PAR4_RAT
ID PAR4_RAT Reviewed; 395 AA.
AC Q920E0;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=Proteinase-activated receptor 4;
DE Short=PAR-4;
DE AltName: Full=Coagulation factor II receptor-like 3;
DE AltName: Full=Thrombin receptor-like 3;
DE Flags: Precursor;
GN Name=F2rl3; Synonyms=Par4;
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 STRAIN=Sprague-Dawley; TISSUE=Duodenum;
RA Hoogerwerf W.A., Lee-Hellmich H., Pasricha P.J.;
RT "Proteinase activated receptor 4 from rat duodenal library.";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Myometrium;
RA Chien E.K., Marietti S., Mendoza J., Phillippe M.;
RT "Cloning of the rat protease activated receptor isoforms 3 and 4.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Receptor for activated thrombin or trypsin coupled to G
CC proteins that stimulate phosphoinositide hydrolysis. May play a role in
CC platelets activation.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- PTM: A proteolytic cleavage generates a new N-terminus that functions
CC as a tethered ligand.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AF310216; AAL26790.1; -; mRNA.
DR EMBL; AF269246; AAK58604.2; -; mRNA.
DR RefSeq; NP_446260.1; NM_053808.1.
DR AlphaFoldDB; Q920E0; -.
DR SMR; Q920E0; -.
DR STRING; 10116.ENSRNOP00000065190; -.
DR GlyGen; Q920E0; 1 site.
DR PhosphoSitePlus; Q920E0; -.
DR PaxDb; Q920E0; -.
DR GeneID; 116498; -.
DR KEGG; rno:116498; -.
DR CTD; 9002; -.
DR RGD; 620872; F2rl3.
DR eggNOG; ENOG502QU4Y; Eukaryota.
DR InParanoid; Q920E0; -.
DR OrthoDB; 995441at2759; -.
DR PhylomeDB; Q920E0; -.
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:Q920E0; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0015057; F:thrombin-activated receptor activity; IEA:InterPro.
DR GO; GO:0030168; P:platelet activation; ISO:RGD.
DR GO; GO:0051482; P:positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G protein-coupled signaling pathway; IBA:GO_Central.
DR GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; ISO:RGD.
DR GO; GO:0035025; P:positive regulation of Rho protein signal transduction; IBA:GO_Central.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR003944; Prot_act_rcpt_4.
DR InterPro; IPR003912; Protea_act_rcpt.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR01428; PROTEASEAR.
DR PRINTS; PR01430; PROTEASEAR4.
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; Receptor;
KW Reference proteome; Signal; Transducer; Transmembrane; Transmembrane helix.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT PROPEP 17..58
FT /note="Removed for receptor activation"
FT /evidence="ECO:0000250"
FT /id="PRO_0000012766"
FT CHAIN 59..395
FT /note="Proteinase-activated receptor 4"
FT /id="PRO_0000012767"
FT TOPO_DOM 59..93
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 94..114
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 115..119
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 120..140
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 141..161
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 162..182
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 183..203
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..224
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 225..254
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 255..275
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 276..295
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 296..316
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 317..330
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 331..354
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 355..395
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 46..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 58..59
FT /note="Cleavage; by thrombin"
FT /evidence="ECO:0000250"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 160..239
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 1..9
FT /note="Missing (in Ref. 2; AAK58604)"
FT /evidence="ECO:0000305"
FT CONFLICT 192
FT /note="S -> P (in Ref. 2; AAK58604)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 395 AA; 42943 MW; 43B36D0DA22FAFAC CRC64;
MCWPLLYPLM LGFSISPAEC QTPSIYDDVE STREGQEASL RPTVELNESK SPDKPNPRGF
PGKPCANNSD TLELPASSEA LLLGWVPTRL VPAIYGLVVV VGLPANGLAL WVLATRVPRL
PSTILLMNLA VADLLLALVL PPRLVYHLRG QRWPFGEAAC RVATAALYGH MYGSVLLLAA
VSLDRYLALV HSLRARALRG QRLTTILCLV AWLSAATLVL PLTFHRQTFL LAGSDRMLCH
DALPLAEQTS HWRPAFICLA VLGCFVPLLA MVLCYGATLR ALAANGQRYS HAVRLTALVL
FSAVAAFTPS NVLLVLHYSN PSPEAWGNLY GAYVPSLALS TLNSCVDPFI YYYVSHEFRE
KVRAMLCRQL KASSSSQASR EAGSRGTAIC SSTLL
