PAR1_PAPHA
ID PAR1_PAPHA Reviewed; 425 AA.
AC P56488;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 1.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=Proteinase-activated receptor 1;
DE Short=PAR-1;
DE AltName: Full=Thrombin receptor;
DE Flags: Precursor;
GN Name=F2R; Synonyms=BTHR12, PAR1;
OS Papio hamadryas (Hamadryas baboon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Papio.
OX NCBI_TaxID=9557;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Shoji M., Hayzer D.J., Hanson S.R.;
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
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. Cleavage at 41-Arg-|-Ser-42 by CTSG results in receptor
CC activation while cleavage at 55-Phe-|-Trp-56 results in inhibition of
CC receptor activation. {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; AF028727; AAB84191.1; -; mRNA.
DR AlphaFoldDB; P56488; -.
DR SMR; P56488; -.
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_0000012744"
FT CHAIN 42..425
FT /note="Proteinase-activated receptor 1"
FT /id="PRO_0000012745"
FT TOPO_DOM 42..102
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 103..128
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 129..137
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..157
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 158..176
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..198
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 199..218
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..239
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 240..268
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 269..288
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 289..311
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 312..334
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 335..350
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 351..374
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 375..425
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 SITE 55..56
FT /note="Cleavage; by CTSG"
FT /evidence="ECO:0000250|UniProtKB:P25116"
FT MOD_RES 418
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25116"
FT CARBOHYD 35
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 250
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 259
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 175..254
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 425 AA; 47253 MW; 118FC5FB39D4DE2C CRC64;
MGPRRLLLVA ACLCLCGPLL SARTRARRPA SKATNATLDP RSFLLRNPND KYEPFWEDEE
KNESGLTEYR LVSINKSSPL QKPLPAFISE DASGYLTSSW LTLFVPSVYT GVFVVSLPVN
IMAIVVFILK MKVKKPAVVY MLHLATADVL FVSVLPFKIS YYLSGSDWQF GSELCRFVTA
AFYCNMYASI LLMTVISIDR FLAVVYPMQS LSWRTLGRAS FTCLAIWALA IAGVVPLLLK
EQTIQVPGLN ITTCHDVLNE TLLEGYYAYY FSAFSAVFFF VPLIISTVCY VSIIRCLSSS
TVANRSKKSR ALFLSAAVFC IFIICFGPTN ILLIAHYSFL SHTSTTEAAY FAYLLCVCVS
SISCCIDPLI YYYASSECQR YVYSILCCKE SSDPSSSNSS GQLMASKMDT CSSNLNNSIY
KKLLT
