位置:首页 > 蛋白库 > PAR1_MOUSE
PAR1_MOUSE
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   03-AUG-2022, entry version 187.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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   GlyGen; P30558; 3 sites.
DR   iPTMnet; P30558; -.
DR   PhosphoSitePlus; P30558; -.
DR   EPD; P30558; -.
DR   MaxQB; P30558; -.
DR   PaxDb; P30558; -.
DR   PeptideAtlas; P30558; -.
DR   PRIDE; P30558; -.
DR   ProteomicsDB; 294011; -.
DR   Antibodypedia; 4409; 650 antibodies from 44 providers.
DR   DNASU; 14062; -.
DR   Ensembl; ENSMUST00000059193; ENSMUSP00000061754; ENSMUSG00000048376.
DR   GeneID; 14062; -.
DR   KEGG; mmu:14062; -.
DR   UCSC; uc007rmn.1; mouse.
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; CCKESPD; -.
DR   OrthoDB; 763273at2759; -.
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 75 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 269 other 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:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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; ISO:MGI.
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: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:0051482; P:positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G protein-coupled signaling pathway; ISS:UniProtKB.
DR   GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:UniProtKB.
DR   GO; GO:0043547; P:positive regulation of GTPase activity; ISO:MGI.
DR   GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISS: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:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; 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:0045893; P:positive regulation of transcription, DNA-templated; 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   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;
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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024