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   24-JAN-2024, entry version 186.
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   GlyCosmos; O08675; 2 sites, No reported glycans.
DR   GlyGen; O08675; 2 sites.
DR   iPTMnet; O08675; -.
DR   PhosphoSitePlus; O08675; -.
DR   MaxQB; O08675; -.
DR   PaxDb; 10090-ENSMUSP00000022182; -.
DR   Antibodypedia; 12465; 209 antibodies from 28 providers.
DR   DNASU; 14064; -.
DR   Ensembl; ENSMUST00000022182.5; ENSMUSP00000022182.5; ENSMUSG00000021675.5.
DR   GeneID; 14064; -.
DR   KEGG; mmu:14064; -.
DR   UCSC; uc007rmq.1; mouse.
DR   AGR; MGI:1298208; -.
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; DWAMYIK; -.
DR   OrthoDB; 4256130at2759; -.
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 79 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 68 other cell types or tissues.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
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:0001648; F:proteinase-activated receptor activity; IGI:MGI.
DR   GO; GO:0048018; F:receptor ligand activity; IDA:MGI.
DR   GO; GO:0015057; F:thrombin-activated receptor activity; IEA:InterPro.
DR   GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:MGI.
DR   GO; GO:1990806; P:ligand-gated ion channel signaling pathway; IDA:MGI.
DR   GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0032024; P:positive regulation of insulin secretion; IDA:MGI.
DR   GO; GO:0035025; P:positive regulation of Rho protein signal transduction; IBA:GO_Central.
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; IPR003943; Prot_act_rcpt_3.
DR   InterPro; IPR003912; Protea_act_rcpt.
DR   PANTHER; PTHR24232; G-PROTEIN COUPLED RECEPTOR; 1.
DR   PANTHER; PTHR24232:SF0; PROTEINASE-ACTIVATED RECEPTOR 3; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR01428; PROTEASEAR.
DR   PRINTS; PR01429; PROTEASEAR3.
DR   SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR   Genevisible; O08675; MM.
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
//