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Q6P7B9 (ACOD2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 76. 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 2

EC=1.14.19.1
Alternative name(s):
Delta(9)-desaturase 2
Short name=Delta-9 desaturase 2
Fatty acid desaturase 2
Stearoyl-CoA desaturase 2
Gene names
Name:Scd2
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length358 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.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein Probable.

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 – 358358Acyl-CoA desaturase 2
PRO_0000185401

Regions

Topological domain2 – 7069Cytoplasmic Potential
Transmembrane71 – 9222Helical; Potential
Topological domain93 – 1019Lumenal Potential
Transmembrane102 – 11817Helical; Potential
Topological domain119 – 21597Cytoplasmic Potential
Transmembrane216 – 23419Helical; Potential
Topological domain235 – 24915Lumenal Potential
Transmembrane250 – 27223Helical; Potential
Topological domain273 – 35886Cytoplasmic Potential
Motif119 – 1246Histidine box-1
Motif156 – 1605Histidine box-2
Motif297 – 3015Histidine box-3

Experimental info

Sequence conflict761V → I in BAA92436. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q6P7B9 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 24EAA2329011C4D9

FASTA35841,013
        10         20         30         40         50         60 
MPAHILQEIS GSYSATTTIT APPSGGQQNG GEKFEKNPHH WGADVRPEIK DDLYDPSYQD 

        70         80         90        100        110        120 
EEGPPPKLEY VWRNIVLMAL LHIGALYGIT LVPSCKVYTC LFAYLYYVIS ALGITAGAHR 

       130        140        150        160        170        180 
LWSHRTYKAR LPLRLFLIIA NTMAFQNDVY EWARDHRAHH KFSETHADPH NSRRGFFFSH 

       190        200        210        220        230        240 
VGWLLVRKHP AVKEKGGKLD MSDLKAEKLV MFQRRYYKPG LLLMCFILPT LVPWYCWGET 

       250        260        270        280        290        300 
FVNSLCVSTF LRYAVVLNAT WLVNSAAHLY GYRPYDKNIS SRENILVSMG AVGEGFHNYH 

       310        320        330        340        350 
HAFPYDYSAS EYRWHINFTT FFIDCMALLG LAYDRKRVSK AAVLARIKRT GEESCKSG 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and tissue expression of rat stearoyl-CoA desaturase 2."
Hoshino T., Ishiguro K., Ohtsu K.
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Prostate.
[3]"Identification of novel mRNAs expressed in oligodendrocytes."
Baba H., Fuss B., Watson J.B., Zane L.T., Macklin W.B.
Neurochem. Res. 19:1091-1099(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-60.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB032243 mRNA. Translation: BAA92436.1.
BC061737 mRNA. Translation: AAH61737.1.
S75730 mRNA. Translation: AAB32826.1.
RefSeqNP_114029.1. NM_031841.1.
UniGeneRn.83595.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000018090.

PTM databases

PhosphoSiteQ6P7B9.

Proteomic databases

PaxDbQ6P7B9.
PRIDEQ6P7B9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID83792.
KEGGrno:83792.
UCSCRGD:621177. rat.

Organism-specific databases

CTD6319.
RGD621177. Scd2.

Phylogenomic databases

eggNOGCOG1398.
HOGENOMHOG000270352.
HOVERGENHBG003367.
InParanoidQ6P7B9.
KOK00507.
OrthoDBEOG7ZPNKS.
PhylomeDBQ6P7B9.
TreeFamTF313251.

Gene expression databases

GenevestigatorQ6P7B9.

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...

Other

NextBio616377.

Entry information

Entry nameACOD2_RAT
AccessionPrimary (citable) accession number: Q6P7B9
Secondary accession number(s): Q64066, Q9JMC9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: July 5, 2004
Last modified: April 16, 2014
This is version 76 of the entry and version 1 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