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Protein

Acyl-CoA desaturase

Gene

SCD

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 4 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 sitei64SubstrateBy similarity1
Metal bindingi109Iron 1By similarity1
Metal bindingi114Iron 1By similarity1
Binding sitei137SubstrateBy similarity1
Binding sitei144SubstrateBy similarity1
Binding sitei145SubstrateBy similarity1
Metal bindingi146Iron 1By similarity1
Metal bindingi149Iron 2By similarity1
Metal bindingi150Iron 1By similarity1
Binding sitei177SubstrateBy similarity1
Binding sitei178SubstrateBy similarity1
Binding sitei251SubstrateBy similarity1
Metal bindingi258Iron 2By similarity1
Metal bindingi287Iron 2By similarity1
Metal bindingi290Iron 1By similarity1
Metal bindingi291Iron 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 desaturase
Gene namesi
Name:SCD
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 61CytoplasmicBy similarityAdd BLAST61
Transmembranei62 – 82HelicalBy similarityAdd BLAST21
Topological domaini83 – 86LumenalBy similarity4
Transmembranei87 – 107HelicalBy similarityAdd BLAST21
Topological domaini108 – 206CytoplasmicBy similarityAdd BLAST99
Transmembranei207 – 226HelicalBy similarityAdd BLAST20
Topological domaini227 – 230LumenalBy similarity4
Transmembranei231 – 252HelicalBy similarityAdd BLAST22
Topological domaini253 – 334CytoplasmicBy similarityAdd BLAST82

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000185399‹1 – ›334Acyl-CoA desaturaseAdd BLAST›334

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei192PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO02858.
PRIDEiO02858.

Interactioni

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000011244.

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi109 – 114Histidine box-1Curated6
Motifi146 – 150Histidine box-2Curated5
Motifi287 – 291Histidine 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.
HOVERGENiHBG003367.
InParanoidiO02858.

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: Fragment.

O02858-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
SSYTTTTTIT APSSRVLQNG GGKSEKTPQY VEEDIRPEMK DDIYDPTYQD
60 70 80 90 100
KEGPQGKLEY VWRNIILMSL LHLGALYGII LIPTCKIYTL LWAFAYYLLS
110 120 130 140 150
AVGVTAGAHR LWSHRTYKAR LPLRVFLIIA NTMAFQNDVY EWARDHRAHH
160 170 180 190 200
KFSETDADPH NSRRGFFFSH VGWLLVRKHP AVKEKGGLLN MSDLKAEKLV
210 220 230 240 250
MFQRRYYKPG ILLMCFILPT IVPWYCWGEA FPQSLFVATF LRYAIVLNAT
260 270 280 290 300
WLVNSAAHLY GYRPYDKTIS PRENILVSLG AVGEGFHNYH HTFPYDYSAS
310 320 330
EYRWHINLTT FFIDCMAALG LAYDRKKVSK AAIL
Length:334
Mass (Da):38,482
Last modified:July 1, 1997 - v1
Checksum:i79183E3918469977
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11
Non-terminal residuei3341

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z97186 mRNA. Translation: CAB10004.1.
UniGeneiSsc.16159.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z97186 mRNA. Translation: CAB10004.1.
UniGeneiSsc.16159.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000011244.

Proteomic databases

PaxDbiO02858.
PRIDEiO02858.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG1600. Eukaryota.
COG1398. LUCA.
HOVERGENiHBG003367.
InParanoidiO02858.

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_PIG
AccessioniPrimary (citable) accession number: O02858
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 1, 1997
Last modified: November 30, 2016
This is version 99 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.