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Protein

Lysophosphatidic acid receptor 1

Gene

Lpar1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Receptor for lysophosphatidic acid (LPA) (PubMed:11087877, PubMed:18066075). 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), G(12)/G(13), and G(q) families of heteromeric G proteins (PubMed:8922387, PubMed:9600933, PubMed:11040035, PubMed:18157949, PubMed:18066075, PubMed:23478264). Signaling inhibits adenylyl cyclase activity and decreases cellular cAMP levels (PubMed:11040035, PubMed:12215548). Signaling triggers an increase of cytoplasmic Ca2+ levels (PubMed:12215548). Activates RALA; this leads to the activation of phospholipase C (PLC) and the formation of inositol 1,4,5-trisphosphate (PubMed:11040035, PubMed:12215548, PubMed:23478264). Signaling mediates activation of down-stream MAP kinases (PubMed:11040035). Contributes to the regulation of cell shape (PubMed:8922387, PubMed:9600933, PubMed:11040035, PubMed:11087877). Promotes Rho-dependent reorganization of the actin cytoskeleton in neuronal cells and neurite retraction (PubMed:9600933, PubMed:11040035, PubMed:12181339). Promotes the activation of Rho and the formation of actin stress fibers (PubMed:9600933, PubMed:12215548). Promotes formation of lamellipodia at the leading edge of migrating cells via activation of RAC1 (PubMed:23478264). Through its function as lysophosphatidic acid receptor, plays a role in chemotaxis and cell migration, including responses to injury and wounding (PubMed:11087877, PubMed:18066075, PubMed:23478264). Plays a role in triggering inflammation in response to bacterial lipopolysaccharide (LPS) via its interaction with CD14 (PubMed:21821728). Promotes cell proliferation in response to lysophosphatidic acid (PubMed:9600933, PubMed:11087877, PubMed:12215548, PubMed:18157949, PubMed:17692995, PubMed:23478264). Required for normal skeleton development (PubMed:21569876). May play a role in osteoblast differentiation (PubMed:21569876). Required for normal brain development (PubMed:17656621, PubMed:18708146). Required for normal proliferation, survival and maturation of newly formed neurons in the adult dentate gyrus (PubMed:18708146). Plays a role in pain perception and in the initiation of neuropathic pain (PubMed:15195086, PubMed:19689455).15 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei39 – 391Lysophosphatidic acidBy similarity
Binding sitei210 – 2101Lysophosphatidic acidBy similarity

GO - Molecular functioni

  • lysophosphatidic acid binding Source: MGI
  • lysophosphatidic acid receptor activity Source: UniProtKB
  • PDZ domain binding Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Receptor, Transducer

Enzyme and pathway databases

ReactomeiR-MMU-416476. G alpha (q) signalling events.
R-MMU-418594. G alpha (i) signalling events.
R-MMU-419408. Lysosphingolipid and LPA receptors.

Names & Taxonomyi

Protein namesi
Recommended name:
Lysophosphatidic acid receptor 1Curated
Short name:
LPA receptor 1Curated
Short name:
LPA-12 Publications
Alternative name(s):
Lysophosphatidic acid receptor Edg-21 Publication
Rec1.31 Publication
VZG-12 Publications
Gene namesi
Name:Lpar1
Synonyms:Edg2, Gpcr261 Publication, Lpa12 Publications, Vzg12 Publications
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:108429. Lpar1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 5050ExtracellularBy similarityAdd
BLAST
Transmembranei51 – 7525Helical; Name=1By similarityAdd
BLAST
Topological domaini76 – 838CytoplasmicBy similarity
Transmembranei84 – 10724Helical; Name=2By similarityAdd
BLAST
Topological domaini108 – 12114ExtracellularBy similarityAdd
BLAST
Transmembranei122 – 14423Helical; Name=3By similarityAdd
BLAST
Topological domaini145 – 16319CytoplasmicBy similarityAdd
BLAST
Transmembranei164 – 18421Helical; Name=4By similarityAdd
BLAST
Topological domaini185 – 20420ExtracellularBy similarityAdd
BLAST
Transmembranei205 – 22521Helical; Name=5By similarityAdd
BLAST
Topological domaini226 – 25530CytoplasmicBy similarityAdd
BLAST
Transmembranei256 – 28025Helical; Name=6By similarityAdd
BLAST
Topological domaini281 – 29414ExtracellularBy similarityAdd
BLAST
Transmembranei295 – 31521Helical; Name=7By similarityAdd
BLAST
Topological domaini316 – 36449CytoplasmicBy similarityAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endosome, Membrane

