Q92633 · LPAR1_HUMAN
- ProteinLysophosphatidic acid receptor 1
- GeneLPAR1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids364 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Plays a role in the reorganization of the actin cytoskeleton, cell migration, differentiation and proliferation, and thereby contributes to the responses to tissue damage and infectious agents. Activates downstream signaling cascades via the G(i)/G(o), G12/G13, and G(q) families of heteromeric G proteins. Signaling inhibits adenylyl cyclase activity and decreases cellular cAMP levels (PubMed:26091040).
Signaling triggers an increase of cytoplasmic Ca2+ levels (PubMed:19656035, PubMed:19733258, PubMed:26091040).
Activates RALA; this leads to the activation of phospholipase C (PLC) and the formation of inositol 1,4,5-trisphosphate (PubMed:19306925).
Signaling mediates activation of down-stream MAP kinases (By similarity).
Contributes to the regulation of cell shape. Promotes Rho-dependent reorganization of the actin cytoskeleton in neuronal cells and neurite retraction (PubMed:26091040).
Promotes the activation of Rho and the formation of actin stress fibers (PubMed:26091040).
Promotes formation of lamellipodia at the leading edge of migrating cells via activation of RAC1 (By similarity).
Through its function as LPA receptor, plays a role in chemotaxis and cell migration, including responses to injury and wounding (PubMed:18066075, PubMed:19656035, PubMed:19733258).
Plays a role in triggering inflammation in response to bacterial lipopolysaccharide (LPS) via its interaction with CD14. Promotes cell proliferation in response to LPA (By similarity).
Inhibits the intracellular ciliogenesis pathway in response to LPA and through AKT1 activation (PubMed:31204173).
Required for normal skeleton development. May play a role in osteoblast differentiation. Required for normal brain development. Required for normal proliferation, survival and maturation of newly formed neurons in the adult dentate gyrus. Plays a role in pain perception and in the initiation of neuropathic pain (By similarity).
Features
Showing features for binding site.
GO annotations
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Chemistry
Names & Taxonomy
Protein names
- Recommended nameLysophosphatidic acid receptor 1
- Short namesLPA receptor 1; LPA-1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ92633
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-50 | Extracellular | ||||
Sequence: MAAISTSIPVISQPQFTAMNEPQCFYNESIAFFYNRSGKHLATEWNTVSK | ||||||
Transmembrane | 51-75 | Helical; Name=1 | ||||
Sequence: LVMGLGITVCIFIMLANLLVMVAIY | ||||||
Topological domain | 76-83 | Cytoplasmic | ||||
Sequence: VNRRFHFP | ||||||
Transmembrane | 84-107 | Helical; Name=2 | ||||
Sequence: IYYLMANLAAADFFAGLAYFYLMF | ||||||
Topological domain | 108-121 | Extracellular | ||||
Sequence: NTGPNTRRLTVSTW | ||||||
Transmembrane | 122-144 | Helical; Name=3 | ||||
Sequence: LLRQGLIDTSLTASVANLLAIAI | ||||||
Topological domain | 145-163 | Cytoplasmic | ||||
Sequence: ERHITVFRMQLHTRMSNRR | ||||||
Transmembrane | 164-184 | Helical; Name=4 | ||||
Sequence: VVVVIVVIWTMAIVMGAIPSV | ||||||
Topological domain | 185-204 | Extracellular | ||||
Sequence: GWNCICDIENCSNMAPLYSD | ||||||
Transmembrane | 205-225 | Helical; Name=5 | ||||
Sequence: SYLVFWAIFNLVTFVVMVVLY | ||||||
Topological domain | 226-255 | Cytoplasmic | ||||
Sequence: AHIFGYVRQRTMRMSRHSSGPRRNRDTMMS | ||||||
Transmembrane | 256-280 | Helical; Name=6 | ||||
Sequence: LLKTVVIVLGAFIICWTPGLVLLLL | ||||||
Topological domain | 281-294 | Extracellular | ||||
Sequence: DVCCPQCDVLAYEK | ||||||
Transmembrane | 295-315 | Helical; Name=7 | ||||
Sequence: FFLLLAEFNSAMNPIIYSYRD | ||||||
Topological domain | 316-364 | Cytoplasmic | ||||
