PAR3_BOVIN
ID PAR3_BOVIN Reviewed; 377 AA.
AC Q58D85;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 80.
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 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].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
CC -!- FUNCTION: Receptor for activated thrombin coupled to G proteins that
CC stimulate phosphoinositide hydrolysis. {ECO:0000250}.
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. {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; BT021712; AAX46559.1; -; mRNA.
DR AlphaFoldDB; Q58D85; -.
DR SMR; Q58D85; -.
DR STRING; 9913.ENSBTAP00000001191; -.
DR PaxDb; Q58D85; -.
DR eggNOG; ENOG502QWI1; Eukaryota.
DR InParanoid; Q58D85; -.
DR Proteomes; UP000009136; 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: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 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; 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..19
FT /evidence="ECO:0000255"
FT PROPEP 20..38
FT /note="Removed for receptor activation"
FT /evidence="ECO:0000250"
FT /id="PRO_0000245016"
FT CHAIN 39..377
FT /note="Proteinase-activated receptor 3"
FT /id="PRO_0000245017"
FT TOPO_DOM 39..94
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 95..120
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 121..127
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 128..147
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 148..166
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..188
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 189..205
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..229
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 230..259
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 260..279
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 280..296
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 297..321
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 322..335
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 336..360
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 361..377
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT SITE 38..39
FT /note="Cleavage; by thrombin"
FT /evidence="ECO:0000250"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 165..244
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 377 AA; 43009 MW; ECCA672ED8FE445D CRC64;
MRAAIFAAIG ALLLSPASCQ SGMEYDADNL AKPTLSIKTF RGAPQNSFEE FPLSAIEGWT
GTTKTVKIKC PEELDSNLHV NNATMGYLSS PLSTKLIPAI YILVFAVGMP ANAVTLWMLF
RTRTIRMTIF YTNLAIADFL FCVTLPFRIA YHLNGNNWVF GEVMCRATTV IFYGNMYCSI
LLLACISINR YLAIVHPFTY RGLPKRTYAL LTCGLVWTTV FLYMLPFFIL KQEYYLVQQD
ITTCHDVHNT CESSSPFQLY YFISLAFFGF LIPFLVIIYC YTAIIWTLNA KDRRWLWYIK
ASLLTFVIFT ICFAPSNIIL IIHHANYYYS NTDALYFVYL IALCLGSLNS CLDPFLYFLM
SKITDHSTAY LTMVKLS