Pathology & Biotechi

Disruption phenotypei

Mutant embryos are detected at the expected Mendelian rate, but there is about 50% perinatal lethality. This is mostly due to suckling defects, possibly because the neonates cannot find a nipple. Surviving mice are smaller, and they have shorter snouts and more widely spaced eyes than wild-type. A small percentage of the embryos and neonates display frontal hematomas. Besides, a small percentage of the embryos display exencephaly (PubMed:11087877). These mice display also deformity of the rib cage with sterno-distal rib fusions, shorter, crooked sternebrae, delayed vertebral calcification and closure of the thoracic spine (PubMed:21569876). Their small size is due to growth defects of limbs and vertebrae (PubMed:21569876). Mutant mice display decreased bone mass, as well as defects in proliferation and osteoblastic differentiation of bone marrow mesenchymal stem cells (PubMed:21569876). A spontaneous variant (the Malaga variant) that appeared among the descendants of the original knockout mice shows almost complete perinatal viability, but the mice still present small size, shorter snouts, wider-spaced eyes and reduced brain volume (PubMed:17656621). Compared to wild-type, the Malaga variants display smaller olfactory bulbs, and generally a smaller brain with slightly decreased thickness of the brain cortex and subtle defects in cortex development (PubMed:17656621). The hippocampus appears normal at birth, but displays a reduced number of cell divisions in adult dentate gyrus, both under normal conditions and when mice are exposed to a stimulating environment that promotes neurogenesis (PubMed:18708146). Compared to wild-type, the newly formed hippocampus cells show reduced survival (PubMed:18708146). Newly formed granule cells display defects in their maturation (PubMed:18708146). Mutant mice present subtle myelination defects in the brain cortex (PubMed:25226845). Mutant mice display minor defects in somesthesis, olfaction, grasping and keeping their equilibrium, and show decreased sensitivity to pain caused by heat (PubMed:19689455). Mutant mice do not display allodynia and hyperalgesia after nerve injury and are protected against demyelination after nerve injury (PubMed:15195086). Mutant mice display increased Schwann cell apoptosis in sciatic nerve, but this still leaves the majority of Schwann cells intact and does not cause any visible effect on movement (PubMed:11087877). Mutant mice display decreased exploration in the open field and increased anxiety-like responses to novelty; they also show subtle deficits in spatial learning and memory (PubMed:19689455). Mutant mice show blunted responses to bacterial lipopolysaccharide (LPS) and show reduced acute inflammation in response to LPS (PubMed:21821728). Mutant mice show decreased migration of fibroblasts to sites of lung injury, decreased injury-induced vascular leak, and are protected against the development of lung fibrosis after bleomycin treatment (PubMed:18066075). Mutant mice have reduced levels of proliferating epithelial cells in their intestinal crypts, and the cells do not migrate normally from the bottom of the crypts up into the villi (PubMed:23478264). Mutant mice show impaired repair after wounding of the intestinal mucosa (PubMed:23478264).Mutant mice have less body weight, but increased brown and white adipose tissue (PubMed:20358347). Contrary to wild-type, mutant mice do not increase their food consumption on a high fat diet and do not gain weight on a high fat diet (PubMed:20358347). Mice deficient in both Lpar1 and Lpar2 have the same phenotype as mice lacking Lpar1, excepting a higher incidence of frontal hematomas and slightly higher perinatal lethality (PubMed:12215548).11 Publications

Chemistry

GuidetoPHARMACOLOGYi272.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 364364Lysophosphatidic acid receptor 1PRO_0000069418Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi24 ↔ 190By similarity
Glycosylationi27 – 271N-linked (GlcNAc...)Sequence analysis
Glycosylationi35 – 351N-linked (GlcNAc...)Sequence analysis
Disulfide bondi188 ↔ 195By similarity
Disulfide bondi284 ↔ 287By similarity
Modified residuei341 – 3411PhosphoserineBy similarity
Modified residuei351 – 3511PhosphothreonineCombined sources

Post-translational modificationi

N-glycosylated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP61793.
PaxDbiP61793.
PRIDEiP61793.

