PAR1_RAT
ID PAR1_RAT Reviewed; 432 AA.
AC P26824;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 25-MAY-2022, entry version 140.
DE RecName: Full=Proteinase-activated receptor 1;
DE Short=PAR-1;
DE AltName: Full=Thrombin receptor;
DE Flags: Precursor;
GN Name=F2r; Synonyms=Par1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Aortic smooth muscle;
RX PubMed=1324917; DOI=10.1016/s0021-9258(18)41880-7;
RA Zhong C., Hayzer D.J., Corsen M.A., Wick K., Runge M.S.;
RT "Molecular cloning of the rat vascular smooth muscle thrombin receptor.
RT Evidence for in vitro regulation by basic fibroblast growth factor.";
RL J. Biol. Chem. 267:16975-16979(1992).
CC -!- FUNCTION: High affinity receptor for activated thrombin coupled to G
CC proteins that stimulate phosphoinositide hydrolysis.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- DOMAIN: The cleaved signal peptide may not be degraded and may function
CC as an intracellular angiogenesis inhibitor peptide known as parstatin.
CC {ECO:0000250}.
CC -!- PTM: Proteolytic cleavage by thrombin generates a new N-terminus that
CC functions as a tethered ligand. Also proteolytically cleaved by
CC cathepsin CTSG. {ECO:0000250|UniProtKB:P25116}.
CC -!- PTM: Phosphorylated in the C-terminal tail; probably mediating
CC desensitization prior to the uncoupling and internalization of the
CC receptor. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; M81642; AAA42274.1; -; mRNA.
DR PIR; A43448; A43448.
DR AlphaFoldDB; P26824; -.
DR SMR; P26824; -.
DR STRING; 10116.ENSRNOP00000065624; -.
DR ChEMBL; CHEMBL6041; -.
DR GlyGen; P26824; 4 sites.
DR PhosphoSitePlus; P26824; -.
DR PaxDb; P26824; -.
DR UCSC; RGD:2586; rat.
DR RGD; 2586; F2r.
DR eggNOG; ENOG502QTR0; Eukaryota.
DR InParanoid; P26824; -.
DR PhylomeDB; P26824; -.
DR Reactome; R-RNO-140875; Common Pathway of Fibrin Clot Formation.
DR Reactome; R-RNO-375276; Peptide ligand-binding receptors.
DR Reactome; R-RNO-416476; G alpha (q) signalling events.
DR Reactome; R-RNO-456926; Thrombin signalling through proteinase activated receptors (PARs).
DR PRO; PR:P26824; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005901; C:caveola; ISS:UniProtKB.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0005769; C:early endosome; ISO:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005770; C:late endosome; ISO:RGD.
DR GO; GO:0031594; C:neuromuscular junction; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0031094; C:platelet dense tubular network; ISS:UniProtKB.
DR GO; GO:0045211; C:postsynaptic membrane; IDA:RGD.
DR GO; GO:0004930; F:G protein-coupled receptor activity; ISS:UniProtKB.
DR GO; GO:0001965; F:G-protein alpha-subunit binding; ISS:UniProtKB.
DR GO; GO:0031681; F:G-protein beta-subunit binding; ISS:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; ISO:RGD.
DR GO; GO:0015057; F:thrombin-activated receptor activity; ISS:UniProtKB.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; ISS:UniProtKB.
DR GO; GO:0007596; P:blood coagulation; TAS:RGD.
DR GO; GO:0045217; P:cell-cell junction maintenance; ISO:RGD.
DR GO; GO:0002248; P:connective tissue replacement involved in inflammatory response wound healing; ISS:UniProtKB.
DR GO; GO:0007529; P:establishment of synaptic specificity at neuromuscular junction; IDA:RGD.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:RGD.
DR GO; GO:0048873; P:homeostasis of number of cells within a tissue; ISS:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; ISS:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0003105; P:negative regulation of glomerular filtration; IDA:UniProtKB.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:RGD.
DR GO; GO:1900134; P:negative regulation of renin secretion into blood stream; ISS:UniProtKB.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; ISO:RGD.
DR GO; GO:0030168; P:platelet activation; ISS:UniProtKB.
DR GO; GO:0030194; P:positive regulation of blood coagulation; ISS:UniProtKB.
DR GO; GO:0051928; P:positive regulation of calcium ion transport; IMP:RGD.
DR GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:RGD.
DR GO; GO:0032967; P:positive regulation of collagen biosynthetic process; ISS:UniProtKB.
DR GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISS:UniProtKB.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISS:UniProtKB.
DR GO; GO:0051482; P:positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G protein-coupled signaling pathway; IMP:RGD.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISO:RGD.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; ISS:UniProtKB.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; ISS:UniProtKB.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IMP:RGD.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; ISS:UniProtKB.
DR GO; GO:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; ISS:UniProtKB.
DR GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; ISS:UniProtKB.
DR GO; GO:0035025; P:positive regulation of Rho protein signal transduction; ISS:UniProtKB.
DR GO; GO:0045987; P:positive regulation of smooth muscle contraction; IDA:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0045907; P:positive regulation of vasoconstriction; IDA:RGD.
DR GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; IMP:RGD.
DR GO; GO:0030193; P:regulation of blood coagulation; ISO:RGD.
DR GO; GO:0032651; P:regulation of interleukin-1 beta production; ISS:UniProtKB.
DR GO; GO:0051930; P:regulation of sensory perception of pain; IDA:RGD.
DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IMP:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; ISS:UniProtKB.
DR GO; GO:0009611; P:response to wounding; ISS:UniProtKB.
DR GO; GO:0070493; P:thrombin-activated receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0099553; P:trans-synaptic signaling by endocannabinoid, modulating synaptic transmission; ISO:RGD.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR003912; Protea_act_rcpt.
DR InterPro; IPR000935; Thrmbn_rcpt.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR01428; PROTEASEAR.
DR PRINTS; PR00908; THROMBINR.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 2: Evidence at transcript level;
KW Blood coagulation; Cell membrane; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Hemostasis; Membrane;
KW Phosphoprotein; Receptor; Reference proteome; Signal; Transducer;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000250"
FT PROPEP 22..45
FT /note="Removed for receptor activation"
FT /evidence="ECO:0000250"
FT /id="PRO_0000012746"
FT CHAIN 46..432
FT /note="Proteinase-activated receptor 1"
FT /id="PRO_0000012747"
FT TOPO_DOM 46..109
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..135
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 136..144
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..164
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 165..183
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..205
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 206..225
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 226..246
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 247..275
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 276..295
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 296..318
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 319..341
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 342..357
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 358..381
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 382..432
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT SITE 45..46
FT /note="Cleavage; by thrombin and CTSG"
FT /evidence="ECO:0000250|UniProtKB:P25116"
FT MOD_RES 425
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25116"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 266
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 182..261
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 432 AA; 48281 MW; DD032B97ABA4A605 CRC64;
MGPRRLLLVA VGLSLCGPLL SSRVPMRQPE SERMYATPYA TPNPRSFFLR NPSEDTFEQF
PLGDEEEKNE SIPLEGRAVY LNKSRFPPMP PPPFISEDAS GYLTSPWLTL FIPSVYTFVF
IVSLPLNILA IAVFVFRMKV KKPAVVYMLH LAMADVLFVS VLPFKISYYF SGTDWQFGSG
MCRFATAACY CNMYASIMLM TVISIDRFLA VVYPIQSLSW RTLGRANFTC VVIWVMAIMG
VVPLLLKEQT TQVPGLNITT CHDVLNETLL HGFYSYYFSA FSAIFFLVPL IISTVCYTSI
IRCLSSSAVA NRSKKSRALF LSAAVFCIFI VCFGPTNVLL IVHYLLLSDS PGTETAYFAY
LLCVCVTSVA SCIDPLIYYY ASSECQKHLY SILCCRESSD SNSCNSTGQL MPSKMDTCSS
HLNNSIYKKL LA
