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Protein

Acyl-CoA desaturase 2

Gene

Scd2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

  • iron ion binding Source: GO_Central
  • stearoyl-CoA 9-desaturase activity Source: RGD

GO - Biological processi

  • fatty acid biosynthetic process Source: RGD
  • long-chain fatty acid biosynthetic process Source: GO_Central
  • monounsaturated fatty acid biosynthetic process Source: GO_Central
  • myelination Source: RGD
  • response to fatty acid Source: UniProtKB
  • unsaturated fatty acid biosynthetic process Source: GO_Central
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. 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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi621177. Scd2.

Subcellular locationi

  • Endoplasmic reticulum membrane By similarity; Multi-pass membrane protein By similarity
  • Microsome membrane By similarity

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

GO - Cellular componenti

Complete GO annotation...

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.

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.
InterProiIPR015876. Acyl-CoA_DS.
IPR005804. FA_desaturase_dom.
IPR001522. FADS-1_CS.
[Graphical view]
PANTHERiPTHR11351. PTHR11351. 1 hit.
PfamiPF00487. FA_desaturase. 1 hit.
[Graphical view]
PRINTSiPR00075. FACDDSATRASE.
PROSITEiPS00476. FATTY_ACID_DESATUR_1. 1 hit.
[Graphical view]

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.

Cross-referencesi

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.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000067809.

Chemistry databases

SwissLipidsiSLP:000000455.

PTM databases

iPTMnetiQ6P7B9.
PhosphoSitePlusiQ6P7B9.

Proteomic databases

PaxDbiQ6P7B9.
PRIDEiQ6P7B9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi83792.
KEGGirno:83792.
UCSCiRGD:621177. rat.

Organism-specific databases

CTDi20250.
RGDi621177. Scd2.

Phylogenomic databases

eggNOGiKOG1600. Eukaryota.
COG1398. LUCA.
HOGENOMiHOG000270352.
HOVERGENiHBG003367.
InParanoidiQ6P7B9.
KOiK00507.
PhylomeDBiQ6P7B9.
TreeFamiTF313251.

Enzyme and pathway databases

BRENDAi1.14.19.1. 5301.

Miscellaneous databases

PROiQ6P7B9.

Family and domain databases

CDDicd03505. Delta9-FADS-like. 1 hit.
InterProiIPR015876. Acyl-CoA_DS.
IPR005804. FA_desaturase_dom.
IPR001522. FADS-1_CS.
[Graphical view]
PANTHERiPTHR11351. PTHR11351. 1 hit.
PfamiPF00487. FA_desaturase. 1 hit.
[Graphical view]
PRINTSiPR00075. FACDDSATRASE.
PROSITEiPS00476. FATTY_ACID_DESATUR_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiACOD2_RAT
AccessioniPrimary (citable) accession number: Q6P7B9
Secondary accession number(s): Q64066, Q9JMC9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: July 5, 2004
Last modified: November 30, 2016
This is version 94 of the entry and version 1 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. 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.