYGLFLF PSARALTWIW FFGCLLFSAL GITAGAHRLW SHRSYKASLP
110 120 130 140 150
LQIFLALGNS MAFQNDIYEW SRDHRVHHKY SETDADPHNA VRGFFFSHVG
160 170 180 190 200
WLLVRKHPDV IEKGRKLELS DLKADKVVMF QRRFYKPSVL LMCFFVPTFV
210 220 230 240 250
PWYVWGESLW VAYFVPALLR YALVLNATWL VNSAAHMWGN RPYDSSINPR
260 270 280 290 300
ENRFVTFSAI GEGFHNYHHT FPFDYATSEF GCKLNLTTCC FIDLMCFLGL
310 320
AREPKRVSRE AVLARAQRTG DGSHWSG
Length:327
Mass (Da):37,820
Last modified:May 1, 2000 - v2
Checksum:i3E794CB408D33089
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U31864 mRNA. Translation: AAB03857.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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: November 26, 2014
This is version 77 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