UniProtKB - Q64420 (SCD_MESAU)
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 | 70 | SubstrateBy similarity | 1 | |
Metal bindingi | 115 | Iron 1By similarity | 1 | |
Metal bindingi | 120 | Iron 1By similarity | 1 | |
Binding sitei | 143 | SubstrateBy similarity | 1 | |
Binding sitei | 150 | SubstrateBy similarity | 1 | |
Binding sitei | 151 | SubstrateBy similarity | 1 | |
Metal bindingi | 152 | Iron 1By similarity | 1 | |
Metal bindingi | 155 | Iron 2By similarity | 1 | |
Metal bindingi | 156 | Iron 1By similarity | 1 | |
Binding sitei | 183 | SubstrateBy similarity | 1 | |
Binding sitei | 184 | SubstrateBy similarity | 1 | |
Binding sitei | 257 | SubstrateBy similarity | 1 | |
Metal bindingi | 264 | Iron 2By similarity | 1 | |
Metal bindingi | 293 | Iron 2By similarity | 1 | |
Metal bindingi | 296 | Iron 1By similarity | 1 | |
Metal bindingi | 297 | 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 |
Enzyme and pathway databases
BRENDAi | 1.14.19.1, 3239 |
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 Synonyms:FAR-17c1 Publication |
Organismi | Mesocricetus auratus (Golden hamster) |
Taxonomic identifieri | 10036 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Cricetidae › Cricetinae › Mesocricetus |
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 – 67 | CytoplasmicBy similarityAdd BLAST | 67 | |
Transmembranei | 68 – 88 | HelicalBy similarityAdd BLAST | 21 | |
Topological domaini | 89 – 92 | LumenalBy similarity | 4 | |
Transmembranei | 93 – 113 | HelicalBy similarityAdd BLAST | 21 | |
Topological domaini | 114 – 212 | CytoplasmicBy similarityAdd BLAST | 99 | |
Transmembranei | 213 – 232 | HelicalBy similarityAdd BLAST | 20 | |
Topological domaini | 233 – 236 | LumenalBy similarity | 4 | |
Transmembranei | 237 – 258 | HelicalBy similarityAdd BLAST | 22 | |
Topological domaini | 259 – 354 | CytoplasmicBy similarityAdd BLAST | 96 |
Keywords - Cellular componenti
Endoplasmic reticulum, MembranePTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000185396 | 1 – 354 | Stearoyl-CoA desaturaseAdd BLAST | 354 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 198 | PhosphoserineBy similarity | 1 |
Keywords - PTMi
PhosphoproteinFamily & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1 – 28 | DisorderedSequence analysisAdd BLAST | 28 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 115 – 120 | Histidine box-1Curated | 6 | |
Motifi | 152 – 156 | Histidine box-2Curated | 5 | |
Motifi | 293 – 297 | Histidine box-3Curated | 5 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 8 – 28 | Polar residuesSequence analysisAdd BLAST | 21 |
Domaini
Sequence similaritiesi
Keywords - Domaini
Transmembrane, Transmembrane helixPhylogenomic databases
eggNOGi | KOG1600, Eukaryota |
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
MPGHLLQEEM TSSYTTTTTT ITEPPSESLQ KTVPLYLEED IRPEMKEDIY
60 70 80 90 100
DPSYQDEEGP PPKLEYVWRN IILMALLHLG ALYGLVLVPS SKVYTLLWAF
110 120 130 140 150
VYYVISIEGI GAGVHRLWSH RTYKARLPLR IFLIIANTMA FQNDVYEWAR
160 170 180 190 200
DHRAHHKFSE TYADPHDSRR GFFFSHVGWL LVRKHPAVKE KGGKLDMSDL
210 220 230 240 250
KAEKLVMFQR RYYKPAILLM CFILPTFVPW YFWGEAFVNS LCVSTFLRYT
260 270 280 290 300
LVLNATWLVN SAAHLYGYRP YDKNIDPREN ALVSLGCLGE GFHNYHHAFP
310 320 330 340 350
YDYSASEYRW HINFTTFFID CMAALGLAYD RKKVSKAAVL ARIKRTGDGS
CKSG
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | L26956 mRNA Translation: AAC42058.1 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | L26956 mRNA Translation: AAC42058.1 |
3D structure databases
SMRi | Q64420 |
ModBasei | Search... |
Phylogenomic databases
eggNOGi | KOG1600, Eukaryota |
Enzyme and pathway databases
BRENDAi | 1.14.19.1, 3239 |
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_MESAU | |
Accessioni | Q64420Primary (citable) accession number: Q64420 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 15, 1998 |
Last sequence update: | November 1, 1996 | |
Last modified: | February 23, 2022 | |
This is version 104 of the entry and version 1 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