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Protein

Acyl-CoA desaturase 2

Gene

Scd2

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

Functioni

Stearyl-CoA desaturase that utilizes O2 and electrons from reduced cytochrome b5 to introduce the first double bond into saturated fatty acyl-CoA substrates (PubMed:16443825). Catalyzes the insertion of a cis double bond at the delta-9 position into fatty acyl-CoA substrates including palmitoyl-CoA and stearoyl-CoA (PubMed:16443825). Gives rise to a mixture of 16:1 and 18:1 unsaturated fatty acids (PubMed:16443825). Contributes to the biosynthesis of membrane phospholipids, cholesterol esters and triglycerides, especially during embryonic development and in neonates (PubMed:16118274). Important for normal permeability barrier function of the skin in neonates (PubMed:16118274).2 Publications

Catalytic activityi

Stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O.1 Publication1 Publication

Cofactori

Fe2+By similarityNote: Expected to bind 2 Fe2+ ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei74 – 741SubstrateBy similarity
Metal bindingi119 – 1191Iron 1By similarity
Metal bindingi124 – 1241Iron 1By similarity
Binding sitei147 – 1471SubstrateBy similarity
Binding sitei154 – 1541SubstrateBy similarity
Binding sitei155 – 1551SubstrateBy similarity
Metal bindingi156 – 1561Iron 1By similarity
Metal bindingi159 – 1591Iron 2By similarity
Metal bindingi160 – 1601Iron 1By similarity
Binding sitei187 – 1871SubstrateBy similarity
Binding sitei188 – 1881SubstrateBy similarity
Binding sitei261 – 2611SubstrateBy similarity
Metal bindingi268 – 2681Iron 2By similarity
Metal bindingi297 – 2971Iron 2By similarity
Metal bindingi300 – 3001Iron 1By similarity
Metal bindingi301 – 3011Iron 2By similarity

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • palmitoyl-CoA 9-desaturase activity Source: MGI
  • stearoyl-CoA 9-desaturase activity Source: MGI

GO - Biological processi

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

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

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

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

BRENDAi1.14.19.1. 3474.
ReactomeiR-MMU-2426168. Activation of gene expression by SREBF (SREBP).
R-MMU-75105. Fatty Acyl-CoA Biosynthesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Acyl-CoA desaturase 2 (EC:1.14.19.11 Publication1 Publication)
Alternative name(s):
Delta(9)-desaturase 2
Short name:
Delta-9 desaturase 21 Publication
Fatty acid desaturase 2
Stearoyl-CoA desaturase 2
Gene namesi
Name:Scd2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:98240. Scd2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 7171CytoplasmicBy similarityAdd
BLAST
Transmembranei72 – 9221HelicalBy similarityAdd
BLAST
Topological domaini93 – 964LumenalBy similarity
Transmembranei97 – 11721HelicalBy similarityAdd
BLAST
Topological domaini118 – 21699CytoplasmicBy similarityAdd
BLAST
Transmembranei217 – 23620HelicalBy similarityAdd
BLAST
Topological domaini237 – 2404LumenalBy similarity
Transmembranei241 – 26222HelicalBy similarityAdd
BLAST
Topological domaini263 – 35896CytoplasmicBy similarityAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome

Pathology & Biotechi

Disruption phenotypei

Mutant mice are born at the expected Mendelian rate. Neonates are smaller than wild-type and present high mortality, ranging from 70 to 100%, depending on the genetic background. Neonates display a shiny skin, but after a few hours their skin appears dry and cracked. The permeability barrier function of their skin is impaired, leading to rapid weight loss due to dehydration. Their epidermis has decreased levels of cholesterol esters, triglycerides, acylceramide, and glucosylacylceramide containing unsaturated fatty acids. In mutant neonates, triglyceride levels in liver and blood plasma are reduced by half, due to strongly reduced levels of stearoyl-CoA desaturase activity in the liver and strongly reduced levels of triglyceride biosynthesis. In contrast, the levels of stearoyl-CoA desaturase activity are normal in adult mice deficient for Scd2. Adult mice display kinked tails.1 Publication

PTM / Processingi

Molecule processing

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

Proteomic databases

EPDiP13011.
MaxQBiP13011.
PaxDbiP13011.
PRIDEiP13011.