PTM databases

iPTMnetiP61793.
PhosphoSiteiP61793.

Expressioni

Tissue specificityi

Detected in lung (PubMed:21821728). Detected in oligodendrocytes in corpus callosum in brain cortex (at protein level) (PubMed:25226845). Expressed within the embryonic cerebral cortex, where it is enriched in the ventricular zone (PubMed:8922387). In the adult brain, also expressed in oligodendrocytes, as well as Schwann cells of the peripheral nervous system (PubMed:9013780, PubMed:25226845). Expressed in many other tissues, including lung, heart, intestine, spleen, thymus, and stomach. No expression in liver (PubMed:9013780). Detected in kidney and testis (PubMed:9013780, PubMed:12215548). Detected in embryonic fibroblasts (PubMed:12215548). Detected in adult lung fibroblasts and lung endothelial cells (PubMed:18066075). Detected in dorsal root ganglion and dorsal root (PubMed:15195086). Detected in astrocytes (PubMed:17692995). Detected in bone (PubMed:21569876).7 Publications

Inductioni

Up-regulated by bacterial lipopolysaccharide (LPS) (at protein level). Up-regulated by bacterial lipopolysaccharide (LPS).1 Publication

Gene expression databases

BgeeiP61793.
ExpressionAtlasiP61793. baseline and differential.
GenevisibleiP61793. MM.

Interactioni

Subunit structurei

Interacts with RALA and ADRBK1 (By similarity). Interacts with GNAQ and GNA13 (PubMed:23478264). Interacts with CD14; the interaction is enhanced by exposure to bacterial lipopolysaccharide (LPS) (PubMed:21821728).By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ARHGEF12Q9NZN53EBI-7512335,EBI-821440From a different organism.

GO - Molecular functioni

  • PDZ domain binding Source: MGI

Protein-protein interaction databases

DIPiDIP-42214N.
IntActiP61793. 2 interactions.
MINTiMINT-1897166.
STRINGi10090.ENSMUSP00000052581.

Structurei

3D structure databases

ProteinModelPortaliP61793.
SMRiP61793. Positions 23-232, 248-326.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni124 – 1296Lysophosphatidic acid bindingBy similarity

Sequence similaritiesi

Belongs to the G-protein coupled receptor 1 family.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3656. Eukaryota.
ENOG410XRW9. LUCA.
GeneTreeiENSGT00760000118804.
HOGENOMiHOG000233501.
HOVERGENiHBG103071.
InParanoidiP61793.
KOiK04289.
OMAiCQRSENT.
OrthoDBiEOG7HTHH1.
PhylomeDBiP61793.
TreeFamiTF330052.

Family and domain databases

InterProiIPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR004065. LPA_rcpt.
IPR002277. LPA_rcpt_EDG2.
[Graphical view]
PfamiPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSiPR01148. EDG2RECEPTOR.
PR00237. GPCRRHODOPSN.
PR01527. LPARECEPTOR.
SMARTiSM01381. 7TM_GPCR_Srsx. 1 hit.
[Graphical view]
PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P61793-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MAAASTSSPV ISQPQFTAMN EQQCFYNESI AFFYNRSGKY LATEWNTVSK
60 70 80 90 100
LVMGLGITVC VFIMLANLLV MVAIYVNRRF HFPIYYLMAN LAAADFFAGL
110 120 130 140 150
AYFYLMFNTG PNTRRLTVST WLLRQGLIDT SLTASVANLL AIAIERHITV
160 170 180 190 200
FRMQLHTRMS NRRVVVVIVV IWTMAIVMGA IPSVGWNCIC DIDHCSNMAP
210 220 230 240 250
LYSDSYLVFW AIFNLVTFVV MVVLYAHIFG YVRQRTMRMS RHSSGPRRNR
260 270 280 290 300
DTMMSLLKTV VIVLGAFIVC WTPGLVLLLL DVCCPQCDVL AYEKFFLLLA
310 320 330 340 350
EFNSAMNPII YSYRDKEMSA TFRQILCCQR NENPNGPTEG SDRSASSLNH
360
TILAGVHSND HSVV
Length:364
Mass (Da):41,119
Last modified:June 7, 2004 - v1
Checksum:iB0FA6265AA6688B7
GO
Isoform 2 (identifier: P61793-2) [UniParc] [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-18: Missing.

