E7EMA0 · E7EMA0_HUMAN
- ProteinSphingolipid delta(4)-desaturase DES1
- GeneDEGS1
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids261 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
Catalytic activity
- 11-cis-retinol = 13-cis-retinolThis reaction proceeds in the forward direction.
- 11-cis-retinol = 9-cis-retinolThis reaction proceeds in the forward direction.
- all-trans-retinol = 11-cis-retinolThis reaction proceeds in the forward and the backward directions.
- all-trans-retinol = 13-cis-retinolThis reaction proceeds in the forward direction.
- all-trans-retinol = 9-cis-retinolThis reaction proceeds in the forward direction.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | membrane | |
Molecular Function | isomerase activity | |
Molecular Function | sphingolipid delta-4 desaturase activity | |
Biological Process | sphingolipid biosynthetic process |
Keywords
- Molecular function
- Biological process
Names & Taxonomy
Protein names
- Recommended nameSphingolipid delta(4)-desaturase DES1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionE7EMA0
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 21-41 | Helical | ||||
Sequence: NLIWIIIMMVLTQLGAFYIVK | ||||||
Transmembrane | 47-71 | Helical | ||||
Sequence: WVIFGAYAFGSCINHSMTLAIHEIA | ||||||
Transmembrane | 83-101 | Helical | ||||
Sequence: WNRWFGMFANLPIGIPYSI | ||||||
Transmembrane | 129-151 | Helical | ||||
Sequence: GWFFCTAFRKFIWVILQPLFYAF | ||||||
Transmembrane | 163-183 | Helical | ||||
Sequence: YLEVINTVAQVTFDILIYYFL | ||||||
Transmembrane | 189-210 | Helical | ||||
Sequence: VYMLAASLLGLGLHPISGHFIA |
Keywords
- Cellular component
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 218 variants from UniProt as well as other sources including ClinVar and dbSNP.
Genetic variation databases
PTM/Processing
Proteomic databases
Expression
Gene expression databases
Interaction
Subunit
Interacts with RLBP1; the interaction increases synthesis of chromophore-precursors by DEGS1.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 47-259 | Fatty acid desaturase | ||||
Sequence: WVIFGAYAFGSCINHSMTLAIHEIAHNAAFGNCKAMWNRWFGMFANLPIGIPYSISFKRYHMDHHRYLGADGVDVDIPTDFEGWFFCTAFRKFIWVILQPLFYAFRPLFINPKPITYLEVINTVAQVTFDILIYYFLGIKSLVYMLAASLLGLGLHPISGHFIAEHYMFLKGHETYSYYGPLNLLTFNVGYHNEHHDFPNIPGKSLPLVRKIA |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusFragment
- Length261
- Mass (Da)30,124
- Last updated2011-03-08 v1
- Checksum89F86A3653B608E1
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
O15121 | DEGS1_HUMAN | DEGS1 | 323 |
Features
Showing features for non-terminal residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Non-terminal residue | 261 | |||||
Sequence: E |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AC092809 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |