PAR1_CRILO
ID PAR1_CRILO Reviewed; 428 AA.
AC Q00991; Q60461;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 25-MAY-2022, entry version 122.
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 Cricetulus longicaudatus (Long-tailed dwarf hamster) (Chinese hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10030;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lung;
RX PubMed=1652467; DOI=10.1016/0014-5793(91)81017-3;
RA Rasmussen U.B., Vouret-Craviari V., Jallat S., Schlesinger Y., Pages G.,
RA Pavirani A., Lecocq J.-P., Pouyssegur J., Obberghen-Schilling E.;
RT "cDNA cloning and expression of a hamster alpha-thrombin receptor coupled
RT to Ca2+ mobilization.";
RL FEBS Lett. 288:123-128(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 42-428.
RX PubMed=7488069; DOI=10.1006/bbrc.1995.2559;
RA Hartmann T., Grace M.B., Buzard G.S., Ruoss S.J.;
RT "Thrombin receptor polymorphism in Chinese hamster.";
RL Biochem. Biophys. Res. Commun. 215:974-980(1995).
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; X61958; CAA43957.1; -; mRNA.
DR EMBL; U34047; AAA86747.1; -; mRNA.
DR PIR; S17148; S17148.
DR AlphaFoldDB; Q00991; -.
DR SMR; Q00991; -.
DR GO; GO:0005901; C:caveola; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031594; C:neuromuscular junction; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0031094; C:platelet dense tubular network; ISS:UniProtKB.
DR GO; GO:0045211; C:postsynaptic membrane; ISS:UniProtKB.
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: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: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; ISS:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISS:UniProtKB.
DR GO; GO:1900134; P:negative regulation of renin secretion into blood stream; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
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; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0045907; P:positive regulation of vasoconstriction; ISS:UniProtKB.
DR GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0032651; P:regulation of interleukin-1 beta production; ISS:UniProtKB.
DR GO; GO:0051930; P:regulation of sensory perception of pain; ISS:UniProtKB.
DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; ISS:UniProtKB.
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 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; Signal; Transducer; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000250"
FT PROPEP 22..41
FT /note="Removed for receptor activation"
FT /evidence="ECO:0000250"
FT /id="PRO_0000012738"
FT CHAIN 42..428
FT /note="Proteinase-activated receptor 1"
FT /id="PRO_0000012739"
FT TOPO_DOM 42..105
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 106..131
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 132..140
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..160
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 161..179
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 180..201
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 202..221
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..242
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 243..271
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 272..291
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 292..314
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 315..337
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 338..352
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 353..377
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 378..428
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT SITE 41..42
FT /note="Cleavage; by thrombin and CTSG"
FT /evidence="ECO:0000250|UniProtKB:P25116"
FT MOD_RES 421
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25116"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 262
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 178..257
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT VARIANT 84
FT /note="Missing (in an allele)"
FT CONFLICT 384
FT /note="H -> T (in Ref. 1; CAA43957)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 428 AA; 47603 MW; E5492AB2CD877E2F CRC64;
MGPQRLLLVA AGLSLCGPLL SSRVPVRQPE SEMTDATVNP RSFFLRNPGE NTFELIPLGD
EEEKNESTLP EGRAIYLNKS HSPPAPLAPF ISEDASGYLT SPWLRLFIPS VYTFVFVVSL
PLNILAIAVF VLKMKVKKPA VVYMLHLAMA DVLFVSVLPL KISYYFSGSD WQFGSGMCRF
ATAAFYCNMY ASIMLMTVIS IDRFLAVVYP IQSLSWRTLG RANFTCLVIW VMAIMGVVPL
LLKEQTTRVP GLNITTCHDV LNETLLQGFY SYYFSAFSAV FFLVPLIIST ICYMSIIRCL
SSSSVANRSK KSRALFLSAA VFCVFIVCFG PTNVLLIMHY LLLSDSPATE KAYFAYLLCV
CVSSVSCCID PLIYYYASSE CQRHLYGILC CKESSDPNSY NSTGQLMPSK MDTCSSHLNN
SIYKKLLA