Show »
Length:346
Mass (Da):39,343
Checksum:i7634E3976257933D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti119 – 1191S → N in AAC34301 (PubMed:9721207).Curated
Sequence conflicti119 – 1191S → N in AAC34302 (PubMed:9721207).Curated
Sequence conflicti181 – 1833IPS → MPT in AAC34301 (PubMed:9721207).Curated
Sequence conflicti181 – 1833IPS → MPT in AAC34302 (PubMed:9721207).Curated
Sequence conflicti225 – 2251Y → S in AAC53035 (PubMed:9013780).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1818Missing in isoform 2. 1 PublicationVSP_001986Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U70622 mRNA. Translation: AAC52923.1.
U48235 mRNA. Translation: AAC53035.1.
AF075456, AF075453, AF075455 Genomic DNA. Translation: AAC34301.1.
AF075456, AF075455 Genomic DNA. Translation: AAC34302.1.
AL807748 Genomic DNA. Translation: CAM16236.1.
BC025425 mRNA. Translation: AAH25425.1.
CCDSiCCDS18212.1.
CCDS71391.1. [P61793-2]
RefSeqiNP_001277415.1. NM_001290486.1. [P61793-2]
NP_034466.2. NM_010336.2. [P61793-1]
NP_766577.1. NM_172989.1. [P61793-1]
XP_011248230.1. XM_011249928.1. [P61793-1]
XP_011248231.1. XM_011249929.1. [P61793-1]
XP_011248232.1. XM_011249930.1. [P61793-1]
XP_011248233.1. XM_011249931.1. [P61793-1]
XP_011248234.1. XM_011249932.1. [P61793-1]
XP_011248235.1. XM_011249933.1. [P61793-1]
XP_011248236.1. XM_011249934.1. [P61793-1]
XP_011248237.1. XM_011249935.1. [P61793-1]
UniGeneiMm.4772.

Genome annotation databases

EnsembliENSMUST00000055018; ENSMUSP00000052581; ENSMUSG00000038668. [P61793-1]
ENSMUST00000107570; ENSMUSP00000103196; ENSMUSG00000038668. [P61793-2]
ENSMUST00000107571; ENSMUSP00000103197; ENSMUSG00000038668. [P61793-1]
ENSMUST00000107574; ENSMUSP00000103200; ENSMUSG00000038668. [P61793-1]
ENSMUST00000107575; ENSMUSP00000103201; ENSMUSG00000038668. [P61793-1]
GeneIDi14745.
KEGGimmu:14745.
UCSCiuc008szb.3. mouse.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U70622 mRNA. Translation: AAC52923.1.
U48235 mRNA. Translation: AAC53035.1.
AF075456, AF075453, AF075455 Genomic DNA. Translation: AAC34301.1.
AF075456, AF075455 Genomic DNA. Translation: AAC34302.1.
AL807748 Genomic DNA. Translation: CAM16236.1.
BC025425 mRNA. Translation: AAH25425.1.
CCDSiCCDS18212.1.
CCDS71391.1. [P61793-2]
RefSeqiNP_001277415.1. NM_001290486.1. [P61793-2]
NP_034466.2. NM_010336.2. [P61793-1]
NP_766577.1. NM_172989.1. [P61793-1]
XP_011248230.1. XM_011249928.1. [P61793-1]
XP_011248231.1. XM_011249929.1. [P61793-1]
XP_011248232.1. XM_011249930.1. [P61793-1]
XP_011248233.1. XM_011249931.1. [P61793-1]
XP_011248234.1. XM_011249932.1. [P61793-1]
XP_011248235.1. XM_011249933.1. [P61793-1]
XP_011248236.1. XM_011249934.1. [P61793-1]
XP_011248237.1. XM_011249935.1. [P61793-1]
UniGeneiMm.4772.

3D structure databases

ProteinModelPortaliP61793.
SMRiP61793. Positions 23-232, 248-326.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-42214N.
IntActiP61793. 2 interactions.
MINTiMINT-1897166.
STRINGi10090.ENSMUSP00000052581.

Chemistry

GuidetoPHARMACOLOGYi272.

Protein family/group databases

GPCRDBiSearch...

PTM databases

iPTMnetiP61793.
PhosphoSiteiP61793.

