Q5M828 · ADTRP_RAT
- ProteinAndrogen-dependent TFPI-regulating protein
- GeneAdtrp
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids230 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
Function
function
Hydrolyzes bioactive fatty-acid esters of hydroxy-fatty acids (FAHFAs), but not other major classes of lipids (By similarity).
Shows a preference for FAHFAs with branching distal from the carboxylate head group of the lipids (By similarity).
Regulates the expression and the cell-associated anticoagulant activity of the inhibitor TFPI in endothelial cells (in vitro) (By similarity).
Shows a preference for FAHFAs with branching distal from the carboxylate head group of the lipids (By similarity).
Regulates the expression and the cell-associated anticoagulant activity of the inhibitor TFPI in endothelial cells (in vitro) (By similarity).
Catalytic activity
- 9-hexadecanoyloxy-octadecanoate + H2O = 9-hydroxy-octadecanoate + H+ + hexadecanoateThis reaction proceeds in the forward direction.
- 12-hexadecanoyloxy-octadecanoate + H2O = 12-hydroxyoctadecanoate + H+ + hexadecanoateThis reaction proceeds in the forward direction.
- 9-(9Z-hexadecenoyloxy)-octadecanoate + H2O = (9Z)-hexadecenoate + 9-hydroxy-octadecanoate + H+This reaction proceeds in the forward direction.
- 12-(9Z-hexadecenoyloxy)-octadecanoate + H2O = (9Z)-hexadecenoate + 12-hydroxyoctadecanoate + H+This reaction proceeds in the forward direction.
- 13-(9Z-hexadecenoyloxy)-octadecanoate + H2O = (9Z)-hexadecenoate + 13-hydroxy-octadecanoate + H+This reaction proceeds in the forward direction.
- 9-octadecanoyloxy-octadecanoate + H2O = 9-hydroxy-octadecanoate + H+ + octadecanoateThis reaction proceeds in the forward direction.
- 12-octadecanoyloxy-octadecanoate + H2O = 12-hydroxyoctadecanoate + H+ + octadecanoateThis reaction proceeds in the forward direction.
- 13-octadecanoyloxy-octadecanoate + H2O = 13-hydroxy-octadecanoate + H+ + octadecanoateThis reaction proceeds in the forward direction.
- 9-(9Z-octadecenoyloxy)-octadecanoate + H2O = (9Z)-octadecenoate + 9-hydroxy-octadecanoate + H+This reaction proceeds in the forward direction.
- 12-(9Z-octadecenoyloxy)-octadecanoate + H2O = (9Z)-octadecenoate + 12-hydroxyoctadecanoate + H+This reaction proceeds in the forward direction.
- 13-(9Z-octadecenoyloxy)-octadecanoate + H2O = (9Z)-octadecenoate + 13-hydroxy-octadecanoate + H+This reaction proceeds in the forward direction.
- 5-(9Z-octadecenoyloxy)-octadecanoate + H2O = (9Z)-octadecenoate + 5-hydroxy-octadecanoate + H+This reaction proceeds in the forward direction.
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 47 | Important for catalytic activity | ||||
Sequence: T | ||||||
Site | 131 | Important for catalytic activity | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | caveola | |
Cellular Component | cell surface | |
Cellular Component | endomembrane system | |
Cellular Component | membrane | |
Molecular Function | hydrolase activity | |
Biological Process | cell migration involved in sprouting angiogenesis | |
Biological Process | cellular response to oxidised low-density lipoprotein particle stimulus | |
Biological Process | cellular response to steroid hormone stimulus | |
Biological Process | long-chain fatty acid catabolic process | |
Biological Process | negative regulation of blood coagulation | |
Biological Process | negative regulation of extracellular matrix constituent secretion | |
Biological Process | negative regulation of leukocyte cell-cell adhesion | |
Biological Process | negative regulation of leukocyte migration | |
Biological Process | negative regulation of lymphocyte migration | |
Biological Process | negative regulation of protein secretion | |
Biological Process | positive regulation of gene expression | |
Biological Process | positive regulation of protein phosphorylation |
Keywords
- Molecular function
- Biological process
Names & Taxonomy
Protein names
- Recommended nameAndrogen-dependent TFPI-regulating protein
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionQ5M828
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Multi-pass membrane protein
Note: Colocalized with TFPI and CAV1 in lipid rafts.
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-7 | Cytoplasmic | ||||
Sequence: MTKTTTC | ||||||
Transmembrane | 8-28 | Helical | ||||
Sequence: LYHFVVLNWYIFLNYYIPQIG | ||||||
Topological domain | 29-45 | Extracellular | ||||
Sequence: KDEEKLKEFHDGGRSKY | ||||||
Transmembrane | 46-66 | Helical | ||||
Sequence: LTLLNLLLQAVFFGVACLDDV | ||||||
Topological domain | 67-85 | Cytoplasmic | ||||
Sequence: LKRVIGRKDIKFITYFRDL | ||||||
Transmembrane | 86-106 | Helical | ||||
Sequence: LFTTLAFPLSTFVFLVFWSLF | ||||||
Topological domain | 107-120 | Extracellular | ||||
Sequence: HYDRSLVYPKGLDD | ||||||
Transmembrane | 121-141 | Helical | ||||
Sequence: FFPAWVNHAMHTSIFPFSLAE | ||||||
Topological domain | 142-155 | Cytoplasmic | ||||
Sequence: TVLRPHNYPSKKLG | ||||||
Transmembrane | 156-173 | Helical | ||||
Sequence: LSLLGACNFAYIIRILWR | ||||||
Topological domain | 174-190 | Extracellular | ||||
Sequence: YVQTGNWVYPVFASLSP | ||||||
Transmembrane | 191-211 | Helical | ||||
Sequence: LGIILFFSASYILSASLYLFG | ||||||
Topological domain | 212-230 | Cytoplasmic | ||||
Sequence: EKINHWKWGATVKPRMKKN |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000190103 | 1-230 | Androgen-dependent TFPI-regulating protein | |||
Sequence: MTKTTTCLYHFVVLNWYIFLNYYIPQIGKDEEKLKEFHDGGRSKYLTLLNLLLQAVFFGVACLDDVLKRVIGRKDIKFITYFRDLLFTTLAFPLSTFVFLVFWSLFHYDRSLVYPKGLDDFFPAWVNHAMHTSIFPFSLAETVLRPHNYPSKKLGLSLLGACNFAYIIRILWRYVQTGNWVYPVFASLSPLGIILFFSASYILSASLYLFGEKINHWKWGATVKPRMKKN |
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Protein-protein interaction databases
Structure
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q5M828-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length230
- Mass (Da)26,904
- Last updated2005-02-01 v1
- ChecksumE3C36DED2E175021
Q5M828-2
- Name2
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0H2UI01 | A0A0H2UI01_RAT | Adtrp | 219 |
Features
Showing features for alternative sequence.
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY325171 EMBL· GenBank· DDBJ | AAP92572.1 EMBL· GenBank· DDBJ | mRNA | ||
BC088287 EMBL· GenBank· DDBJ | AAH88287.1 EMBL· GenBank· DDBJ | mRNA |