O00116 · ADAS_HUMAN
- ProteinAlkyldihydroxyacetonephosphate synthase, peroxisomal
- GeneAGPS
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids658 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the exchange of the acyl chain in acyl-dihydroxyacetonephosphate (acyl-DHAP) for a long chain fatty alcohol, yielding the first ether linked intermediate, i.e. alkyl-dihydroxyacetonephosphate (alkyl-DHAP), in the pathway of ether lipid biosynthesis.
Catalytic activity
- a 1-acylglycerone 3-phosphate + a long chain fatty alcohol = 1-O-alkylglycerone 3-phosphate + a long-chain fatty acid + H+This reaction proceeds in the forward direction.
- 1-hexadecanoylglycerone 3-phosphate + hexadecan-1-ol = 1-O-hexadecylglycerone 3-phosphate + H+ + hexadecanoateThis reaction proceeds in the forward direction.
- 1-hexadecanoylglycerone 3-phosphate + a long-chain fatty acid = a 1-acylglycerone 3-phosphate + hexadecanoateThis reaction proceeds in the forward direction.
Cofactor
Pathway
Glycerolipid metabolism; ether lipid biosynthesis.
Features
Showing features for binding site, site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 234-240 | FAD (UniProtKB | ChEBI) | ||||
Sequence: PIGGGTS | ||||||
Binding site | 303-309 | FAD (UniProtKB | ChEBI) | ||||
Sequence: DSLEFST | ||||||
Binding site | 316-319 | FAD (UniProtKB | ChEBI) | ||||
Sequence: TRAS | ||||||
Binding site | 368-374 | FAD (UniProtKB | ChEBI) | ||||
Sequence: EGTLGVI | ||||||
Site | 419 | Important for enzyme activity | ||||
Sequence: R | ||||||
Binding site | 515 | substrate | ||||
Sequence: R | ||||||
Active site | 578 | Proton donor/acceptor | ||||
Sequence: Y |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | membrane | |
Cellular Component | mitochondrion | |
Cellular Component | peroxisomal matrix | |
Cellular Component | peroxisomal membrane | |
Cellular Component | peroxisome | |
Molecular Function | alkylglycerone-phosphate synthase activity | |
Molecular Function | FAD binding | |
Biological Process | ether lipid biosynthetic process | |
Biological Process | lipid biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Chemistry
Names & Taxonomy
Protein names
- Recommended nameAlkyldihydroxyacetonephosphate synthase, peroxisomal
- EC number
- Short namesAlkyl-DHAP synthase
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO00116
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Involvement in disease
Rhizomelic chondrodysplasia punctata 3 (RCDP3)
- Note
- DescriptionA form of rhizomelic chondrodysplasia punctata, a disease characterized by severely disturbed endochondral bone formation, rhizomelic shortening of femur and humerus, vertebral disorders, dwarfism, cataract, cutaneous lesions, facial dysmorphism, and severe intellectual disability with spasticity.
- See alsoMIM:600121
Natural variants in RCDP3
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_066929 | 182 | R>Q | in RCDP3; severely reduced protein levels | |
VAR_025895 | 309 | T>I | in RCDP3; dbSNP:rs121434412 | |
VAR_005002 | 419 | R>H | in RCDP3; loss of enzyme activity; dbSNP:rs121434411 | |
VAR_025896 | 469 | L>P | in RCDP3; dbSNP:rs121434413 | |
VAR_066930 | 471 | E>K | in RCDP3; severely reduced protein levels | |
VAR_066931 | 568 | T>M | in RCDP3; does not affect protein levels; dbSNP:rs387907214 |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_066929 | 182 | in RCDP3; severely reduced protein levels | |||
Sequence: R → Q | ||||||
Natural variant | VAR_025895 | 309 | in RCDP3; dbSNP:rs121434412 | |||
Sequence: T → I | ||||||
Natural variant | VAR_005002 | 419 | in RCDP3; loss of enzyme activity; dbSNP:rs121434411 | |||
Sequence: R → H | ||||||
Natural variant | VAR_025896 | 469 | in RCDP3; dbSNP:rs121434413 | |||
Sequence: L → P | ||||||
Natural variant | VAR_066930 | 471 | in RCDP3; severely reduced protein levels | |||
Sequence: E → K | ||||||
Natural variant | VAR_066931 | 568 | in RCDP3; does not affect protein levels; dbSNP:rs387907214 | |||
