P13011 · SCD2_MOUSE
- ProteinStearoyl-CoA desaturase 2
- GeneScd2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids358 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Stearoyl-CoA desaturase that utilizes O2 and electrons from reduced cytochrome b5 to introduce the first double bond into saturated fatty acyl-CoA substrates (PubMed:16443825).
Catalyzes the insertion of a cis double bond at the delta-9 position into fatty acyl-CoA substrates including palmitoyl-CoA and stearoyl-CoA (PubMed:16443825).
Gives rise to a mixture of 16:1 and 18:1 unsaturated fatty acids (PubMed:16443825).
Contributes to the biosynthesis of membrane phospholipids, cholesterol esters and triglycerides, especially during embryonic development and in neonates (PubMed:16118274).
Important for normal permeability barrier function of the skin in neonates (PubMed:16118274).
Catalyzes the insertion of a cis double bond at the delta-9 position into fatty acyl-CoA substrates including palmitoyl-CoA and stearoyl-CoA (PubMed:16443825).
Gives rise to a mixture of 16:1 and 18:1 unsaturated fatty acids (PubMed:16443825).
Contributes to the biosynthesis of membrane phospholipids, cholesterol esters and triglycerides, especially during embryonic development and in neonates (PubMed:16118274).
Important for normal permeability barrier function of the skin in neonates (PubMed:16118274).
Catalytic activity
- 2 Fe(II)-[cytochrome b5] + 2 H+ + O2 + octadecanoyl-CoA = (9Z)-octadecenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2OThis reaction proceeds in the forward direction.
- 2 Fe(II)-[cytochrome b5] + 2 H+ + hexadecanoyl-CoA + O2 = (9Z)-hexadecenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2OThis reaction proceeds in the forward direction.
Cofactor
Note: Expected to bind 2 Fe2+ ions per subunit.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 74 | substrate | ||||
Sequence: N | ||||||
Binding site | 119 | Fe cation 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 124 | Fe cation 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 147 | substrate | ||||
Sequence: N | ||||||
Binding site | 154 | substrate | ||||
Sequence: R | ||||||
Binding site | 155 | substrate | ||||
Sequence: D | ||||||
Binding site | 156 | Fe cation 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 159 | Fe cation 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 160 | Fe cation 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 187 | substrate | ||||
Sequence: R | ||||||
Binding site | 188 | substrate | ||||
Sequence: K | ||||||
Binding site | 261 | substrate | ||||
Sequence: W | ||||||
Binding site | 268 | Fe cation 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 297 | Fe cation 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 300 | Fe cation 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 301 | Fe cation 2 (UniProtKB | ChEBI) | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | endoplasmic reticulum | |
Cellular Component | endoplasmic reticulum membrane | |
Molecular Function | iron ion binding | |
Molecular Function | palmitoyl-CoA 9-desaturase activity | |
Molecular Function | stearoyl-CoA 9-desaturase activity | |
Biological Process | monounsaturated fatty acid biosynthetic process | |
Biological Process | response to fatty acid | |
Biological Process | unsaturated fatty acid biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameStearoyl-CoA desaturase 2
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionP13011
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Endoplasmic reticulum membrane ; Multi-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-71 | Cytoplasmic | ||||
Sequence: MPAHILQEISGAYSATTTITAPPSGGQQNGGEKFEKSSHHWGADVRPELKDDLYDPTYQDDEGPPPKLEYV | ||||||
Transmembrane | 72-92 | Helical | ||||
Sequence: WRNIILMALLHLGALYGITLV | ||||||
Topological domain | 93-96 | Lumenal | ||||
Sequence: PSCK | ||||||
Transmembrane | 97-117 | Helical | ||||
Sequence: LYTCLFAYLYYVISALGITAG | ||||||
Topological domain | 118-216 | Cytoplasmic | ||||
Sequence: AHRLWSHRTYKARLPLRLFLIIANTMAFQNDVYEWARDHRAHHKFSETHADPHNSRRGFFFSHVGWLLVRKHPAVKEKGGKLDMSDLKAEKLVMFQRRY | ||||||
Transmembrane | 217-236 | Helical | ||||
Sequence: YKPGLLLMCFVLPTLVPWYC | ||||||
Topological domain | 237-240 | Lumenal | ||||
Sequence: WGET | ||||||
Transmembrane | 241-262 | Helical | ||||
Sequence: FVNSLCVSTFLRYAVVLNATWL | ||||||
Topological domain | 263-358 | Cytoplasmic | ||||
Sequence: VNSAAHLYGYRPYDKNISSRENILVSMGAVGEGFHNYHHAFPYDYSASEYRWHINFTTFFIDCMALLGLAYDRKRVSRAAVLARIKRTGDGSCKSG |
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Mutant mice are born at the expected Mendelian rate. Neonates are smaller than wild-type and present high mortality, ranging from 70 to 100%, depending on the genetic background. Neonates display a shiny skin, but after a few hours their skin appears dry and cracked. The permeability barrier function of their skin is impaired, leading to rapid weight loss due to dehydration. Their epidermis has decreased levels of cholesterol esters, triglycerides, acylceramide, and glucosylacylceramide containing unsaturated fatty acids. In mutant neonates, triglyceride levels in liver and blood plasma are reduced by half, due to strongly reduced levels of stearoyl-CoA desaturase activity in the liver and strongly reduced levels of triglyceride biosynthesis. In contrast, the levels of stearoyl-CoA desaturase activity are normal in adult mice deficient for Scd2. Adult mice display kinked tails.
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 11 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000185398 | 1-358 | Stearoyl-CoA desaturase 2 | |||
Sequence: MPAHILQEISGAYSATTTITAPPSGGQQNGGEKFEKSSHHWGADVRPELKDDLYDPTYQDDEGPPPKLEYVWRNIILMALLHLGALYGITLVPSCKLYTCLFAYLYYVISALGITAGAHRLWSHRTYKARLPLRLFLIIANTMAFQNDVYEWARDHRAHHKFSETHADPHNSRRGFFFSHVGWLLVRKHPAVKEKGGKLDMSDLKAEKLVMFQRRYYKPGLLLMCFVLPTLVPWYCWGETFVNSLCVSTFLRYAVVLNATWLVNSAAHLYGYRPYDKNISSRENILVSMGAVGEGFHNYHHAFPYDYSASEYRWHINFTTFFIDCMALLGLAYDRKRVSRAAVLARIKRTGDGSCKSG |
Proteomic databases
PTM databases
Expression
Tissue specificity
Detected in brain and skin (PubMed:10545940, PubMed:11161812, PubMed:16118274).
Highly expressed in brain, and detected at low levels in heart, stomach, lung and testis (PubMed:11161812, PubMed:12815040).
Detected both in dermis and epidermis (PubMed:16118274).
Highly expressed in brain, and detected at low levels in heart, stomach, lung and testis (PubMed:11161812, PubMed:12815040).
Detected both in dermis and epidermis (PubMed:16118274).
Induction
Up-regulated by agonists that activate NR1H3 (PubMed:12815040).
Slightly down-regulated by a high-carbohydrate diet enriched in unsaturated fatty acids (PubMed:12815040).
Slightly down-regulated by a high-carbohydrate diet enriched in unsaturated fatty acids (PubMed:12815040).
Developmental stage
Highly expressed during embryonic development and during the first three weeks after birth. Expression is low in adults.
Gene expression databases
Structure
Family & Domains
Features
Showing features for compositional bias, region, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 16-32 | Polar residues | ||||
Sequence: TTTITAPPSGGQQNGGE | ||||||
Region | 16-39 | Disordered | ||||
Sequence: TTTITAPPSGGQQNGGEKFEKSSH | ||||||
Motif | 119-124 | Histidine box-1 | ||||
Sequence: HRLWSH | ||||||
Motif | 156-160 | Histidine box-2 | ||||
Sequence: HRAHH | ||||||
Motif | 297-301 | Histidine box-3 | ||||
Sequence: HNYHH |
Domain
The histidine box domains are involved in binding the catalytic metal ions.
Sequence similarities
Belongs to the fatty acid desaturase type 1 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length358
- Mass (Da)40,916
- Last updated2011-07-27 v2
- Checksum3E04893F12E92A9A
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A494BAV5 | A0A494BAV5_MOUSE | Scd2 | 215 |
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 16-32 | Polar residues | ||||
Sequence: TTTITAPPSGGQQNGGE | ||||||
Sequence conflict | 220 | in Ref. 1; AAA40094 | ||||
Sequence: G → D | ||||||
Sequence conflict | 295 | in Ref. 1; AAA40094 | ||||
Sequence: G → R |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M26270 EMBL· GenBank· DDBJ | AAA40094.1 EMBL· GenBank· DDBJ | mRNA | ||
AK083922 EMBL· GenBank· DDBJ | BAC39066.1 EMBL· GenBank· DDBJ | mRNA | ||
AK147406 EMBL· GenBank· DDBJ | BAE27893.1 EMBL· GenBank· DDBJ | mRNA | ||
CH466534 EMBL· GenBank· DDBJ | EDL41928.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC040384 EMBL· GenBank· DDBJ | AAH40384.1 EMBL· GenBank· DDBJ | mRNA |