Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Acyl-CoA desaturase 2

Gene

Scd2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -Experimental evidence at transcript 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. Catalyzes the insertion of a cis double bond at the delta-9 position into fatty acyl-CoA substrates including palmitoyl-CoA and stearoyl-CoA. Gives rise to a mixture of 16:1 and 18:1 unsaturated fatty acids. Contributes to the biosynthesis of membrane phospholipids, cholesterol esters and triglycerides, especially during embryonic development and in neonates. Important for normal permeability barrier function of the skin in neonates.By similarity

Catalytic activityi

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

Cofactori

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei74SubstrateBy similarity1
Metal bindingi119Iron 1By similarity1
Metal bindingi124Iron 1By similarity1
Binding sitei147SubstrateBy similarity1
Binding sitei154SubstrateBy similarity1
Binding sitei155SubstrateBy similarity1
Metal bindingi156Iron 1By similarity1
Metal bindingi159Iron 2By similarity1
Metal bindingi160Iron 1By similarity1
Binding sitei187SubstrateBy similarity1
Binding sitei188SubstrateBy similarity1
Binding sitei261SubstrateBy similarity1
Metal bindingi268Iron 2By similarity1
Metal bindingi297Iron 2By similarity1
Metal bindingi300Iron 1By similarity1
Metal bindingi301Iron 2By similarity1

GO - Molecular functioni

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

GO - Biological processi

  • fatty acid biosynthetic process Source: RGD
  • monounsaturated fatty acid biosynthetic process Source: GO_Central
  • myelination Source: RGD
  • response to fatty acid Source: UniProtKB

Keywordsi

Molecular functionOxidoreductase
Biological processFatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism
LigandIron, Metal-binding

Enzyme and pathway databases

BRENDAi1.14.19.1 5301

Chemistry databases

SwissLipidsiSLP:000000455

Names & Taxonomyi

Protein namesi
Recommended name:
Acyl-CoA desaturase 2 (EC:1.14.19.1By similarity)
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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi621177 Scd2

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 71CytoplasmicBy similarityAdd BLAST71
Transmembranei72 – 92HelicalBy similarityAdd BLAST21
Topological domaini93 – 96LumenalBy similarity4
Transmembranei97 – 117HelicalBy similarityAdd BLAST21
Topological domaini118 – 216CytoplasmicBy similarityAdd BLAST99
Transmembranei217 – 236HelicalBy similarityAdd BLAST20
Topological domaini237 – 240LumenalBy similarity4
Transmembranei241 – 262HelicalBy similarityAdd BLAST22
Topological domaini263 – 358CytoplasmicBy similarityAdd BLAST96

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001854011 – 358Acyl-CoA desaturase 2Add BLAST358

Proteomic databases

PaxDbiQ6P7B9
PRIDEiQ6P7B9

PTM databases

iPTMnetiQ6P7B9
PhosphoSitePlusiQ6P7B9

Expressioni

Tissue specificityi

Detected in brain and adipose tissue, and at much lower levels in testis. Detected in liver when rats are kept on a fat-free diet, but not when their food contains unsaturated fatty acids.1 Publication

Inductioni

Up-regulated in liver in the absence of dietary unsaturated fatty acids(PubMed:1982442). Expression in adipose tissue seems to be constitutive (PubMed:1982442).1 Publication

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000067809

Structurei

3D structure databases

SMRiQ6P7B9
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi119 – 124Histidine box-1Curated6
Motifi156 – 160Histidine box-2Curated5
Motifi297 – 301Histidine box-3Curated5

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
HOGENOMiHOG000270352
HOVERGENiHBG003367
InParanoidiQ6P7B9
KOiK00507
PhylomeDBiQ6P7B9
TreeFamiTF313251

Family and domain databases

CDDicd03505 Delta9-FADS-like, 1 hit
InterProiView protein in InterPro
IPR015876 Acyl-CoA_DS
IPR005804 FA_desaturase_dom
IPR001522 FADS-1_CS
PANTHERiPTHR11351 PTHR11351, 1 hit
PfamiView protein in Pfam
PF00487 FA_desaturase, 1 hit
PRINTSiPR00075 FACDDSATRASE
PROSITEiView protein in PROSITE
PS00476 FATTY_ACID_DESATUR_1, 1 hit

Sequencei

Sequence statusi: Complete.

Q6P7B9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPAHILQEIS GSYSATTTIT APPSGGQQNG GEKFEKNPHH WGADVRPEIK
60 70 80 90 100
DDLYDPSYQD EEGPPPKLEY VWRNIVLMAL LHIGALYGIT LVPSCKVYTC
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 LLLMCFILPT LVPWYCWGET FVNSLCVSTF
260 270 280 290 300
LRYAVVLNAT WLVNSAAHLY GYRPYDKNIS SRENILVSMG AVGEGFHNYH
310 320 330 340 350
HAFPYDYSAS EYRWHINFTT FFIDCMALLG LAYDRKRVSK AAVLARIKRT

GEESCKSG
Length:358
Mass (Da):41,013
Last modified:July 5, 2004 - v1
Checksum:i24EAA2329011C4D9
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti76V → I in BAA92436 (Ref. 1) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB032243 mRNA Translation: BAA92436.1
BC061737 mRNA Translation: AAH61737.1
S75730 mRNA Translation: AAB32826.1
RefSeqiNP_114029.1, NM_031841.1
UniGeneiRn.83595

Genome annotation databases

GeneIDi83792
KEGGirno:83792
UCSCiRGD:621177 rat

Similar proteinsi

Entry informationi

Entry nameiACOD2_RAT
AccessioniPrimary (citable) accession number: Q6P7B9
Secondary accession number(s): Q64066, Q9JMC9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: July 5, 2004
Last modified: May 23, 2018
This is version 99 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health