Proteomic databases

MaxQBiP61793.
PaxDbiP61793.
PRIDEiP61793.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000055018; ENSMUSP00000052581; ENSMUSG00000038668. [P61793-1]
ENSMUST00000107570; ENSMUSP00000103196; ENSMUSG00000038668. [P61793-2]
ENSMUST00000107571; ENSMUSP00000103197; ENSMUSG00000038668. [P61793-1]
ENSMUST00000107574; ENSMUSP00000103200; ENSMUSG00000038668. [P61793-1]
ENSMUST00000107575; ENSMUSP00000103201; ENSMUSG00000038668. [P61793-1]
GeneIDi14745.
KEGGimmu:14745.
UCSCiuc008szb.3. mouse.

Organism-specific databases

CTDi1902.
MGIiMGI:108429. Lpar1.

Phylogenomic databases

eggNOGiKOG3656. Eukaryota.
ENOG410XRW9. LUCA.
GeneTreeiENSGT00760000118804.
HOGENOMiHOG000233501.
HOVERGENiHBG103071.
InParanoidiP61793.
KOiK04289.
OMAiCQRSENT.
OrthoDBiEOG7HTHH1.
PhylomeDBiP61793.
TreeFamiTF330052.

Enzyme and pathway databases

ReactomeiR-MMU-416476. G alpha (q) signalling events.
R-MMU-418594. G alpha (i) signalling events.
R-MMU-419408. Lysosphingolipid and LPA receptors.

Miscellaneous databases

PROiP61793.
SOURCEiSearch...

Gene expression databases

BgeeiP61793.
ExpressionAtlasiP61793. baseline and differential.
GenevisibleiP61793. MM.