Sequence: KEMSATFRQILCCQRSENPTGPTEGSDRSASSLNHTILAGVHSNDHSVV |
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_049414 | 77 | in dbSNP:rs11542862 | |||
Sequence: N → S | ||||||
Mutagenesis | 85 | Impairs localization at the cell membrane. | ||||
Sequence: Y → A | ||||||
Mutagenesis | 87 | Impairs localization at the cell membrane. | ||||
Sequence: L → A | ||||||
Mutagenesis | 325-326 | Impairs localization at the cell membrane. | ||||
Sequence: IL → AA |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 380 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, disulfide bond, glycosylation, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000069417 | 1-364 | UniProt | Lysophosphatidic acid receptor 1 | |||
Sequence: MAAISTSIPVISQPQFTAMNEPQCFYNESIAFFYNRSGKHLATEWNTVSKLVMGLGITVCIFIMLANLLVMVAIYVNRRFHFPIYYLMANLAAADFFAGLAYFYLMFNTGPNTRRLTVSTWLLRQGLIDTSLTASVANLLAIAIERHITVFRMQLHTRMSNRRVVVVIVVIWTMAIVMGAIPSVGWNCICDIENCSNMAPLYSDSYLVFWAIFNLVTFVVMVVLYAHIFGYVRQRTMRMSRHSSGPRRNRDTMMSLLKTVVIVLGAFIICWTPGLVLLLLDVCCPQCDVLAYEKFFLLLAEFNSAMNPIIYSYRDKEMSATFRQILCCQRSENPTGPTEGSDRSASSLNHTILAGVHSNDHSVV | |||||||
Disulfide bond | 24↔190 | UniProt | |||||
Sequence: CFYNESIAFFYNRSGKHLATEWNTVSKLVMGLGITVCIFIMLANLLVMVAIYVNRRFHFPIYYLMANLAAADFFAGLAYFYLMFNTGPNTRRLTVSTWLLRQGLIDTSLTASVANLLAIAIERHITVFRMQLHTRMSNRRVVVVIVVIWTMAIVMGAIPSVGWNCIC | |||||||
Glycosylation | 27 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 35 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 188↔195 | UniProt | |||||
Sequence: CICDIENC | |||||||
Disulfide bond | 284↔287 | UniProt | |||||
Sequence: CPQC | |||||||
Modified residue | 341 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 341 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 344 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 346 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 347 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 351 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 351 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 358 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 362 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Detected in lung fibroblasts from bronchoalveolar fluid from patients with idiopathic pulmonary fibrosis (PubMed:18066075).
Detected in bone marrow-derived mesenchymal stem cells (PubMed:19733258).
Gene expression databases
Organism-specific databases
Interaction
Structure
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q92633-1
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
- Length364
- Mass (Da)41,109
- Last updated2002-12-06 v3
- Checksum4CA6262FD00DFE74
Q92633-2
- Name2
- Differences from canonical
- 1-15: MAAISTSIPVISQPQ → MLLLLIPAHSSVLENE
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
B1AP63 | B1AP63_HUMAN | LPAR1 | 182 |
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_057046 | 1-15 | in isoform 2 | |||
Sequence: MAAISTSIPVISQPQ → MLLLLIPAHSSVLENE | ||||||
Sequence conflict | 340 | in Ref. 1; AAC51139 | ||||
Sequence: G → S |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U80811 EMBL· GenBank· DDBJ | AAC51139.1 EMBL· GenBank· DDBJ | mRNA | ||
Y09479 EMBL· GenBank· DDBJ | CAA70686.1 EMBL· GenBank· DDBJ | mRNA | ||
Y09479 EMBL· GenBank· DDBJ | CAA70687.1 EMBL· GenBank· DDBJ | mRNA | ||
U78192 EMBL· GenBank· DDBJ | AAC00530.1 EMBL· GenBank· DDBJ | mRNA | ||
AY322546 EMBL· GenBank· DDBJ | AAP84359.1 EMBL· GenBank· DDBJ | mRNA | ||
AK296374 EMBL· GenBank· DDBJ | BAG59048.1 EMBL· GenBank· DDBJ | mRNA | ||
AC007157 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL157881 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL442064 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC030615 EMBL· GenBank· DDBJ | AAH30615.1 EMBL· GenBank· DDBJ | mRNA | ||
BC036034 EMBL· GenBank· DDBJ | AAH36034.1 EMBL· GenBank· DDBJ | mRNA |