ID PAR1_MOUSE Reviewed; 430 AA.
AC P30558; P97507; Q3TVP3;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 24-JAN-2024, entry version 195.
DE RecName: Full=Proteinase-activated receptor 1;
DE Short=PAR-1;
DE AltName: Full=Thrombin receptor;
DE Flags: Precursor;
GN Name=F2r; Synonyms=Cf2r, Par1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA Coughlin S.R.;
RT "Cloning of cDNA for the mouse thrombin receptor.";
RL Submitted (OCT-1992) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129;
RX PubMed=8784787; DOI=10.1007/bf03401632;
RA Kahn M.L., Ishii K., Kuo W.L., Piper M., Connolly A.J., Shi Y.P., Wu R.,
RA Lin C.C., Coughlin S.R.;
RT "Conserved structure and adjacent location of the thrombin receptor and
RT protease-activated receptor 2 genes define a protease-activated receptor
RT gene cluster.";
RL Mol. Med. 2:349-357(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Heart;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-74.
RC STRAIN=129/Sv;
RX PubMed=8678993; DOI=10.1007/s003359900189;
RA Xue J., Jenkins N.A., Gilbert D.J., Copeland N.G., Sadler J.E.;
RT "Structure and localization of the thrombin receptor gene on mouse
RT chromosome 13.";
RL Mamm. Genome 7:625-626(1996).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-67.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
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 -!- 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; L03529; AAA40438.1; -; mRNA.
DR EMBL; U36757; AAB38308.1; -; Genomic_DNA.
DR EMBL; U36756; AAB38308.1; JOINED; Genomic_DNA.
DR EMBL; AK085990; BAC39587.1; -; mRNA.
DR EMBL; AK159282; BAE34960.1; -; mRNA.
DR EMBL; AK160032; BAE35575.1; -; mRNA.
DR EMBL; BC031516; AAH31516.1; -; mRNA.
DR EMBL; AH003565; AAB00198.1; -; Genomic_DNA.
DR CCDS; CCDS26701.1; -.
DR RefSeq; NP_034299.2; NM_010169.3.
DR AlphaFoldDB; P30558; -.
DR SMR; P30558; -.
DR IntAct; P30558; 1.
DR STRING; 10090.ENSMUSP00000061754; -.
DR ChEMBL; CHEMBL4523212; -.
DR GlyCosmos; P30558; 3 sites, No reported glycans.
DR GlyGen; P30558; 3 sites.
DR iPTMnet; P30558; -.
DR PhosphoSitePlus; P30558; -.
DR EPD; P30558; -.
DR MaxQB; P30558; -.
DR PaxDb; 10090-ENSMUSP00000061754; -.
DR PeptideAtlas; P30558; -.
DR ProteomicsDB; 294011; -.
DR Antibodypedia; 4409; 723 antibodies from 44 providers.
DR DNASU; 14062; -.
DR Ensembl; ENSMUST00000059193.7; ENSMUSP00000061754.6; ENSMUSG00000048376.7.
DR GeneID; 14062; -.
DR KEGG; mmu:14062; -.
DR UCSC; uc007rmn.1; mouse.
DR AGR; MGI:101802; -.
DR CTD; 2149; -.
DR MGI; MGI:101802; F2r.
DR VEuPathDB; HostDB:ENSMUSG00000048376; -.
DR eggNOG; ENOG502QTR0; Eukaryota.
DR GeneTree; ENSGT01050000244840; -.
DR HOGENOM; CLU_009579_8_2_1; -.
DR InParanoid; P30558; -.
DR OMA; FIMCFGP; -.
DR OrthoDB; 5361746at2759; -.
DR PhylomeDB; P30558; -.
DR TreeFam; TF330775; -.
DR Reactome; R-MMU-140875; Common Pathway of Fibrin Clot Formation.
DR Reactome; R-MMU-375276; Peptide ligand-binding receptors.
DR Reactome; R-MMU-416476; G alpha (q) signalling events.
DR Reactome; R-MMU-456926; Thrombin signalling through proteinase activated receptors (PARs).
DR BioGRID-ORCS; 14062; 1 hit in 80 CRISPR screens.
DR ChiTaRS; F2r; mouse.
DR PRO; PR:P30558; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; P30558; Protein.
DR Bgee; ENSMUSG00000048376; Expressed in molar tooth and 271 other cell types or tissues.
DR Genevisible; P30558; MM.
DR GO; GO:0005901; C:caveola; ISS:UniProtKB.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005769; C:early endosome; ISO:MGI.
DR GO; GO:0005770; C:late endosome; ISO:MGI.
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; IMP:UniProtKB.
DR GO; GO:0001965; F:G-protein alpha-subunit binding; IDA:UniProtKB.