Sequence: T → M |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 527 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for transit peptide, modified residue (large scale data), chain, modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Transit peptide | 1-58 | UniProt | Peroxisome | ||||
Sequence: MAEAAAAAGGTGLGAGASYGSAADRDRDPDPDRAGRRLRVLSGHLLGRPREALSTNEC | |||||||
Modified residue (large scale data) | 42 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Chain | PRO_0000020431 | 59-658 | UniProt | Alkyldihydroxyacetonephosphate synthase, peroxisomal | |||
Sequence: KARRAASAATAAPTATPAAQESGTIPKKRQEVMKWNGWGYNDSKFIFNKKGQIELTGKRYPLSGMGLPTFKEWIQNTLGVNVEHKTTSKASLNPSDTPPSVVNEDFLHDLKETNISYSQEADDRVFRAHGHCLHEIFLLREGMFERIPDIVLWPTCHDDVVKIVNLACKYNLCIIPIGGGTSVSYGLMCPADETRTIISLDTSQMNRILWVDENNLTAHVEAGITGQELERQLKESGYCTGHEPDSLEFSTVGGWVSTRASGMKKNIYGNIEDLVVHIKMVTPRGIIEKSCQGPRMSTGPDIHHFIMGSEGTLGVITEATIKIRPVPEYQKYGSVAFPNFEQGVACLREIAKQRCAPASIRLMDNKQFQFGHALKPQVSSIFTSFLDGLKKFYITKFKGFDPNQLSVATLLFEGDREKVLQHEKQVYDIAAKFGGLAAGEDNGQRGYLLTYVIAYIRDLALEYYVLGESFETSAPWDRVVDLCRNVKERITRECKEKGVQFAPFSTCRVTQTYDAGACIYFYFAFNYRGISDPLTVFEQTEAAAREEILANGGSLSHHHGVGKLRKQWLKESISDVGFGMLKSVKEYVDPNNIFGNRNLL | |||||||
Modified residue | 65 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 65 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 68 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 72 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 74 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 74 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 80 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 82 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 102 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 149 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 155 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 347 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 589 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 645 | PRIDE | Phosphotyrosine | ||||
Sequence: Y |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Homodimer.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O00116 | GORASP1 Q9BQQ3 | 7 | EBI-2838732, EBI-2561458 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-41 | Disordered | ||||
Sequence: MAEAAAAAGGTGLGAGASYGSAADRDRDPDPDRAGRRLRVL | ||||||
Compositional bias | 23-39 | Basic and acidic residues | ||||
Sequence: ADRDRDPDPDRAGRRLR | ||||||
Region | 63-86 | Disordered | ||||
Sequence: AASAATAAPTATPAAQESGTIPKK | ||||||
Domain | 202-384 | FAD-binding PCMH-type | ||||
Sequence: FERIPDIVLWPTCHDDVVKIVNLACKYNLCIIPIGGGTSVSYGLMCPADETRTIISLDTSQMNRILWVDENNLTAHVEAGITGQELERQLKESGYCTGHEPDSLEFSTVGGWVSTRASGMKKNIYGNIEDLVVHIKMVTPRGIIEKSCQGPRMSTGPDIHHFIMGSEGTLGVITEATIKIRPV | ||||||
Region | 615-617 | Important for enzyme activity | ||||
Sequence: HHH | ||||||
Region | 654-658 | Important for enzyme activity | ||||
Sequence: NRNLL |
Sequence similarities
Belongs to the FAD-binding oxidoreductase/transferase type 4 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length658
- Mass (Da)72,912
- Last updated1997-07-01 v1
- Checksum0E97AE86B513DF32
Computationally mapped potential isoform sequences
There are 11 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A2R8YEL0 | A0A2R8YEL0_HUMAN | AGPS | 676 | ||
A0A7P0T9C9 | A0A7P0T9C9_HUMAN | AGPS | 341 | ||
A0A7P0T8Q7 | A0A7P0T8Q7_HUMAN | AGPS | 245 | ||
A0A7P0T984 | A0A7P0T984_HUMAN | AGPS | 624 | ||
A0A7P0T857 | A0A7P0T857_HUMAN | AGPS | 122 | ||
A0A1B0GWA2 | A0A1B0GWA2_HUMAN | AGPS | 629 | ||
B7Z3Q4 | B7Z3Q4_HUMAN | AGPS | 568 | ||
A0A7P0TAU9 | A0A7P0TAU9_HUMAN | AGPS | 410 | ||
A0A7P0TA54 | A0A7P0TA54_HUMAN | AGPS | 251 | ||
A0A7P0TAL3 | A0A7P0TAL3_HUMAN | AGPS | 638 | ||
B8ZZ81 | B8ZZ81_HUMAN | AGPS | 189 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 23-39 | Basic and acidic residues | ||||
Sequence: ADRDRDPDPDRAGRRLR |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
Y09443 EMBL· GenBank· DDBJ | CAA70591.1 EMBL· GenBank· DDBJ | mRNA | ||
AY544121 EMBL· GenBank· DDBJ | AAT11152.1 EMBL· GenBank· DDBJ | mRNA | ||
AK314259 EMBL· GenBank· DDBJ | BAG36924.1 EMBL· GenBank· DDBJ | mRNA | ||
BC141820 EMBL· GenBank· DDBJ | AAI41821.1 EMBL· GenBank· DDBJ | mRNA |