PAR4_MOUSE
ID PAR4_MOUSE Reviewed; 396 AA.
AC O88634; Q8BZ77;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 162.
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 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].
RX PubMed=9722561; DOI=10.1074/jbc.273.36.23290;
RA Kahn M.L., Hammes S.R., Botka C., Coughlin S.R.;
RT "Gene and locus structure and chromosomal localization of the protease-
RT activated receptor gene family.";
RL J. Biol. Chem. 273:23290-23296(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9716134; DOI=10.1038/29325;
RA Kahn M.L., Zheng Y.-W., Huang W., Bigornia V., Zeng D., Moff S.,
RA Farese R.V. Jr., Tam C., Coughlin S.R.;
RT "A dual thrombin receptor system for platelet activation.";
RL Nature 394:690-694(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Bone, Spleen, and Thymus;
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 GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) 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 -!- TISSUE SPECIFICITY: Highly expressed in the spleen. Slight expression
CC in the heart, lung, skeletal muscle and kidney. No detectable
CC expression in brain, liver or testis. Also detected in platelets.
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; AF080215; AAC28861.1; -; mRNA.
DR EMBL; AK036427; BAC29423.1; -; mRNA.
DR EMBL; AK153720; BAE32155.1; -; mRNA.
DR EMBL; AK156729; BAE33823.1; -; mRNA.
DR EMBL; CH466525; EDL10818.1; -; Genomic_DNA.
DR CCDS; CCDS22419.1; -.
DR RefSeq; NP_032001.2; NM_007975.4.
DR PDB; 2PV9; X-ray; 3.50 A; C=51-76.
DR PDBsum; 2PV9; -.
DR AlphaFoldDB; O88634; -.
DR SMR; O88634; -.
DR DIP; DIP-42480N; -.
DR IntAct; O88634; 2.
DR MINT; O88634; -.
DR STRING; 10090.ENSMUSP00000054426; -.
DR GlyGen; O88634; 1 site.
DR iPTMnet; O88634; -.
DR PhosphoSitePlus; O88634; -.
DR MaxQB; O88634; -.
DR PaxDb; O88634; -.
DR PRIDE; O88634; -.
DR ProteomicsDB; 287955; -.
DR Antibodypedia; 14245; 403 antibodies from 33 providers.
DR DNASU; 14065; -.
DR Ensembl; ENSMUST00000058099; ENSMUSP00000054426; ENSMUSG00000050147.
DR GeneID; 14065; -.
DR KEGG; mmu:14065; -.
DR UCSC; uc009mgr.1; mouse.
DR CTD; 9002; -.
DR MGI; MGI:1298207; F2rl3.
DR VEuPathDB; HostDB:ENSMUSG00000050147; -.
DR eggNOG; ENOG502QU4Y; Eukaryota.
DR GeneTree; ENSGT01050000244840; -.
DR HOGENOM; CLU_009579_8_2_1; -.
DR InParanoid; O88634; -.
DR OMA; CPRAIPG; -.
DR OrthoDB; 995441at2759; -.
DR PhylomeDB; O88634; -.
DR TreeFam; TF350010; -.
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; 14065; 4 hits in 76 CRISPR screens.
DR EvolutionaryTrace; O88634; -.
DR PRO; PR:O88634; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; O88634; protein.
DR Bgee; ENSMUSG00000050147; Expressed in left lobe of liver and 67 other tissues.
DR Genevisible; O88634; MM.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
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:MGI.
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:MGI.
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 1: Evidence at protein level;
KW 3D-structure; 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..59
FT /note="Removed for receptor activation"
FT /evidence="ECO:0000250"
FT /id="PRO_0000012764"
FT CHAIN 60..396
FT /note="Proteinase-activated receptor 4"
FT /id="PRO_0000012765"
FT TOPO_DOM 60..94
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 95..115
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 116..120
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..141
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 142..162
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..183
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 184..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..255
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 256..276
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 277..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..331
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 332..355
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 356..396
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 28..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 59..60
FT /note="Cleavage; by thrombin"
FT /evidence="ECO:0000250"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 161..240
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 88
FT /note="P -> S (in Ref. 1; AAC28861)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="M -> T (in Ref. 1; AAC28861)"
FT /evidence="ECO:0000305"
FT CONFLICT 135
FT /note="L -> S (in Ref. 1; AAC28861)"
FT /evidence="ECO:0000305"
FT CONFLICT 141
FT /note="L -> P (in Ref. 1; AAC28861)"
FT /evidence="ECO:0000305"
FT TURN 62..65
FT /evidence="ECO:0007829|PDB:2PV9"
SQ SEQUENCE 396 AA; 42786 MW; DC10502E7AAE1B86 CRC64;
MCWPLLYPLV LGLSISLAEG IQTPSIYDDV ESTRGSHEGP LGPTVELKEP KSSDKPNPRG
YPGKFCANDS DTLELPASSQ ALLLGWVPTR LVPALYGLVV AVGLPANGLA LWVLATRVPR
LPSTILLMNL AVADLLLALV LPPRLAYHLR GQRWPFGEAA CRVATAALYG HMYGSVLLLA
AVSLDRYLAL VHPLRARALR GQRLTTGLCL VAWLSAATLA LPLTLHRQTF RLAGSDRMLC
HDALPLTEQT SHWRPAFICL AVLGCFVPLL AMGLCYGATL RALAANGQRY SHALRLTALV
LFSAVASFTP SNVLLVLHYS NPSPEAWGNL YGAYVPSLAL STLNSCVDPF IYYYVSHEFR
EKVRAMLCRQ PEASSSSQAS REAGSRGTAI CSSTLL