DR GO; GO:0031681; F:G-protein beta-subunit binding; IDA:UniProtKB.
DR GO; GO:0032795; F:heterotrimeric G-protein binding; TAS:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
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:0045217; P:cell-cell junction maintenance; ISO:MGI.
DR GO; GO:0002248; P:connective tissue replacement involved in inflammatory response wound healing; ISS:UniProtKB.
DR GO; GO:0036145; P:dendritic cell homeostasis; IMP:MGI.
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; ISO:MGI.
DR GO; GO:0048873; P:homeostasis of number of cells within a tissue; IMP:MGI.
DR GO; GO:0006954; P:inflammatory response; IMP:MGI.
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; IDA:UniProtKB.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0030168; P:platelet activation; ISS:UniProtKB.
DR GO; GO:0030194; P:positive regulation of blood coagulation; IMP:MGI.
DR GO; GO:0051928; P:positive regulation of calcium ion transport; ISS:UniProtKB.
DR GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; ISS:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; IDA: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; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISS:UniProtKB.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA: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:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IDA: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; IDA:UniProtKB.
DR GO; GO:0045987; P:positive regulation of smooth muscle contraction; ISS:UniProtKB.
DR GO; GO:0045907; P:positive regulation of vasoconstriction; IDA:UniProtKB.
DR GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0030193; P:regulation of blood coagulation; ISO:MGI.
DR GO; GO:0032651; P:regulation of interleukin-1 beta production; IMP:MGI.
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; IMP:MGI.
DR GO; GO:0009611; P:response to wounding; ISS:UniProtKB.
DR GO; GO:0070493; P:thrombin-activated receptor signaling pathway; IGI:MGI.
DR GO; GO:0099553; P:trans-synaptic signaling by endocannabinoid, modulating synaptic transmission; IMP:ParkinsonsUK-UCL.
DR CDD; cd15369; 7tmA_PAR1; 1.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR003912; Protea_act_rcpt.
DR InterPro; IPR000935; Thrmbn_rcpt.
DR PANTHER; PTHR24232; G-PROTEIN COUPLED RECEPTOR; 1.
DR PANTHER; PTHR24232:SF20; PROTEINASE-ACTIVATED RECEPTOR 1; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR01428; PROTEASEAR.
DR PRINTS; PR00908; THROMBINR.
DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
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;
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_0000012742"
FT CHAIN 42..430
FT /note="Proteinase-activated receptor 1"
FT /id="PRO_0000012743"
FT TOPO_DOM 42..107
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 108..133
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 134..142
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..162
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 163..181
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 182..203
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 204..223
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 224..244
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 245..273
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..293
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 294..316
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 317..339
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 340..354
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 355..379
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 380..430
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT SITE 41..42
FT /note="Cleavage; by thrombin and CTSG"
FT /evidence="ECO:0000250|UniProtKB:P25116"
FT MOD_RES 423
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25116"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 255
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 180..259
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 162
FT /note="F -> S (in Ref. 1; AAA40438)"
FT /evidence="ECO:0000305"
FT CONFLICT 189
FT /note="G -> Y (in Ref. 1; AAA40438)"
FT /evidence="ECO:0000305"
FT CONFLICT 223
FT /note="R -> G (in Ref. 1; AAA40438)"
FT /evidence="ECO:0000305"
FT CONFLICT 262
FT /note="V -> L (in Ref. 1; AAA40438)"
FT /evidence="ECO:0000305"
FT CONFLICT 365
FT /note="S -> T (in Ref. 1; AAA40438)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 430 AA; 47790 MW; 395FD64FAE52C9BF CRC64;
MGPRRLLIVA LGLSLCGPLL SSRVPMSQPE SERTDATVNP RSFFLRNPSE NTFELVPLGD
EEEEEKNESV LLEGRAVYLN ISLPPHTPPP PFISEDASGY LTSPWLTLFM PSVYTIVFIV
SLPLNVLAIA VFVLRMKVKK PAVVYMLHLA MADVLFVSVL PFKISYYFSG TDWQFGSGMC
RFATAAFYGN MYASIMLMTV ISIDRFLAVV YPIQSLSWRT LGRANFTCVV IWVMAIMGVV
PLLLKEQTTR VPGLNITTCH DVLSENLMQG FYSYYFSAFS AIFFLVPLIV STVCYTSIIR
CLSSSAVANR SKKSRALFLS AAVFCIFIVC FGPTNVLLIV HYLFLSDSPG TEAAYFAYLL
CVCVSSVSCC IDPLIYYYAS SECQRHLYSI LCCKESSDPN SCNSTGQLMP SKMDTCSSHL
NNSIYKKLLA
//
