PAR3_MOUSE
ID PAR3_MOUSE Reviewed; 369 AA.
AC O08675; B9EIT2; Q3UXV3;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 178.
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 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 STRAIN=C57BL/6J;
RX PubMed=9087410; DOI=10.1038/386502a0;
RA Ishihara H., Connolly A.J., Zeng D., Kahn M.L., Zheng Y.-W., Timmons C.,
RA Tram T., Coughlin S.R.;
RT "Protease-activated receptor 3 is a second thrombin receptor in humans.";
RL Nature 386:502-506(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Wolffian duct;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [4]
RP INTERACTION WITH INSC AND GPSM2.
RC STRAIN=CD-1; TISSUE=Epidermis;
RX PubMed=16094321; DOI=10.1038/nature03922;
RA Lechler T., Fuchs E.;
RT "Asymmetric cell divisions promote stratification and differentiation of
RT mammalian skin.";
RL Nature 437:275-280(2005).
CC -!- FUNCTION: High affinity receptor for activated thrombin coupled to G
CC proteins that stimulate phosphoinositide hydrolysis. May play a role in
CC platelets activation.
CC -!- SUBUNIT: Interacts with INSC/inscuteable and GPSM2.
CC {ECO:0000269|PubMed:16094321}.
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; U92972; AAC53137.1; -; mRNA.
DR EMBL; AK135212; BAE22460.1; -; mRNA.
DR EMBL; BC140985; AAI40986.1; -; mRNA.
DR CCDS; CCDS26702.1; -.
DR RefSeq; NP_034300.3; NM_010170.4.
DR PDB; 2PUX; X-ray; 2.00 A; C=44-56.
DR PDBsum; 2PUX; -.
DR AlphaFoldDB; O08675; -.
DR SMR; O08675; -.
DR DIP; DIP-41474N; -.
DR IntAct; O08675; 1.
DR MINT; O08675; -.
DR STRING; 10090.ENSMUSP00000022182; -.
DR GlyGen; O08675; 2 sites.
DR iPTMnet; O08675; -.
DR PhosphoSitePlus; O08675; -.
DR MaxQB; O08675; -.
DR PaxDb; O08675; -.
DR PRIDE; O08675; -.
DR Antibodypedia; 12465; 185 antibodies from 28 providers.
DR DNASU; 14064; -.
DR Ensembl; ENSMUST00000022182; ENSMUSP00000022182; ENSMUSG00000021675.
DR GeneID; 14064; -.
DR KEGG; mmu:14064; -.
DR UCSC; uc007rmq.1; mouse.
DR CTD; 2151; -.
DR MGI; MGI:1298208; F2rl2.
DR VEuPathDB; HostDB:ENSMUSG00000021675; -.
DR eggNOG; ENOG502QWI1; Eukaryota.
DR GeneTree; ENSGT01050000244840; -.
DR HOGENOM; CLU_009579_8_2_1; -.
DR InParanoid; O08675; -.
DR OMA; HHINYYY; -.
DR OrthoDB; 892946at2759; -.
DR PhylomeDB; O08675; -.
DR TreeFam; TF330775; -.
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; 14064; 2 hits in 74 CRISPR screens.
DR EvolutionaryTrace; O08675; -.
DR PRO; PR:O08675; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; O08675; protein.
DR Bgee; ENSMUSG00000021675; Expressed in lumbar dorsal root ganglion and 67 other tissues.
DR Genevisible; O08675; MM.
DR GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; 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: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; 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..19
FT /evidence="ECO:0000255"
FT PROPEP 20..37
FT /note="Removed for receptor activation"
FT /evidence="ECO:0000250"
FT /id="PRO_0000012758"
FT CHAIN 38..369
FT /note="Proteinase-activated receptor 3"
FT /id="PRO_0000012759"
FT TOPO_DOM 38..93
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 94..119
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 120..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..369
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT SITE 37..38
FT /note="Cleavage; by thrombin"
FT /evidence="ECO:0000250"
FT CARBOHYD 24
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 165..244
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 110
FT /note="A -> S (in Ref. 1; AAC53137 and 3; AAI40986)"
FT /evidence="ECO:0000305"
FT CONFLICT 164
FT /note="T -> M (in Ref. 1; AAC53137 and 3; AAI40986)"
FT /evidence="ECO:0000305"
FT CONFLICT 210
FT /note="M -> L (in Ref. 1; AAC53137 and 3; AAI40986)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="M -> I (in Ref. 1; AAC53137 and 3; AAI40986)"
FT /evidence="ECO:0000305"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:2PUX"
SQ SEQUENCE 369 AA; 41697 MW; C8E6B0097F0BF90F CRC64;
MKILILVAAG LLFLPVTVCQ SGINVSDNSA KPTLTIKSFN GGPQNTFEEF PLSDIEGWTG
ATTTIKAECP EDSISTLHVN NATIGYLRSS LSTQVIPAIY ILLFVVGVPA NIVTLWKLSL
RTKSISLVIF HTNLAIADLL FCVTLPFKIA YHLNGNNWVF GEVTCRITTV VFYGNMYCAI
LILTCMGINR YLATAHPFTY QKLPKRSFSM LMCGMVWVMV FLYMLPFVIL KQEYHLVHSE
ITTCHDVVDA CESPSSFRFY YFVSLAFFGF LIPFVIIIFC YTTLIHKLKS KDRIWLGYIK
AVLLILVIFT ICFAPTNIIL VIHHANYYYH NTDSLYFMYL IALCLGSLNS CLDPFLYFVM
SKVVDQLNP
