PAR3_RAT
ID PAR3_RAT Reviewed; 368 AA.
AC Q920E1;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 114.
DE RecName: Full=Proteinase-activated receptor 3;
DE Short=PAR-3;
DE AltName: Full=Coagulation factor II receptor-like 2;
DE AltName: Full=Thrombin receptor-like 2;
DE Flags: Precursor;
GN Name=F2rl2; Synonyms=Par3;
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=Spleen;
RA Chien E.K., Marietti S., Mendoza J., Phillippe M.;
RT "Cloning of the rat protease activated receptor isoforms 3 and 4.";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Receptor for activated thrombin coupled to G proteins that
CC stimulate phosphoinositide hydrolysis.
CC -!- SUBUNIT: Interacts with INSC/inscuteable and GPSM2. {ECO:0000250}.
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; AF310076; AAL26789.1; -; mRNA.
DR RefSeq; NP_445765.1; NM_053313.1.
DR AlphaFoldDB; Q920E1; -.
DR SMR; Q920E1; -.
DR IntAct; Q920E1; 1.
DR MINT; Q920E1; -.
DR STRING; 10116.ENSRNOP00000024292; -.
DR GlyGen; Q920E1; 1 site.
DR PhosphoSitePlus; Q920E1; -.
DR PaxDb; Q920E1; -.
DR GeneID; 29636; -.
DR KEGG; rno:29636; -.
DR UCSC; RGD:620871; rat.
DR CTD; 2151; -.
DR RGD; 620871; F2rl2.
DR eggNOG; ENOG502QWI1; Eukaryota.
DR InParanoid; Q920E1; -.
DR OrthoDB; 892946at2759; -.
DR PhylomeDB; Q920E1; -.
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:Q920E1; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; ISO:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
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:0007596; P:blood coagulation; IEA:UniProtKB-KW.
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:0035025; P:positive regulation of Rho protein signal transduction; IBA:GO_Central.
DR GO; GO:0009611; P:response to wounding; IEP:RGD.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR003943; Prot_act_rcpt_3.
DR InterPro; IPR003912; Protea_act_rcpt.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR01428; PROTEASEAR.
DR PRINTS; PR01429; PROTEASEAR3.
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..21
FT /evidence="ECO:0000255"
FT PROPEP 22..37
FT /note="Removed for receptor activation"
FT /evidence="ECO:0000250"
FT /id="PRO_0000012760"
FT CHAIN 38..368
FT /note="Proteinase-activated receptor 3"
FT /id="PRO_0000012761"
FT TOPO_DOM 38..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..123
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 124..144
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 145..166
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..187
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 188..208
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 209..229
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 230..257
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..278
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 279..300
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 301..321
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 322..338
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 339..359
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 360..368
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT SITE 37..38
FT /note="Cleavage; by thrombin"
FT /evidence="ECO:0000250"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 164..243
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 368 AA; 41796 MW; CE0E94EDA3B80EF1 CRC64;
MEMKVLILVG VRLLFLPTTV CQSGMKHVSD NSALTAESFN GNEHSFEEFP LSDIEGWTGA
TTTIKAKCPE ESITTLHVNN ATMGYLRSSL STKVIPAIYI LVFVIGVPAN IVTLWKLSSR
TKSICLVIFH TNLAIADLLF CVTLPFKIAY HLNGNDWVFG EVMCRVTTVA FYGNMYCAIL
ILTCMGINRY LATVHPFTYR KLPKRNFTLL MCGVVWVMVV LYMLPLAILK QEYHLVQPGI
TTCHDVHDTC ESPLPFQFYY FVSLAFFGFL IPFVVSVFCY TTLIHKLNAQ DRKWLRYIKA
VLLILVIFTI CFAPTNIILI IHHANYYYSN TDSLYFMYLI ALCLGSLNSC LDPFLYFIMS
KIVDQLTS
