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Protein

Acyl-CoA desaturase

Gene

SCD

Organism
Ovis aries (Sheep)
Status
Reviewed-Annotation score: Annotation score: 3 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 (By similarity). Gives rise to a mixture of 16:1 and 18:1 unsaturated fatty acids. Plays an important role in lipid biosynthesis. Plays an important role in regulating the expression of genes that are involved in lipogenesis and in regulating mitochondrial fatty acid oxidation (By similarity). Plays an important role in body energy homeostasis (By similarity). Contributes to the biosynthesis of membrane phospholipids, cholesterol esters and triglycerides (By similarity).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 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

GO - Biological processi

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

Names & Taxonomyi

Protein namesi
Recommended name:
Acyl-CoA desaturase (EC:1.14.19.1By similarity)
Alternative name(s):
Delta(9)-desaturase
Short name:
Delta-9 desaturase
Fatty acid desaturase
Stearoyl-CoA desaturase1 Publication
Gene namesi
Name:SCD
OrganismiOvis aries (Sheep)
Taxonomic identifieri9940 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeCaprinaeOvis
Proteomesi
  • UP000002356 Componenti: Unplaced

Subcellular locationi

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

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001854021 – 359Acyl-CoA desaturaseAdd BLAST359

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei203PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Structurei

3D structure databases

ProteinModelPortaliO62849.
SMRiO62849.
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

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

HOVERGENiHBG003367.
KOiK00507.

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.

O62849-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPAHLLQEEI SSSYTTTTTI TAPPSRVLQN GGGKLEKTPL YLEEDIRPEM
60 70 80 90 100
RDDIYDPNYQ DKEGPKPKLE YVWRNIILMG LLHLGALYGI TLIPTCKIYT
110 120 130 140 150
FLWVLFYYVI SALGITAGVH RLWSHRTYKA RLPLRVFLII ANTMAFQNDV
160 170 180 190 200
FEWSRDHRAH HKFSETDADP HNSRRGFFFS HVGWLLVRKH PAVREKGATL
210 220 230 240 250
DLSDLRAEKL VMFQRRYYKP GVLLLCFILP TLVPWYLWGE SFQNSLFFAT
260 270 280 290 300
FLRYAVVLNA TWLVNSAAHM YGYRPYDKTI NPRENILVSL GAVGEGFHNY
310 320 330 340 350
HHTFPYDYSA SEYRWHINFT TFFIDCMAAI GLAYDRKKVS KAAVLGRMKR

TGEESYKSG
Length:359
Mass (Da):41,671
Last modified:August 1, 1998 - v1
Checksum:i219CFEBB1E353418
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ001048 mRNA. Translation: CAA04502.1.
RefSeqiNP_001009254.1. NM_001009254.1.
UniGeneiOar.610.

Genome annotation databases

GeneIDi443185.
KEGGioas:443185.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ001048 mRNA. Translation: CAA04502.1.
RefSeqiNP_001009254.1. NM_001009254.1.
UniGeneiOar.610.

3D structure databases

ProteinModelPortaliO62849.
SMRiO62849.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi443185.
KEGGioas:443185.

Organism-specific databases

CTDi6319.

Phylogenomic databases

HOVERGENiHBG003367.
KOiK00507.

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 nameiACOD_SHEEP
AccessioniPrimary (citable) accession number: O62849
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: August 1, 1998
Last modified: November 30, 2016
This is version 95 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.