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Protein

Acyl-CoA desaturase

Gene

SCD

Organism
Sus scrofa (Pig)
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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei64 – 641SubstrateBy similarity
Metal bindingi109 – 1091Iron 1By similarity
Metal bindingi114 – 1141Iron 1By similarity
Binding sitei137 – 1371SubstrateBy similarity
Binding sitei144 – 1441SubstrateBy similarity
Binding sitei145 – 1451SubstrateBy similarity
Metal bindingi146 – 1461Iron 1By similarity
Metal bindingi149 – 1491Iron 2By similarity
Metal bindingi150 – 1501Iron 1By similarity
Binding sitei177 – 1771SubstrateBy similarity
Binding sitei178 – 1781SubstrateBy similarity
Binding sitei251 – 2511SubstrateBy similarity
Metal bindingi258 – 2581Iron 2By similarity
Metal bindingi287 – 2871Iron 2By similarity
Metal bindingi290 – 2901Iron 1By similarity
Metal bindingi291 – 2911Iron 2By similarity

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)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 6161CytoplasmicBy similarityAdd
BLAST
Transmembranei62 – 8221HelicalBy similarityAdd
BLAST
Topological domaini83 – 864LumenalBy similarity
Transmembranei87 – 10721HelicalBy similarityAdd
BLAST
Topological domaini108 – 20699CytoplasmicBy similarityAdd
BLAST
Transmembranei207 – 22620HelicalBy similarityAdd
BLAST
Topological domaini227 – 2304LumenalBy similarity
Transmembranei231 – 25222HelicalBy similarityAdd
BLAST
Topological domaini253 – 33482CytoplasmicBy similarityAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – ›334›334Acyl-CoA desaturasePRO_0000185399Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei192 – 1921PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO02858.

Interactioni

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000011244.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi109 – 1146Histidine box-1Curated
Motifi146 – 1505Histidine box-2Curated
Motifi287 – 2915Histidine box-3Curated

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

InterProiIPR001522. Fatty_acid_desaturase-1_C.
IPR015876. Fatty_acid_desaturase-1_core.
IPR005804. Fatty_acid_desaturase_dom.
[Graphical view]
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)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11
Non-terminal residuei334 – 3341

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.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

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

Family and domain databases

InterProiIPR001522. Fatty_acid_desaturase-1_C.
IPR015876. Fatty_acid_desaturase-1_core.
IPR005804. Fatty_acid_desaturase_dom.
[Graphical view]
PfamiPF00487. FA_desaturase. 1 hit.
[Graphical view]
PRINTSiPR00075. FACDDSATRASE.
PROSITEiPS00476. FATTY_ACID_DESATUR_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Fumiere O.
    Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

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: March 16, 2016
This is version 96 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.