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Protein

Acyl-CoA desaturase 2

Gene

Scd2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

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 activityi

Stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O.

Cofactori

GO - Molecular functioni

  • palmitoyl-CoA 9-desaturase activity Source: MGI
  • stearoyl-CoA 9-desaturase activity Source: MGI

GO - Biological processi

  • monounsaturated fatty acid biosynthetic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Keywords - Ligandi

Iron

Enzyme and pathway databases

BRENDAi1.14.19.1. 3474.

Names & Taxonomyi

Protein namesi
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 namesi
Name:Scd2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:98240. Scd2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 7070CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei71 – 9222HelicalSequence AnalysisAdd
BLAST
Topological domaini93 – 1019LumenalSequence Analysis
Transmembranei102 – 11817HelicalSequence AnalysisAdd
BLAST
Topological domaini119 – 21597CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei216 – 23419HelicalSequence AnalysisAdd
BLAST
Topological domaini235 – 24915LumenalSequence AnalysisAdd
BLAST
Transmembranei250 – 27223HelicalSequence AnalysisAdd
BLAST
Topological domaini273 – 35886CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 358358Acyl-CoA desaturase 2PRO_0000185398Add
BLAST

Proteomic databases

MaxQBiP13011.
PaxDbiP13011.
PRIDEiP13011.

PTM databases

PhosphoSiteiP13011.

Expressioni

Gene expression databases

BgeeiP13011.
CleanExiMM_SCD2.
GenevisibleiP13011. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000026221.

Structurei

3D structure databases

ProteinModelPortaliP13011.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi119 – 1246Histidine box-1
Motifi156 – 1605Histidine box-2
Motifi297 – 3015Histidine box-3

Domaini

The histidine box domains may contain the active site and/or be involved in metal ion binding.

Sequence similaritiesi

Belongs to the fatty acid desaturase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1398.
GeneTreeiENSGT00530000063158.
HOGENOMiHOG000270352.
HOVERGENiHBG003367.
InParanoidiP13011.
KOiK00507.
OMAiWRNVIAF.
OrthoDBiEOG7ZPNKS.
TreeFamiTF313251.

Family and domain databases

InterProiIPR005804. Fatty_acid_desaturase-1.
IPR001522. Fatty_acid_desaturase-1_C.
IPR015876. Fatty_acid_desaturase-1_core.
[Graphical view]
PfamiPF00487. FA_desaturase. 1 hit.
[Graphical view]
PRINTSiPR00075. FACDDSATRASE.
PROSITEiPS00476. FATTY_ACID_DESATUR_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P13011-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPAHILQEIS GAYSATTTIT APPSGGQQNG GEKFEKSSHH WGADVRPELK
60 70 80 90 100
DDLYDPTYQD DEGPPPKLEY VWRNIILMAL LHLGALYGIT LVPSCKLYTC
110 120 130 140 150
LFAYLYYVIS ALGITAGAHR LWSHRTYKAR LPLRLFLIIA NTMAFQNDVY
160 170 180 190 200
EWARDHRAHH KFSETHADPH NSRRGFFFSH VGWLLVRKHP AVKEKGGKLD
210 220 230 240 250
MSDLKAEKLV MFQRRYYKPG LLLMCFVLPT LVPWYCWGET FVNSLCVSTF
260 270 280 290 300
LRYAVVLNAT WLVNSAAHLY GYRPYDKNIS SRENILVSMG AVGEGFHNYH
310 320 330 340 350
HAFPYDYSAS EYRWHINFTT FFIDCMALLG LAYDRKRVSR AAVLARIKRT

GDGSCKSG
Length:358
Mass (Da):40,916
Last modified:July 27, 2011 - v2
Checksum:i3E04893F12E92A9A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti220 – 2201G → D in AAA40094 (PubMed:2570068).Curated
Sequence conflicti295 – 2951G → R in AAA40094 (PubMed:2570068).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS29848.1.
PIRiA36507.
RefSeqiNP_033154.2. NM_009128.2.
UniGeneiMm.487021.

Genome annotation databases

EnsembliENSMUST00000026221; ENSMUSP00000026221; ENSMUSG00000025203.
GeneIDi20250.
KEGGimmu:20250.
UCSCiuc008hpp.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS29848.1.
PIRiA36507.
RefSeqiNP_033154.2. NM_009128.2.
UniGeneiMm.487021.

3D structure databases

ProteinModelPortaliP13011.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000026221.

PTM databases

PhosphoSiteiP13011.

Proteomic databases

MaxQBiP13011.
PaxDbiP13011.
PRIDEiP13011.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000026221; ENSMUSP00000026221; ENSMUSG00000025203.
GeneIDi20250.
KEGGimmu:20250.
UCSCiuc008hpp.2. mouse.

Organism-specific databases

CTDi20250.
MGIiMGI:98240. Scd2.

Phylogenomic databases

eggNOGiCOG1398.
GeneTreeiENSGT00530000063158.
HOGENOMiHOG000270352.
HOVERGENiHBG003367.
InParanoidiP13011.
KOiK00507.
OMAiWRNVIAF.
OrthoDBiEOG7ZPNKS.
TreeFamiTF313251.

Enzyme and pathway databases

BRENDAi1.14.19.1. 3474.

Miscellaneous databases

ChiTaRSiScd2. mouse.
NextBioi297901.
PROiP13011.
SOURCEiSearch...

Gene expression databases

BgeeiP13011.
CleanExiMM_SCD2.
GenevisibleiP13011. MM.

Family and domain databases

InterProiIPR005804. Fatty_acid_desaturase-1.
IPR001522. Fatty_acid_desaturase-1_C.
IPR015876. Fatty_acid_desaturase-1_core.
[Graphical view]
PfamiPF00487. FA_desaturase. 1 hit.
[Graphical view]
PRINTSiPR00075. FACDDSATRASE.
PROSITEiPS00476. FATTY_ACID_DESATUR_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiACOD2_MOUSE
AccessioniPrimary (citable) accession number: P13011
Secondary accession number(s): Q8BH96
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: July 27, 2011
Last modified: June 24, 2015
This is version 130 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.