PTM databases

iPTMnetiP13011.
PhosphoSiteiP13011.

Expressioni

Tissue specificityi

Detected in brain and skin (PubMed:10545940, PubMed:11161812, PubMed:16118274). Highly expressed in brain, and detected at low levels in heart, stomach, lung and testis (PubMed:11161812, PubMed:12815040). Detected both in dermis and epidermis (PubMed:16118274).3 Publications

Developmental stagei

Highly expressed during embryonic development and during the first three weeks after birth. Expression is low in adults.1 Publication

Inductioni

Up-regulated by agonists that activate NR1H3 (PubMed:12815040). Slightly down-regulated by a high-carbohydrate diet enriched in unsaturated fatty acids (PubMed:12815040).1 Publication

Gene expression databases

BgeeiP13011.
CleanExiMM_SCD2.
GenevisibleiP13011. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000026221.

Structurei

3D structure databases

ProteinModelPortaliP13011.
SMRiP13011. Positions 44-357.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

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

Domaini

The histidine box domains are involved in binding the catalytic metal ions.By similarity

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1600. Eukaryota.
COG1398. LUCA.
GeneTreeiENSGT00530000063158.
HOGENOMiHOG000270352.
HOVERGENiHBG003367.
InParanoidiP13011.
KOiK00507.
OMAiGFHRYLA.
OrthoDBiEOG7ZPNKS.
TreeFamiTF313251.

Family and domain databases

InterProiIPR001522. Fatty_acid_desaturase-1_C.
IPR015876. Fatty_acid_desaturase-1_core.
IPR005804. Fatty_acid_desaturase_dom.
[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.
SMRiP13011. Positions 44-357.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000026221.

PTM databases

iPTMnetiP13011.
PhosphoSiteiP13011.

Proteomic databases

EPDiP13011.
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

eggNOGiKOG1600. Eukaryota.
COG1398. LUCA.
GeneTreeiENSGT00530000063158.
HOGENOMiHOG000270352.
HOVERGENiHBG003367.
InParanoidiP13011.
KOiK00507.
OMAiGFHRYLA.
OrthoDBiEOG7ZPNKS.
TreeFamiTF313251.

Enzyme and pathway databases

BRENDAi1.14.19.1. 3474.
ReactomeiR-MMU-2426168. Activation of gene expression by SREBF (SREBP).
R-MMU-75105. Fatty Acyl-CoA Biosynthesis.

Miscellaneous databases

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

Gene expression databases

BgeeiP13011.
CleanExiMM_SCD2.
GenevisibleiP13011. MM.

Family and domain databases

InterProiIPR001522. Fatty_acid_desaturase-1_C.
IPR015876. Fatty_acid_desaturase-1_core.
IPR005804. Fatty_acid_desaturase_dom.
[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/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.
  5. "Scd1 is expressed in sebaceous glands and is disrupted in the asebia mouse."
    Zheng Y., Eilertsen K.J., Ge L., Zhang L., Sundberg J.P., Prouty S.M., Stenn K.S., Parimoo S.
    Nat. Genet. 23:268-270(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  6. "Scd3--a novel gene of the stearoyl-CoA desaturase family with restricted expression in skin."
    Zheng Y., Prouty S.M., Harmon A., Sundberg J.P., Stenn K.S., Parimoo S.
    Genomics 71:182-191(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  7. "Identification and characterization of murine SCD4, a novel heart-specific stearoyl-CoA desaturase isoform regulated by leptin and dietary factors."
    Miyazaki M., Jacobson M.J., Man W.C., Cohen P., Asilmaz E., Friedman J.M., Ntambi J.M.
    J. Biol. Chem. 278:33904-33911(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY UNSATURATED FATTY ACIDS AND NR1H3, TISSUE SPECIFICITY.
  8. "Stearoyl-CoA desaturase-2 gene expression is required for lipid synthesis during early skin and liver development."
    Miyazaki M., Dobrzyn A., Elias P.M., Ntambi J.M.
    Proc. Natl. Acad. Sci. U.S.A. 102:12501-12506(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.
  9. "Identification of mouse palmitoyl-coenzyme A Delta9-desaturase."
    Miyazaki M., Bruggink S.M., Ntambi J.M.
    J. Lipid Res. 47:700-704(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.

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: March 16, 2016
This is version 138 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

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 one 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.