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Q92038 (ACOD_CYPCA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismCyprinus carpio (Common carp)
Taxonomic identifier7962 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeCyprinus

Protein attributes

Sequence length327 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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 activity

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

Cofactor

Iron By similarity.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein Probable.

Induction

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

Domain

The histidine box domains may contain the active site and/or be involved in metal ion binding.

Sequence similarities

Belongs to the fatty acid desaturase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 327327Acyl-CoA desaturase
PRO_0000185403

Regions

Topological domain2 – 3837Cytoplasmic Potential
Transmembrane39 – 6022Helical; Potential
Topological domain61 – 699Lumenal Potential
Transmembrane70 – 8617Helical; Potential
Topological domain87 – 18397Cytoplasmic Potential
Transmembrane184 – 20219Helical; Potential
Topological domain203 – 21715Lumenal Potential
Transmembrane218 – 24023Helical; Potential
Topological domain241 – 32787Cytoplasmic Potential
Motif87 – 926Histidine box-1
Motif124 – 1285Histidine box-2
Motif265 – 2695Histidine box-3

Sequences

Sequence LengthMass (Da)Tools
Q92038 [UniParc].

Last modified May 1, 2000. Version 2.
Checksum: 3E794CB408D33089

FASTA32737,820
        10         20         30         40         50         60 
MPDREIKSPI WHPEPGTVED VFDHTYKEKE GPKPPTVIVW RNVILMSLLH LGALYGLFLF 

        70         80         90        100        110        120 
PSARALTWIW FFGCLLFSAL GITAGAHRLW SHRSYKASLP LQIFLALGNS MAFQNDIYEW 

       130        140        150        160        170        180 
SRDHRVHHKY SETDADPHNA VRGFFFSHVG WLLVRKHPDV IEKGRKLELS DLKADKVVMF 

       190        200        210        220        230        240 
QRRFYKPSVL LMCFFVPTFV PWYVWGESLW VAYFVPALLR YALVLNATWL VNSAAHMWGN 

       250        260        270        280        290        300 
RPYDSSINPR ENRFVTFSAI GEGFHNYHHT FPFDYATSEF GCKLNLTTCC FIDLMCFLGL 

       310        320 
AREPKRVSRE AVLARAQRTG DGSHWSG 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U31864 mRNA. Translation: AAB03857.2.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG003367.

Family and domain databases

InterProIPR005804. Fatty_acid_desaturase-1.
IPR001522. Fatty_acid_desaturase-1_C.
IPR015876. Fatty_acid_desaturase-1_core.
[Graphical view]
PfamPF00487. FA_desaturase. 1 hit.
[Graphical view]
PRINTSPR00075. FACDDSATRASE.
PROSITEPS00476. FATTY_ACID_DESATUR_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameACOD_CYPCA
AccessionPrimary (citable) accession number: Q92038
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2003
Last sequence update: May 1, 2000
Last modified: February 19, 2014
This is version 74 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families