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P13011 (ACOD2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

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.

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_0000185398

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 conflict2201G → D in AAA40094. Ref.1
Sequence conflict2951G → R in AAA40094. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P13011 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 3E04893F12E92A9A

FASTA35840,916
        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

« Hide

References

« Hide '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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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] [Europe PMC] [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.
IPIIPI00117142.
PIRA36507.
RefSeqNP_033154.2. NM_009128.2.
UniGeneMm.487021.

3D structure databases

ProteinModelPortalP13011.
ModBaseSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000026221.

PTM databases

PhosphoSiteP13011.

Proteomic databases

PaxDbP13011.
PRIDEP13011.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000026221; ENSMUSP00000026221; ENSMUSG00000025203.
GeneID20250.
KEGGmmu:20250.

Organism-specific databases

CTD20250.
MGIMGI:98240. Scd2.

Phylogenomic databases

eggNOGCOG1398.
GeneTreeENSGT00530000063158.
HOGENOMHOG000270352.
HOVERGENHBG003367.
InParanoidQ8BH96.
KOK00507.
OMAYSATTTI.
OrthoDBEOG4W9J41.

Enzyme and pathway databases

BRENDA1.14.19.1. 3474.

Gene expression databases

BgeeP13011.
CleanExMM_SCD2.
GenevestigatorP13011.
GermOnlineENSMUSG00000025203. Mus musculus.

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

ChiTaRSScd2. mouse.
NextBio297901.
SOURCESearch...

Entry information

Entry nameACOD2_MOUSE
AccessionPrimary (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: April 3, 2013
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

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