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PTAFR_MOUSE
ID   PTAFR_MOUSE             Reviewed;         341 AA.
AC   Q62035; B1B170; Q8C017;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 168.
DE   RecName: Full=Platelet-activating factor receptor;
DE            Short=PAF-R;
DE            Short=PAFr;
GN   Name=Ptafr;
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 [GENOMIC DNA], TISSUE SPECIFICITY, AND INDUCTION.
RC   STRAIN=129/Sv;
RX   PubMed=8670084; DOI=10.1042/bj3140671;
RA   Ishii S., Matsuda Y., Nakamura M., Waga I., Kume K., Izumi T., Noma M.,
RA   Shimizu T.;
RT   "A murine platelet-activating factor receptor gene: cloning, chromosomal
RT   localization and up-regulation of expression by lipopolysaccharide in
RT   peritoneal resident macrophages.";
RL   Biochem. J. 314:671-678(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Olfactory bulb;
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 GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Receptor for platelet activating factor, a chemotactic
CC       phospholipid mediator that possesses potent inflammatory, smooth-muscle
CC       contractile and hypotensive activity. Seems to mediate its action via a
CC       G protein that activates a phosphatidylinositol-calcium second
CC       messenger system.
CC   -!- SUBUNIT: Interacts with ARRB1. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Found in a range of organs. Expressed most strongly
CC       in spleen, followed by skeletal muscle, lung and small intestine.
CC       Expressed at moderate levels in the heart. Expressed at relatively low
CC       levels in the brain, liver and kidney. {ECO:0000269|PubMed:8670084}.
CC   -!- INDUCTION: By lipopolysaccharide (LPS). {ECO:0000269|PubMed:8670084}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; D50872; BAA09468.1; -; Genomic_DNA.
DR   EMBL; AK032547; BAC27919.1; -; mRNA.
DR   EMBL; CR931794; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS38899.1; -.
DR   PIR; S63666; S63666.
DR   RefSeq; NP_001074680.1; NM_001081211.2.
DR   AlphaFoldDB; Q62035; -.
DR   SMR; Q62035; -.
DR   STRING; 10090.ENSMUSP00000070925; -.
DR   BindingDB; Q62035; -.
DR   ChEMBL; CHEMBL3993; -.
DR   GuidetoPHARMACOLOGY; 334; -.
DR   GlyGen; Q62035; 2 sites.
DR   iPTMnet; Q62035; -.
DR   PhosphoSitePlus; Q62035; -.
DR   MaxQB; Q62035; -.
DR   PaxDb; Q62035; -.
DR   PRIDE; Q62035; -.
DR   ProteomicsDB; 301893; -.
DR   Antibodypedia; 30903; 192 antibodies from 26 providers.
DR   DNASU; 19204; -.
DR   Ensembl; ENSMUST00000070690; ENSMUSP00000070925; ENSMUSG00000056529.
DR   GeneID; 19204; -.
DR   KEGG; mmu:19204; -.
DR   UCSC; uc008vbn.1; mouse.
DR   CTD; 5724; -.
DR   MGI; MGI:106066; Ptafr.
DR   VEuPathDB; HostDB:ENSMUSG00000056529; -.
DR   eggNOG; ENOG502QTQI; Eukaryota.
DR   GeneTree; ENSGT01050000244845; -.
DR   HOGENOM; CLU_009579_8_2_1; -.
DR   InParanoid; Q62035; -.
DR   OMA; AIHVIIC; -.
DR   OrthoDB; 800525at2759; -.
DR   PhylomeDB; Q62035; -.
DR   TreeFam; TF350009; -.
DR   Reactome; R-MMU-373076; Class A/1 (Rhodopsin-like receptors).
DR   Reactome; R-MMU-416476; G alpha (q) signalling events.
DR   Reactome; R-MMU-6798695; Neutrophil degranulation.
DR   BioGRID-ORCS; 19204; 4 hits in 73 CRISPR screens.
DR   ChiTaRS; Ptafr; mouse.
DR   PRO; PR:Q62035; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; Q62035; protein.
DR   Bgee; ENSMUSG00000056529; Expressed in granulocyte and 49 other tissues.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0045028; F:G protein-coupled purinergic nucleotide receptor activity; IBA:GO_Central.
DR   GO; GO:0001530; F:lipopolysaccharide binding; IMP:MGI.
DR   GO; GO:0001875; F:lipopolysaccharide immune receptor activity; IMP:MGI.
DR   GO; GO:0051019; F:mitogen-activated protein kinase binding; ISO:MGI.
DR   GO; GO:0005543; F:phospholipid binding; ISO:MGI.
