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Protein

Acyl-CoA desaturase

Gene
N/A
Organism
Cyprinus carpio (Common carp)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Stearyl-CoA desaturase that utilizes O2 and electrons from reduced cytochrome b5 to introduce the first double bond into saturated fatty acyl-CoA substrates. Has high specificity and catalyzes the insertion of a cis double bond at the delta-9 position into fatty acyl-CoA substrates including palmitoyl-CoA and stearoyl-CoA. Contributes to the biosynthesis of membrane phospholipids, cholesterol esters and triglycerides.By similarity

Catalytic activityi

Stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O.By similarity

Cofactori

Fe2+By similarityNote: Expected to bind 2 Fe2+ ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei42 – 421SubstrateBy similarity
Metal bindingi87 – 871Iron 1By similarity
Metal bindingi92 – 921Iron 1By similarity
Binding sitei115 – 1151SubstrateBy similarity
Binding sitei122 – 1221SubstrateBy similarity
Binding sitei123 – 1231SubstrateBy similarity
Metal bindingi124 – 1241Iron 1By similarity
Metal bindingi127 – 1271Iron 2By similarity
Metal bindingi128 – 1281Iron 1By similarity
Binding sitei155 – 1551SubstrateBy similarity
Binding sitei156 – 1561SubstrateBy similarity
Binding sitei229 – 2291SubstrateBy similarity
Metal bindingi236 – 2361Iron 2By similarity
Metal bindingi265 – 2651Iron 2By similarity
Metal bindingi268 – 2681Iron 1By similarity
Metal bindingi269 – 2691Iron 2By similarity

GO - Molecular functioni

GO - Biological processi

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, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Acyl-CoA desaturase (EC:1.14.19.1By similarity)
Alternative name(s):
Delta(9)-desaturase
Short name:
Delta-9 desaturase1 Publication
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 – 3939CytoplasmicBy similarityAdd
BLAST
Transmembranei40 – 6021HelicalBy similarityAdd
BLAST
Topological domaini61 – 644LumenalBy similarity
Transmembranei65 – 8521HelicalBy similarityAdd
BLAST
Topological domaini86 – 18499CytoplasmicBy similarityAdd
BLAST
Transmembranei185 – 20420HelicalBy similarityAdd
BLAST
Topological domaini205 – 2084LumenalBy similarity
Transmembranei209 – 23022HelicalBy similarityAdd
BLAST
Topological domaini231 – 32797CytoplasmicBy similarityAdd
BLAST

GO - Cellular componenti

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-1Curated
Motifi124 – 1285Histidine box-2Curated
Motifi265 – 2695Histidine box-3Curated

Domaini

The histidine box domains are involved in binding the catalytic metal ions.By similarity

Sequence similaritiesi

Belongs to the fatty acid desaturase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

HOVERGENiHBG003367.

Family and domain databases

InterProiIPR001522. Fatty_acid_desaturase-1_C.
IPR015876. Fatty_acid_desaturase-1_core.
IPR005804. Fatty_acid_desaturase_dom.
[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

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG003367.

Family and domain databases

InterProiIPR001522. Fatty_acid_desaturase-1_C.
IPR015876. Fatty_acid_desaturase-1_core.
IPR005804. Fatty_acid_desaturase_dom.
[Graphical view]
PfamiPF00487. FA_desaturase. 1 hit.
[Graphical view]
PRINTSiPR00075. FACDDSATRASE.
PROSITEiPS00476. FATTY_ACID_DESATUR_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

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 14, 2015
This is version 81 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.