Reviewed, UniProtKB/Swiss-Prot Q6P7B9 (ACOD2_RAT)

Names and origin

Protein names

Recommended name:
    Acyl-CoA desaturase 2
    EC=1.14.19.1
Alternative name(s):
    Stearoyl-CoA desaturase 2
    Fatty acid desaturase 2
    Delta(9)-desaturase 2

Gene names

Name:

Scd2

Organism

Rattus norvegicus (Rat)

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.
Sequence processing	The displayed sequence is not processed.
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 Lipid synthesis
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane
Ligand	Iron
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological process	fatty acid biosynthetic process Traceable author statement. Source: RGD myelination Inferred from expression pattern. Source: RGD oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW microsome Traceable author statement. Source: RGD
Molecular function	iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW stearoyl-CoA 9-desaturase activity Inferred from direct assay. 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
	Transmembrane	75 – 95	21	Potential
	Transmembrane	97 – 117	21	Potential
	Transmembrane	222 – 242	21	Potential
	Transmembrane	314 – 334	21	Potential
	Motif	119 – 124	6	Histidine box-1
	Motif	156 – 160	5	Histidine box-2
	Motif	297 – 301	5	Histidine box-3
Experimental info
	Sequence conflict	76	1	V → I in BAA92436. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q6P7B9-1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 24EAA2329011C4D9	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

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: 15489334] [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: 7800118] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-60.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB032243 mRNA. Translation: BAA92436.1. BC061737 mRNA. Translation: AAH61737.1. S75730 mRNA. Translation: AAB32826.1.
IPI	IPI00464460.
RefSeq	NP_114029.1.
UniGene	Rn.83595
3D structure databases
ModBase	Search...
Proteomic databases
PRIDE	Q6P7B9.
Genome annotation databases
Ensembl	ENSRNOG00000013279. Rattus norvegicus. [Contig view]
GeneID	83792.
KEGG	rno:83792.
Organism-specific databases
RGD	621177. Scd2.
Phylogenomic databases
HOVERGEN	Q6P7B9.
Enzyme and pathway databases
BRENDA	1.14.19.1. 248.
Gene expression databases
ArrayExpress	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.
ProDom	PD002221. Desaturase. 1 hit. PD001081. FA_desat_sub. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00476. FATTY_ACID_DESATUR_1. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
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:	June 16, 2009
This is version 43 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)