UniProtKB - O02858 (SCD_PIG)
Stearoyl-CoA desaturase
SCD
Functioni
Stearoyl-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 similarityCatalytic activityi
- 2 Fe(II)-[cytochrome b5] + 2 H+ + O2 + octadecanoyl-CoA = (9Z)-octadecenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2OBy similarityEC:1.14.19.1By similarity
- 2 Fe(II)-[cytochrome b5] + 2 H+ + hexadecanoyl-CoA + O2 = (9Z)-hexadecenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2OBy similarity
Cofactori
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 75 | SubstrateBy similarity | 1 | |
Metal bindingi | 120 | Iron 1By similarity | 1 | |
Metal bindingi | 125 | Iron 1By similarity | 1 | |
Binding sitei | 148 | SubstrateBy similarity | 1 | |
Binding sitei | 155 | SubstrateBy similarity | 1 | |
Binding sitei | 156 | SubstrateBy similarity | 1 | |
Metal bindingi | 157 | Iron 1By similarity | 1 | |
Metal bindingi | 160 | Iron 2By similarity | 1 | |
Metal bindingi | 161 | Iron 1By similarity | 1 | |
Binding sitei | 188 | SubstrateBy similarity | 1 | |
Binding sitei | 189 | SubstrateBy similarity | 1 | |
Binding sitei | 262 | SubstrateBy similarity | 1 | |
Metal bindingi | 269 | Iron 2By similarity | 1 | |
Metal bindingi | 298 | Iron 2By similarity | 1 | |
Metal bindingi | 301 | Iron 1By similarity | 1 | |
Metal bindingi | 302 | Iron 2By similarity | 1 |
GO - Molecular functioni
- iron ion binding Source: UniProtKB
- oxidoreductase activity Source: UniProtKB
- stearoyl-CoA 9-desaturase activity Source: UniProtKB
GO - Biological processi
- unsaturated fatty acid biosynthetic process Source: UniProtKB
Keywordsi
Molecular function | Oxidoreductase |
Biological process | Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism |
Ligand | Iron, Metal-binding |
Names & Taxonomyi
Protein namesi | Recommended name: Stearoyl-CoA desaturase (EC:1.14.19.1By similarity)Alternative name(s): Acyl-CoA desaturase Delta(9)-desaturase Short name: Delta-9 desaturase Fatty acid desaturase |
Gene namesi | Name:SCD |
Organismi | Sus scrofa (Pig) |
Taxonomic identifieri | 9823 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Artiodactyla › Suina › Suidae › Sus |
Proteomesi |
|
Subcellular locationi
Endoplasmic reticulum
- Endoplasmic reticulum membrane By similarity; Multi-pass membrane protein Curated
Endoplasmic reticulum
- endoplasmic reticulum membrane Source: UniProtKB
Other locations
- integral component of membrane Source: UniProtKB
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 1 – 72 | CytoplasmicBy similarityAdd BLAST | 72 | |
Transmembranei | 73 – 93 | HelicalBy similarityAdd BLAST | 21 | |
Topological domaini | 94 – 97 | LumenalBy similarity | 4 | |
Transmembranei | 98 – 118 | HelicalBy similarityAdd BLAST | 21 | |
Topological domaini | 119 – 217 | CytoplasmicBy similarityAdd BLAST | 99 | |
Transmembranei | 218 – 237 | HelicalBy similarityAdd BLAST | 20 | |
Topological domaini | 238 – 241 | LumenalBy similarity | 4 | |
Transmembranei | 242 – 263 | HelicalBy similarityAdd BLAST | 22 | |
Topological domaini | 264 – 359 | CytoplasmicBy similarityAdd BLAST | 96 |
Keywords - Cellular componenti
Endoplasmic reticulum, MembranePTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000185399 | 1 – 359 | Stearoyl-CoA desaturaseAdd BLAST | 359 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 203 | PhosphoserineBy similarity | 1 |
Keywords - PTMi
PhosphoproteinProteomic databases
PaxDbi | O02858 |
PRIDEi | O02858 |
Expressioni
Gene expression databases
Bgeei | ENSSSCG00000010554, Expressed in adipose tissue and 47 other tissues |
Family & Domainsi
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 120 – 125 | Histidine box-1Curated | 6 | |
Motifi | 157 – 161 | Histidine box-2Curated | 5 | |
Motifi | 298 – 302 | Histidine box-3Curated | 5 |
Domaini
Sequence similaritiesi
Keywords - Domaini
Transmembrane, Transmembrane helixPhylogenomic databases
eggNOGi | KOG1600, Eukaryota |
HOGENOMi | CLU_027359_0_0_1 |
InParanoidi | O02858 |
OMAi | QGFRWWE |
OrthoDBi | 971318at2759 |
TreeFami | TF313251 |
Family and domain databases
CDDi | cd03505, Delta9-FADS-like, 1 hit |
InterProi | View protein in InterPro IPR015876, Acyl-CoA_DS IPR005804, FA_desaturase_dom IPR001522, FADS-1_CS |
PANTHERi | PTHR11351, PTHR11351, 1 hit |
Pfami | View protein in Pfam PF00487, FA_desaturase, 1 hit |
PRINTSi | PR00075, FACDDSATRASE |
PROSITEi | View protein in PROSITE PS00476, FATTY_ACID_DESATUR_1, 1 hit |
i Sequence
Sequence statusi: Complete.
