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Protein

Acyl-CoA desaturase 4

Gene

Scd4

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. 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:12815040, PubMed:16443825). Required for the biosynthesis of membrane phospholipids, cholesterol esters and triglycerides (By similarity).By similarity2 Publications

Catalytic activityi

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

Cofactori

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei69SubstrateBy similarity1
Metal bindingi114Iron 1By similarity1
Metal bindingi119Iron 1By similarity1
Binding sitei142SubstrateBy similarity1
Binding sitei149SubstrateBy similarity1
Binding sitei150SubstrateBy similarity1
Metal bindingi151Iron 1By similarity1
Metal bindingi154Iron 2By similarity1
Metal bindingi155Iron 1By similarity1
Binding sitei182SubstrateBy similarity1
Binding sitei183SubstrateBy similarity1
Binding sitei256SubstrateBy similarity1
Metal bindingi263Iron 2By similarity1
Metal bindingi292Iron 2By similarity1
Metal bindingi295Iron 1By similarity1
Metal bindingi296Iron 2By similarity1

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

  • cellular response to nutrient Source: UniProtKB
  • fatty acid biosynthetic process Source: MGI
  • monounsaturated fatty acid biosynthetic process 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. 3474.
ReactomeiR-MMU-75105. Fatty acyl-CoA biosynthesis.

Chemistry databases

SwissLipidsiSLP:000001657.

Names & Taxonomyi

Protein namesi
Recommended name:
Acyl-CoA desaturase 4Curated (EC:1.14.19.12 Publications)
Alternative name(s):
Delta(9)-desaturase 41 Publication
Short name:
Delta-9 desaturase 41 Publication
Fatty acid desaturase 4Curated
Stearoyl-CoA desaturase 41 Publication
Gene namesi
Name:Scd4Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:2670997. Scd4.

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 – 66CytoplasmicBy similarityAdd BLAST66
Transmembranei67 – 87HelicalBy similarityAdd BLAST21
Topological domaini88 – 91LumenalBy similarity4
Transmembranei92 – 112HelicalBy similarityAdd BLAST21
Topological domaini113 – 211CytoplasmicBy similarityAdd BLAST99
Transmembranei212 – 231HelicalBy similarityAdd BLAST20
Topological domaini232 – 235LumenalBy similarity4
Transmembranei236 – 257HelicalBy similarityAdd BLAST22
Topological domaini258 – 353CytoplasmicBy similarityCuratedAdd BLAST96

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004338721 – 353Acyl-CoA desaturase 4Add BLAST353

Proteomic databases

MaxQBiQ6T707.
PaxDbiQ6T707.
PRIDEiQ6T707.

PTM databases

iPTMnetiQ6T707.
PhosphoSitePlusiQ6T707.

Expressioni

Tissue specificityi

Detected in heart, but not in brain, liver, skin or adipose tissue.1 Publication

Inductioni

Up-regulated by agonists that activate NR1H3. Up-regulated by a fat-free high-carbohydrate diet. Not down-regulated by a high-carbohydrate diet supplemented with unsaturated fatty acids. Down-regulated by leptin.1 Publication

Gene expression databases

BgeeiENSMUSG00000050195.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000059860.

Structurei

3D structure databases

ProteinModelPortaliQ6T707.
SMRiQ6T707.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi114 – 119Histidine box-1Curated6
Motifi151 – 155Histidine box-2Curated5
Motifi292 – 296Histidine box-3Curated5

Domaini

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

Sequence similaritiesi

Belongs to the fatty acid desaturase type 1 family.UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1600. Eukaryota.
COG1398. LUCA.
GeneTreeiENSGT00530000063158.
HOGENOMiHOG000270352.
HOVERGENiHBG003367.
KOiK00507.
OMAiILMPIFC.
OrthoDBiEOG091G0B5S.
PhylomeDBiQ6T707.
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.

Q6T707-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTAHLPQEIS SRCSTTNIME PHSRRQQDGE EKMPLQAEDI RPEIKDDLYD
60 70 80 90 100
PSYQDEEGPP PKLEYVWRNI IFMALLHVGA LYGITLVPSC KVYTWLLGVF
110 120 130 140 150
YNVVAGLGIT AGAHRLWSHR TYKARLPLRI FLIMANTMAF QNDVYEWARD
160 170 180 190 200
HRAHHKFSET HADPHNSRRG FFFSHVGWLL VRKHPAVKEK GKNLDMSDLK
210 220 230 240 250
AEKLVMFQRR YYKLAVTLMF IILPTLVPWY LWGETFQHSL CVSNFLRYAV
260 270 280 290 300
LLNFTWLVNS AAHLYGYRPY DRGIGARENP FVSMASLGEG FHNYHHTFPY
310 320 330 340 350
DYSVSEYRWH INFTTFFIDC MAALGLAYDR KKVSKAVVLA RIKRTGDGSH

KSS
Length:353
Mass (Da):41,042
Last modified:July 5, 2004 - v1
Checksum:iEEF07F95776A4E0D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti193N → S in EDL41929 (Ref. 3) Curated1
Sequence conflicti193N → S in AAI41235 (PubMed:15489334).Curated1
Sequence conflicti219M → T in EDL41929 (Ref. 3) Curated1
Sequence conflicti219M → T in AAI41235 (PubMed:15489334).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY430080 mRNA. Translation: AAR06950.1.
AC123853 Genomic DNA. No translation available.
CH466534 Genomic DNA. Translation: EDL41929.1.
BC141234 mRNA. Translation: AAI41235.1.
CCDSiCCDS29849.1.
RefSeqiNP_899039.2. NM_183216.3.
UniGeneiMm.313583.

Genome annotation databases

EnsembliENSMUST00000058856; ENSMUSP00000059860; ENSMUSG00000050195.
GeneIDi329065.
KEGGimmu:329065.
UCSCiuc008hpq.1. mouse.

Similar proteinsi

Entry informationi

Entry nameiSCD4_MOUSE
AccessioniPrimary (citable) accession number: Q6T707
Secondary accession number(s): B9EIY5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 16, 2015
Last sequence update: July 5, 2004
Last modified: June 7, 2017
This is version 95 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

Documents

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