PAR1_XENLA
ID PAR1_XENLA Reviewed; 420 AA.
AC P47749;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Proteinase-activated receptor 1;
DE Short=PAR-1;
DE AltName: Full=Thrombin receptor;
DE Flags: Precursor;
GN Name=f2r;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEOLYTIC CLEAVAGE.
RX PubMed=8145852; DOI=10.1038/368648a0;
RA Gerszten R.E., Chen J., Ishii M., Ishii K., Nanevicz T., Turck C.W.,
RA Vu T.-K.H., Coughlin S.R.;
RT "Specificity of the thrombin receptor for agonist peptide is defined by its
RT extracellular surface.";
RL Nature 368:648-651(1994).
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 -!- PTM: Proteolytic cleavage generates a new N-terminus that functions as
CC a tethered ligand. {ECO:0000269|PubMed:8145852}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; U09632; AAA18498.1; -; mRNA.
DR PIR; I51667; I51667.
DR RefSeq; NP_001079252.1; NM_001085783.1.
DR AlphaFoldDB; P47749; -.
DR SMR; P47749; -.
DR GeneID; 378526; -.
DR KEGG; xla:378526; -.
DR CTD; 378526; -.
DR Xenbase; XB-GENE-985800; f2r.L.
DR OrthoDB; 1436400at2759; -.
DR Proteomes; UP000186698; Chromosome 1L.
DR Bgee; 378526; Expressed in heart and 10 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015057; F:thrombin-activated receptor activity; IEA:InterPro.
DR GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
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 1: Evidence at protein 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..20
FT /evidence="ECO:0000255"
FT PROPEP 21..42
FT /note="Removed for receptor activation"
FT /id="PRO_0000012748"
FT CHAIN 43..420
FT /note="Proteinase-activated receptor 1"
FT /id="PRO_0000012749"
FT TOPO_DOM 43..101
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..127
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 128..136
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..156
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 157..175
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..197
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 198..217
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..238
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 239..267
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 268..287
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 288..310
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 311..333
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 334..345
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 346..369
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 370..420
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 61..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 42..43
FT /note="Cleavage; by thrombin"
FT /evidence="ECO:0000269|PubMed:8145852"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 174..253
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT MUTAGEN 42
FT /note="K->A: Lack of activation by thrombin."
SQ SEQUENCE 420 AA; 47436 MW; D5163F56AFE12372 CRC64;
MMELRVLLLL LLLTLLGAMG SLCLANSDTQ AKGAHSNNMT IKTFRIFDDS ESEFEEIPWD
ELDESGEGSG DQAPVSRSAR KPIRRNITKE AEQYLSSQWL TKFVPSLYTV VFIVGLPLNL
LAIIIFLFKM KVRKPAVVYM LNLAIADVFF VSVLPFKIAY HLSGNDWLFG PGMCRIVTAI
FYCNMYCSVL LIASISVDRF LAVVYPMHSL SWRTMSRAYM ACSFIWLISI ASTIPLLVTE
QTQKIPRLDI TTCHDVLDLK DLKDFYIYYF SSFCLLFFFV PFIITTICYI GIIRSLSSSS
IENSCKKTRA LFLAVVVLCV FIICFGPTNV LFLTHYLQEA NEFLYFAYIL SACVGSVSCC
LDPLIYYYAS SQCQRYLYSL LCCRKVSEPG SSTGQLMSTA MKNDNCSTNA KSSIYKKLLA
