PAR1_BOVIN
ID PAR1_BOVIN Reviewed; 427 AA.
AC A7YY44;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 25-MAY-2022, entry version 78.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Heart ventricle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: High affinity receptor for activated thrombin coupled to G
CC proteins that stimulate phosphoinositide hydrolysis. {ECO:0000250}.
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; BC151272; AAI51273.1; -; mRNA.
DR RefSeq; NP_001096567.1; NM_001103097.2.
DR AlphaFoldDB; A7YY44; -.
DR SMR; A7YY44; -.
DR STRING; 9913.ENSBTAP00000026902; -.
DR PaxDb; A7YY44; -.
DR PRIDE; A7YY44; -.
DR GeneID; 526585; -.
DR KEGG; bta:526585; -.
DR CTD; 2149; -.
DR eggNOG; ENOG502QTR0; Eukaryota.
DR InParanoid; A7YY44; -.
DR OrthoDB; 763273at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005901; C:caveola; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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; Reference proteome; Signal; Transducer;
KW Transmembrane; 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_0000317424"
FT CHAIN 42..427
FT /note="Proteinase-activated receptor 1"
FT /id="PRO_0000317425"
FT TOPO_DOM 42..104
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..130
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 131..139
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..159
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 160..178
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..200
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 201..220
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 221..241
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 242..270
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 271..290
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 291..313
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 314..336
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 337..351
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 352..376
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 377..427
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 23..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 41..42
FT /note="Cleavage; by thrombin and CTSG"
FT /evidence="ECO:0000250|UniProtKB:P25116"
FT MOD_RES 420
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25116"
FT CARBOHYD 35
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 252
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 177..256
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 427 AA; 46818 MW; D824334A8C0C73FD CRC64;
MGPRWLLLWA AGLGLCSPLV SARTRGPRPG TDPTNGTLGP RSFFLRNSND GYEQIPLPED
EDSSEGEFTE DRLSSGNRSS PPQKSPPGFI SKSASGYLTS AWLTVFIPSV YTGVFLVSLP
LNIMAVVVFV LKMKVKKPAV VYMLHLAAAD VLFVCVLPFK ISYYFSGSDW RFGSAMCRFV
TAAFYGNMYA SIMLMTAISV DRFLAVVYPI QSLSWRTLGR ASFICLAIWA MAIAGVAPLL
LQEQATQVPG LNITACHDVL NQTLLEGYYS YYFSAFSAVF FFVPLTLSTV SYVSIIRCLS
SSTVANQNKK SRALLLSAAV FCIFILCFGP TNILLLLHYA FLSSDPMTEA AYFAYLLCVC
VSSISCCIDP LIYYYASSEC QRHLFAILHC KESSDPGSCN SSGQLMPSKM DTCSSNLSSS
LYKKLLT
