P13011 (ACOD2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

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

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

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

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.
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 Transmembrane helix
Ligand	Iron
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	fatty acid biosynthetic process 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
Molecular function	iron ion binding Inferred from electronic annotation. Source: InterPro stearoyl-CoA 9-desaturase activity Inferred from electronic annotation. Source: EC
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_0000185398
Regions
	Topological domain	2 – 70	69	Cytoplasmic Potential
	Transmembrane	71 – 92	22	Helical; Potential
	Topological domain	93 – 101	9	Lumenal Potential
	Transmembrane	102 – 118	17	Helical; Potential
	Topological domain	119 – 215	97	Cytoplasmic Potential
	Transmembrane	216 – 234	19	Helical; Potential
	Topological domain	235 – 249	15	Lumenal Potential
	Transmembrane	250 – 272	23	Helical; Potential
	Topological domain	273 – 358	86	Cytoplasmic 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	220	1	G → D in AAA40094. Ref.1
	Sequence conflict	295	1	G → R in AAA40094. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P13011 [UniParc]. Last modified July 27, 2011. Version 2. Checksum: 3E04893F12E92A9A	FASTA	358	40,916
	10 20 30 40 50 60 MPAHILQEIS GAYSATTTIT APPSGGQQNG GEKFEKSSHH WGADVRPELK DDLYDPTYQD 70 80 90 100 110 120 DEGPPPKLEY VWRNIILMAL LHLGALYGIT LVPSCKLYTC LFAYLYYVIS ALGITAGAHR 130 140 150 160 170 180 LWSHRTYKAR LPLRLFLIIA NTMAFQNDVY EWARDHRAHH KFSETHADPH NSRRGFFFSH 190 200 210 220 230 240 VGWLLVRKHP AVKEKGGKLD MSDLKAEKLV MFQRRYYKPG LLLMCFVLPT LVPWYCWGET 250 260 270 280 290 300 FVNSLCVSTF LRYAVVLNAT WLVNSAAHLY GYRPYDKNIS SRENILVSMG AVGEGFHNYH 310 320 330 340 350 HAFPYDYSAS EYRWHINFTT FFIDCMALLG LAYDRKRVSR AAVLARIKRT GDGSCKSG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Differentiation-induced gene expression in 3T3-L1 preadipocytes. A second differentially expressed gene encoding stearoyl-CoA desaturase." Kaestner K.H., Ntambi J.M., Kelly T.J. Jr., Lane M.D. J. Biol. Chem. 264:14755-14761(1989) [PubMed: 2570068] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Adipocyte.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6 and C57BL/6J. Tissue: Brain and Spinal ganglion.
[3]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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]. Strain: 129. Tissue: Mammary tumor.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M26270 mRNA. Translation: AAA40094.1. AK083922 mRNA. Translation: BAC39066.1. AK147406 mRNA. Translation: BAE27893.1. CH466534 Genomic DNA. Translation: EDL41928.1. BC040384 mRNA. Translation: AAH40384.1.
IPI	IPI00117142.
PIR	A36507.
RefSeq	NP_033154.2. NM_009128.2.
UniGene	Mm.485035.
3D structure databases
ProteinModelPortal	P13011.
ModBase	Search...
Protein-protein interaction databases
STRING	P13011.
Proteomic databases
PRIDE	P13011.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000026221; ENSMUSP00000026221; ENSMUSG00000025203.
GeneID	20250.
KEGG	mmu:20250.
NMPDR	fig|10090.3.peg.5128.
Organism-specific databases
CTD	20250.
MGI	MGI:98240. Scd2.
Phylogenomic databases
eggNOG	roNOG13436.
HOGENOM	HBG380611.
HOVERGEN	HBG003367.
InParanoid	P13011.
OrthoDB	EOG4W9J41.
Enzyme and pathway databases
BRENDA	1.14.19.1. 3474.
Gene expression databases
ArrayExpress	P13011.
Bgee	P13011.
CleanEx	MM_SCD2.
Genevestigator	P13011.
GermOnline	ENSMUSG00000025203. Mus musculus.
Family and domain databases
InterPro	IPR005804. Fatty_acid_desaturase-1. IPR001522. Fatty_acid_desaturase-1_C. IPR015876. Fatty_acid_desaturase-1_core. [Graphical view]
KO	K00507.
Pfam	PF00487. FA_desaturase. 1 hit. [Graphical view]
PRINTS	PR00075. FACDDSATRASE.
PROSITE	PS00476. FATTY_ACID_DESATUR_1. 1 hit. [Graphical view]
ProtoNet	Search...
Other
SOURCE	Search...

Entry information

Entry name

ACOD2_MOUSE

Accession

Primary (citable) accession number: P13011
Secondary accession number(s): Q8BH96

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	July 27, 2011
Last modified:	January 25, 2012
This is version 108 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program