Family and domain databases

InterProiIPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR004065. LPA_rcpt.
IPR002277. LPA_rcpt_EDG2.
[Graphical view]
PfamiPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSiPR01148. EDG2RECEPTOR.
PR00237. GPCRRHODOPSN.
PR01527. LPARECEPTOR.
SMARTiSM01381. 7TM_GPCR_Srsx. 1 hit.
[Graphical view]
PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Ventricular zone gene-1 (vzg-1) encodes a lysophosphatidic acid receptor expressed in neurogenic regions of the developing cerebral cortex."
    Hecht J.H., Weiner J.A., Post S.R., Chun J.
    J. Cell Biol. 135:1071-1083(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Strain: BALB/cJ.
  2. "Cloning, characterization, and chromosomal localization of rec1.3, a member of the G-protein-coupled receptor family highly expressed in brain."
    Macrae A.D., Premont R.T., Jaber M., Petersen A.S., Lefkowitz R.J.
    Brain Res. Mol. Brain Res. 42:245-254(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY.
    Strain: C57BL/6J.
    Tissue: Brain.
  3. "Complete cDNA sequence, genomic structure, and chromosomal localization of the LPA receptor gene, lpA1/vzg-1/Gpcr26."
    Contos J.J.A., Chun J.
    Genomics 51:364-378(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2).
    Strain: 129/SvJ.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: FVB/N-3.
  6. "A single receptor encoded by vzg-1/lpA1/edg-2 couples to G proteins and mediates multiple cellular responses to lysophosphatidic acid."
    Fukushima N., Kimura Y., Chun J.
    Proc. Natl. Acad. Sci. U.S.A. 95:6151-6156(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  7. "Functional comparisons of the lysophosphatidic acid receptors, LP(A1)/VZG-1/EDG-2, LP(A2)/EDG-4, and LP(A3)/EDG-7 in neuronal cell lines using a retrovirus expression system."
    Ishii I., Contos J.J., Fukushima N., Chun J.
    Mol. Pharmacol. 58:895-902(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Lysophosphatidic acid receptors."
    Contos J.J.A., Ishii I., Chun J.
    Mol. Pharmacol. 58:1188-1196(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  9. "Requirement for the lpA1 lysophosphatidic acid receptor gene in normal suckling behavior."
    Contos J.J., Fukushima N., Weiner J.A., Kaushal D., Chun J.
    Proc. Natl. Acad. Sci. U.S.A. 97:13384-13389(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION.
  10. "Dual regulation of actin rearrangement through lysophosphatidic acid receptor in neuroblast cell lines: actin depolymerization by Ca(2+)-alpha-actinin and polymerization by rho."
    Fukushima N., Ishii I., Habara Y., Allen C.B., Chun J.
    Mol. Biol. Cell 13:2692-2705(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Characterization of lpa(2) (Edg4) and lpa(1)/lpa(2) (Edg2/Edg4) lysophosphatidic acid receptor knockout mice: signaling deficits without obvious phenotypic abnormality attributable to lpa(2)."
    Contos J.J., Ishii I., Fukushima N., Kingsbury M.A., Ye X., Kawamura S., Brown J.H., Chun J.
    Mol. Cell. Biol. 22:6921-6929(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION, TISSUE SPECIFICITY.
  12. "Initiation of neuropathic pain requires lysophosphatidic acid receptor signaling."
    Inoue M., Rashid M.H., Fujita R., Contos J.J., Chun J., Ueda H.
    Nat. Med. 10:712-718(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION, TISSUE SPECIFICITY.
  13. "A lysophosphatidic acid receptor lacking the PDZ-binding domain is constitutively active and stimulates cell proliferation."
    Shano S., Hatanaka K., Ninose S., Moriyama R., Tsujiuchi T., Fukushima N.
    Biochim. Biophys. Acta 1783:748-759(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  14. Cited for: DISRUPTION PHENOTYPE, FUNCTION.
  15. "Lysophosphatidic acid stimulates astrocyte proliferation through LPA1."
    Shano S., Moriyama R., Chun J., Fukushima N.
    Neurochem. Int. 52:216-220(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  16. Cited for: DISRUPTION PHENOTYPE, FUNCTION.
  17. "The lysophosphatidic acid receptor LPA1 links pulmonary fibrosis to lung injury by mediating fibroblast recruitment and vascular leak."
    Tager A.M., LaCamera P., Shea B.S., Campanella G.S., Selman M., Zhao Z., Polosukhin V., Wain J., Karimi-Shah B.A., Kim N.D., Hart W.K., Pardo A., Blackwell T.S., Xu Y., Chun J., Luster A.D.
    Nat. Med. 14:45-54(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.
  18. Cited for: DISRUPTION PHENOTYPE, FUNCTION.
  19. "Altered food consumption in mice lacking lysophosphatidic acid receptor-1."
    Dusaulcy R., Daviaud D., Pradere J.P., Gres S., Valet P., Saulnier-Blache J.S.
    J. Physiol. Biochem. 65:345-350(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  20. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-351, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  21. "Lysophosphatidic acid receptor 1 modulates lipopolysaccharide-induced inflammation in alveolar epithelial cells and murine lungs."
    Zhao J., He D., Su Y., Berdyshev E., Chun J., Natarajan V., Zhao Y.
    Am. J. Physiol. 301:L547-L556(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION, INTERACTION WITH CD14, SUBCELLULAR LOCATION, INDUCTION BY BACTERIAL LIPOPOLYSACCHARIDE, TISSUE SPECIFICITY.
  22. "Absence of the lysophosphatidic acid receptor LPA1 results in abnormal bone development and decreased bone mass."
    Gennero I., Laurencin-Dalicieux S., Conte-Auriol F., Briand-Mesange F., Laurencin D., Rue J., Beton N., Malet N., Mus M., Tokumura A., Bourin P., Vico L., Brunel G., Oreffo R.O., Chun J., Salles J.P.
    Bone 49:395-403(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION, TISSUE SPECIFICITY.
  23. "Distinct phospholipase C-beta isozymes mediate lysophosphatidic acid receptor 1 effects on intestinal epithelial homeostasis and wound closure."
    Lee S.J., Leoni G., Neumann P.A., Chun J., Nusrat A., Yun C.C.
    Mol. Cell. Biol. 33:2016-2028(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION, INTERACTION WITH GNAQ AND GNA13.
  24. Cited for: DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.
  25. "Comparative analyses of lysophosphatidic acid receptor-mediated signaling."
    Fukushima N., Ishii S., Tsujiuchi T., Kagawa N., Katoh K.
    Cell. Mol. Life Sci. 72:2377-2394(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.

Entry informationi

Entry nameiLPAR1_MOUSE
AccessioniPrimary (citable) accession number: P61793
Secondary accession number(s): A2AMJ2
, O88584, P56487, P70420, Q61130
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 7, 2004
Last modified: June 8, 2016
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.