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P13011

- ACOD2_MOUSE

UniProt

P13011 - ACOD2_MOUSE

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Protein

Acyl-CoA desaturase 2

Gene

Scd2

Organism
Mus musculus (Mouse)
Status
Reviewed - 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

Iron.

GO - Molecular functioni

  1. iron ion binding Source: InterPro
  2. stearoyl-CoA 9-desaturase activity Source: UniProtKB-EC

GO - Biological processi

  1. fatty acid biosynthetic process Source: UniProtKB-KW
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: Chromosome 19

Organism-specific databases

MGIiMGI:98240. Scd2.

Subcellular locationi

GO - Cellular componenti

  1. endoplasmic reticulum Source: MGI
  2. integral component of membrane Source: UniProtKB-KW
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.
GenevestigatoriP13011.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000026221.

Structurei

3D structure databases

ProteinModelPortaliP13011.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 7069CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini93 – 1019LumenalSequence Analysis
Topological domaini119 – 21597CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini235 – 24915LumenalSequence AnalysisAdd
BLAST
Topological domaini273 – 35886CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei71 – 9222HelicalSequence AnalysisAdd
BLAST
Transmembranei102 – 11817HelicalSequence AnalysisAdd
BLAST
Transmembranei216 – 23419HelicalSequence AnalysisAdd
BLAST
Transmembranei250 – 27223HelicalSequence AnalysisAdd
BLAST

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.
OMAiRRENSIT.
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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS29848.1.
PIRi A36507.
RefSeqi NP_033154.2. NM_009128.2.
UniGenei Mm.487021.

3D structure databases

ProteinModelPortali P13011.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10090.ENSMUSP00000026221.

PTM databases

PhosphoSitei P13011.

Proteomic databases

MaxQBi P13011.
PaxDbi P13011.
PRIDEi P13011.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000026221 ; ENSMUSP00000026221 ; ENSMUSG00000025203 .
GeneIDi 20250.
KEGGi mmu:20250.
UCSCi uc008hpp.2. mouse.

Organism-specific databases

CTDi 20250.
MGIi MGI:98240. Scd2.

Phylogenomic databases

eggNOGi COG1398.
GeneTreei ENSGT00530000063158.
HOGENOMi HOG000270352.
HOVERGENi HBG003367.
InParanoidi P13011.
KOi K00507.
OMAi RRENSIT.
OrthoDBi EOG7ZPNKS.
TreeFami TF313251.

Enzyme and pathway databases

BRENDAi 1.14.19.1. 3474.

Miscellaneous databases

ChiTaRSi Scd2. mouse.
NextBioi 297901.
PROi P13011.
SOURCEi Search...

Gene expression databases

Bgeei P13011.
CleanExi MM_SCD2.
Genevestigatori P13011.

Family and domain databases

InterProi IPR005804. Fatty_acid_desaturase-1.
IPR001522. Fatty_acid_desaturase-1_C.
IPR015876. Fatty_acid_desaturase-1_core.
[Graphical view ]
Pfami PF00487. FA_desaturase. 1 hit.
[Graphical view ]
PRINTSi PR00075. FACDDSATRASE.
PROSITEi PS00476. FATTY_ACID_DESATUR_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 29, 2014
This is version 126 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