DR   GO; GO:0004992; F:platelet activating factor receptor activity; ISO:MGI.
DR   GO; GO:1904317; P:cellular response to 2-O-acetyl-1-O-hexadecyl-sn-glycero-3-phosphocholine; IEA:Ensembl.
DR   GO; GO:0071320; P:cellular response to cAMP; IEA:Ensembl.
DR   GO; GO:0071398; P:cellular response to fatty acid; IEA:Ensembl.
DR   GO; GO:0071258; P:cellular response to gravity; IEA:Ensembl.
DR   GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:MGI.
DR   GO; GO:0006954; P:inflammatory response; IMP:MGI.
DR   GO; GO:0032959; P:inositol trisphosphate biosynthetic process; IMP:MGI.
DR   GO; GO:0045776; P:negative regulation of blood pressure; ISO:MGI.
DR   GO; GO:0007567; P:parturition; ISO:MGI.
DR   GO; GO:0048015; P:phosphatidylinositol-mediated signaling; ISO:MGI.
DR   GO; GO:0002693; P:positive regulation of cellular extravasation; ISO:MGI.
DR   GO; GO:1904306; P:positive regulation of gastro-intestinal system smooth muscle contraction; ISO:MGI.
DR   GO; GO:0060732; P:positive regulation of inositol phosphate biosynthetic process; ISO:MGI.
DR   GO; GO:0032755; P:positive regulation of interleukin-6 production; ISO:MGI.
DR   GO; GO:1903039; P:positive regulation of leukocyte cell-cell adhesion; ISO:MGI.
DR   GO; GO:1903238; P:positive regulation of leukocyte tethering or rolling; ISO:MGI.
DR   GO; GO:1904303; P:positive regulation of maternal process involved in parturition; ISO:MGI.
DR   GO; GO:0043315; P:positive regulation of neutrophil degranulation; ISO:MGI.
DR   GO; GO:0010863; P:positive regulation of phospholipase C activity; ISO:MGI.
DR   GO; GO:1904058; P:positive regulation of sensory perception of pain; ISO:MGI.
DR   GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISO:MGI.
DR   GO; GO:0045987; P:positive regulation of smooth muscle contraction; ISO:MGI.
DR   GO; GO:1904300; P:positive regulation of transcytosis; ISO:MGI.
DR   GO; GO:0045727; P:positive regulation of translation; ISO:MGI.
DR   GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISO:MGI.
DR   GO; GO:1902943; P:positive regulation of voltage-gated chloride channel activity; ISO:MGI.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
DR   GO; GO:0071548; P:response to dexamethasone; IEA:Ensembl.
DR   GO; GO:0032496; P:response to lipopolysaccharide; IMP:MGI.
DR   GO; GO:0009609; P:response to symbiotic bacterium; IEA:Ensembl.
DR   GO; GO:0045056; P:transcytosis; ISO:MGI.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   InterPro; IPR002282; PAF_rcpt.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR01153; PAFRECEPTOR.
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   Cell membrane; Chemotaxis; Disulfide bond; G-protein coupled receptor;
KW   Glycoprotein; Membrane; Receptor; Reference proteome; Transducer;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..341
FT                   /note="Platelet-activating factor receptor"
FT                   /id="PRO_0000070094"
FT   TOPO_DOM        1..16
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        17..38
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        39..54
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        55..74
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        75..91
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        92..113
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        114..133
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        134..155
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        156..184
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        185..205
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        206..233
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        234..254
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        255..275
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        276..295
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        296..341
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        4
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        169
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        90..173
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   CONFLICT        181..182
FT                   /note="SV -> RG (in Ref. 2; BAC27919)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   341 AA;  39148 MW;  CAA8CDDBD8D26897 CRC64;
     MEHNGSFRVD SEFRYTLFPI VYSVIFILGV VANGYVLWVF ANLYPSKKLN EIKIFMVNLT
     MADLLFLITL PLWIVYYYNE GDWILPNFLC NVAGCLFFIN TYCSVAFLGV ITYNRYQAVA
     YPIKTAQATT RKRGISLSLI IWVSIVATAS YFLATDSTNL VPNKDGSGNI TRCFEHYEPY
     SVPILVVHVF IAFCFFLVFF LIFYCNLVII HTLLTQPMRQ QRKAGVKRRA LWMVCTVLAV
     FIICFVPHHV VQLPWTLAEL GYQTNFHQAI NDAHQITLCL LSTNCVLDPV IYCFLTKKFR
     KHLSEKFYSM RSSRKCSRAT SDTCTEVIVP ANQTPIVSLK N
 
 
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