Acyl-CoA desaturase 2 - Rattus norvegicus (Rat)

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Q6P7B9 (ACOD2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 69. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	358 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Fatty acid metabolism Lipid biosynthesis Lipid metabolism
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane Transmembrane helix
Ligand	Iron
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	fatty acid biosynthetic process Traceable author statement PubMed 16207839. Source: RGD myelination Inferred from expression pattern PubMed 9751207. Source: RGD
Cellular_component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	iron ion binding Inferred from electronic annotation. Source: InterPro stearoyl-CoA 9-desaturase activity Inferred from direct assay PubMed 16207839. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 358

358

Acyl-CoA desaturase 2

PRO_0000185401

Regions

Topological domain

2 – 70

Cytoplasmic Potential

Transmembrane

71 – 92

Helical; Potential

Topological domain

93 – 101

Lumenal Potential

Transmembrane

102 – 118

Helical; Potential

Topological domain

119 – 215

Cytoplasmic Potential

Transmembrane

216 – 234

Helical; Potential

Topological domain

235 – 249

Lumenal Potential

Transmembrane

250 – 272

Helical; Potential

Topological domain

273 – 358

Cytoplasmic Potential

Motif

119 – 124

Histidine box-1

Motif

156 – 160

Histidine box-2

Motif

297 – 301

Histidine box-3

Experimental info

Sequence conflict

V → I in BAA92436. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

Q6P7B9 [UniParc].

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

358

41,013

        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' referencesShow '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.
IPI	IPI00464460.
RefSeq	NP_114029.1. NM_031841.1.
UniGene	Rn.83595.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	10116.ENSRNOP00000018090.
PTM databases
PhosphoSite	Q6P7B9.
Proteomic databases
PaxDb	Q6P7B9.
PRIDE	Q6P7B9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	83792.
KEGG	rno:83792.
UCSC	RGD:621177. rat.
Organism-specific databases
CTD	6319.
RGD	621177. Scd2.
Phylogenomic databases
eggNOG	COG1398.
HOGENOM	HOG000270352.
HOVERGEN	HBG003367.
InParanoid	Q6P7B9.
KO	K00507.
OrthoDB	EOG4W9J41.
Gene expression databases
ArrayExpress	Q6P7B9.
Genevestigator	Q6P7B9.
GermOnline	ENSRNOG00000013279. Rattus norvegicus.
Family and domain databases
InterPro	IPR005804. Fatty_acid_desaturase-1. IPR001522. Fatty_acid_desaturase-1_C. IPR015876. Fatty_acid_desaturase-1_core. [Graphical view]
Pfam	PF00487. FA_desaturase. 1 hit. [Graphical view]
PRINTS	PR00075. FACDDSATRASE.
PROSITE	PS00476. FATTY_ACID_DESATUR_1. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	616377.

Entry information

Entry name

ACOD2_RAT

Accession

Primary (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 3, 2013
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents