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Protein

Acyl-CoA desaturase 3

Gene

Scd3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -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 (PubMed:16443825, PubMed:26098370). Has a strong preference for saturated fatty acids with chain lengths of 14 or 16 carbon atoms (C14:0 and C16:0), and has only very low activity with stearatate (C18:0) (PubMed:16443825, PubMed:26098370). Required for the biosynthesis of membrane phospholipids, cholesterol esters and triglycerides (By similarity).By similarity2 Publications

Catalytic activityi

Palmitoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = palmitoleoyl-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 sitei75SubstrateBy similarity1
Metal bindingi120Iron 1By similarity1
Metal bindingi125Iron 1By similarity1
Binding sitei148SubstrateBy similarity1
Binding sitei155SubstrateBy similarity1
Binding sitei156SubstrateBy similarity1
Metal bindingi157Iron 1By similarity1
Metal bindingi160Iron 2By similarity1
Metal bindingi161Iron 1By similarity1
Binding sitei188SubstrateBy similarity1
Binding sitei189SubstrateBy similarity1
Binding sitei262SubstrateBy similarity1
Metal bindingi269Iron 2By similarity1
Metal bindingi298Iron 2By similarity1
Metal bindingi301Iron 1By similarity1
Metal bindingi302Iron 2By similarity1

GO - Molecular functioni

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

GO - Biological processi

  • monounsaturated fatty acid biosynthetic process Source: MGI

Keywordsi

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

Enzyme and pathway databases

ReactomeiR-MMU-75105 Fatty acyl-CoA biosynthesis

Names & Taxonomyi

Protein namesi
Recommended name:
Acyl-CoA desaturase 3Curated (EC:1.14.19.-2 Publications)
Alternative name(s):
Delta(9)-desaturase 31 Publication
Short name:
Delta-9 desaturase 31 Publication
Fatty acid desaturase 3Curated
Palmitoyl-CoA desaturase1 Publication
Stearoyl-CoA desaturase 31 Publication
Gene namesi
Name:Scd3Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:1353437 Scd3

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 – 72CytoplasmicBy similarityAdd BLAST72
Transmembranei73 – 93HelicalBy similarityAdd BLAST21
Topological domaini94 – 97LumenalBy similarity4
Transmembranei98 – 118HelicalBy similarityAdd BLAST21
Topological domaini119 – 217CytoplasmicBy similarityAdd BLAST99
Transmembranei218 – 237HelicalBy similarityAdd BLAST20
Topological domaini238 – 241LumenalBy similarity4
Transmembranei242 – 263HelicalBy similarityAdd BLAST22
Topological domaini264 – 359CytoplasmicBy similarityAdd BLAST96

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi112 – 113IE → AL: Changes substrate specificity so that stearate becomes a good substrate. 2

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004338711 – 359Acyl-CoA desaturase 3Add BLAST359

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei203PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ99PL7
PRIDEiQ99PL7

PTM databases

iPTMnetiQ99PL7
PhosphoSitePlusiQ99PL7

Expressioni

Tissue specificityi

Detected in skin, but at lower levels compared to Scd1. Detected in the middlle part of the sebaceous gland, but not in hair follicle. Not detected in liver and brain.1 Publication

Developmental stagei

Expression is increased during the first eight days (anagen) of the hair cycle in male mice, and is low during the quiescent phase (telogen) of the hair cycle. Expression is very low throughout the hair cycle in female mice.1 Publication

Gene expression databases

BgeeiENSMUSG00000025202
GenevisibleiQ99PL7 MM

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000026220

Structurei

3D structure databases

ProteinModelPortaliQ99PL7
SMRiQ99PL7
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi120 – 125Histidine box-1Curated6
Motifi157 – 161Histidine box-2Curated5
Motifi298 – 302Histidine 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
OMAiILMFQRK
OrthoDBiEOG091G0B5S
PhylomeDBiQ99PL7
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

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q99PL7-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MPGHLLQEEM TPSYTTTTTI TAPPSGSLQN GREKVKTVPL YLEEDIRPEM
60 70 80 90 100
KEDIYDPTYQ DEEGPPPKLE YVWRNIILMA LLHVGALYGI TLVPSCKLYT
110 120 130 140 150
CLFAFVYYVI SIEGIGAGVH RLWSHRTYKA RLPLRIFLII ANTMAFQNDV
160 170 180 190 200
YEWARDHRAH HKFSETHADP HNSRRGFFFS HVGWLLVRKH PAVKEKGGKL
210 220 230 240 250
DMSDLKAEKL VMFQRRYYKP GILLMCFILP TLVPWYCWGE TFLNSFYVAT
260 270 280 290 300
LLRYAVVLNA TWLVNSAAHL YGYRPYDKNI DPRQNALVSL GSMGEGFHNY
310 320 330 340 350
HHAFPYDYSA SEYRWHINFT TFFIDCMAAL GLAYDRKRVS KATVLARIKR

TGDGSHKSG
Length:359
Mass (Da):41,432
Last modified:June 1, 2001 - v1
Checksum:i60E30AD688587E0F
GO
Isoform 2 (identifier: Q99PL7-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-224: Missing.

Show »
Length:135
Mass (Da):15,502
Checksum:iDC6F1DBFFF71EFFD
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti124S → G in BAE22909 (PubMed:16141072).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0578481 – 224Missing in isoform 2. Add BLAST224

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF272037 mRNA Translation: AAK13256.1
AK015784 mRNA Translation: BAB29975.1
AK136277 mRNA Translation: BAE22909.1
AC123853 Genomic DNA No translation available.
AC125101 Genomic DNA No translation available.
CH468367 Genomic DNA Translation: EDL01300.1
BC118033 mRNA Translation: AAI18034.1
BC118045 mRNA Translation: AAI18046.1
CCDSiCCDS29847.1 [Q99PL7-1]
RefSeqiNP_077770.1, NM_024450.2 [Q99PL7-1]
UniGeneiMm.480594

Genome annotation databases

EnsembliENSMUST00000026220; ENSMUSP00000026220; ENSMUSG00000025202 [Q99PL7-1]
GeneIDi30049
KEGGimmu:30049
UCSCiuc008hpn.1 mouse [Q99PL7-1]
uc008hpo.1 mouse

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiSCD3_MOUSE
AccessioniPrimary (citable) accession number: Q99PL7
Secondary accession number(s): Q3UWK5, Q9D550
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 16, 2015
Last sequence update: June 1, 2001
Last modified: March 28, 2018
This is version 118 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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health