10 20 30 40 50
MPAHLLQEEI SSSYTTTTTI TAPSSRVLQN GGGKLEKTPQ YVEEDIRPEM
60 70 80 90 100
KDDIYDPTYQ DKEGPRPKLE YVWRNIILMS LLHLGALYGI ILIPTCKIYT
110 120 130 140 150
LLWAFAYYLL SAVGVTAGAH RLWSHRTYKA RLPLRVFLII ANTMAFQNDV
160 170 180 190 200
YEWARDHRAH HKFSETDADP HNSRRGFFFS HVGWLLVRKH PAVKEKGGLL
210 220 230 240 250
NMSDLKAEKL VMFQRRYYKP GILLMCFILP TIVPWYCWGE AFPQSLFVAT
260 270 280 290 300
FLRYAIVLNA TWLVNSAAHL YGYRPYDKTI SPRENILVSL GAVGEGFHNY
310 320 330 340 350
HHTFPYDYSA SEYRWHINLT TFFIDCMAAL GLAYDRKKVS KAAILARIKR
TGDESYKSG
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 35 | L → S in CAB10004 (Ref. 4) | 1 | |
Sequence conflicti | 66 – 67 | RP → QG in CAB10004 (Ref. 4) | 2 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | Z97186 mRNA Translation: CAB10004.1 AY487829 mRNA Translation: AAR87713.1 AY487830 Genomic DNA Translation: AAR87714.1 JN613287 mRNA Translation: AEY68756.1 DQIR01249731 Transcribed RNA Translation: HDC05209.1 |
RefSeqi | NP_998946.1, NM_213781.1 |
Genome annotation databases
Ensembli | ENSSSCT00015091855; ENSSSCP00015037586; ENSSSCG00015068485 ENSSSCT00070027417; ENSSSCP00070022809; ENSSSCG00070014006 |
GeneIDi | 396670 |
KEGGi | ssc:396670 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | Z97186 mRNA Translation: CAB10004.1 AY487829 mRNA Translation: AAR87713.1 AY487830 Genomic DNA Translation: AAR87714.1 JN613287 mRNA Translation: AEY68756.1 DQIR01249731 Transcribed RNA Translation: HDC05209.1 |
RefSeqi | NP_998946.1, NM_213781.1 |
3D structure databases
SMRi | O02858 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 9823.ENSSSCP00000011244 |
Proteomic databases
PaxDbi | O02858 |
PRIDEi | O02858 |
Genome annotation databases
Ensembli | ENSSSCT00015091855; ENSSSCP00015037586; ENSSSCG00015068485 ENSSSCT00070027417; ENSSSCP00070022809; ENSSSCG00070014006 |
GeneIDi | 396670 |
KEGGi | ssc:396670 |
Organism-specific databases
CTDi | 6319 |
Phylogenomic databases
eggNOGi | KOG1600, Eukaryota |
HOGENOMi | CLU_027359_0_0_1 |
InParanoidi | O02858 |
OMAi | QGFRWWE |
OrthoDBi | 971318at2759 |
TreeFami | TF313251 |
Gene expression databases
Bgeei | ENSSSCG00000010554, Expressed in adipose tissue and 47 other tissues |
Family and domain databases
CDDi | cd03505, Delta9-FADS-like, 1 hit |
InterProi | View protein in InterPro IPR015876, Acyl-CoA_DS IPR005804, FA_desaturase_dom IPR001522, FADS-1_CS |
PANTHERi | PTHR11351, PTHR11351, 1 hit |
Pfami | View protein in Pfam PF00487, FA_desaturase, 1 hit |
PRINTSi | PR00075, FACDDSATRASE |
PROSITEi | View protein in PROSITE PS00476, FATTY_ACID_DESATUR_1, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | SCD_PIG | |
Accessioni | O02858Primary (citable) accession number: O02858 Secondary accession number(s): A0A4X1U207, Q6RWA7 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 15, 1998 |
Last sequence update: | February 10, 2021 | |
Last modified: | February 23, 2022 | |
This is version 114 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- SIMILARITY comments
Index of protein domains and families