PEAR1_MOUSE
ID PEAR1_MOUSE Reviewed; 1034 AA.
AC Q8VIK5; Q3URX7; Q6KAQ6; Q8CGA7; Q8VHF4; Q8VHL7;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Platelet endothelial aggregation receptor 1;
DE Short=mPEAR1;
DE AltName: Full=Jagged and Delta protein;
DE Short=Protein Jedi;
DE AltName: Full=Multiple epidermal growth factor-like domains protein 12;
DE Short=Multiple EGF-like domains protein 12;
DE Flags: Precursor;
GN Name=Pear1; Synonyms=Jedi, Megf12;
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] (ISOFORMS 1 AND 3), FUNCTION, PHOSPHORYLATION,
RP AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=17226770; DOI=10.1002/jcb.21232;
RA Krivtsov A.V., Rozov F.N., Zinovyeva M.V., Hendrikx P.J., Jiang Y.,
RA Visser J.W., Belyavsky A.V.;
RT "Jedi -- a novel transmembrane protein expressed in early hematopoietic
RT cells.";
RL J. Cell. Biochem. 101:767-784(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Fetal liver;
RA Ivanova N.B., Lemischka I.R.;
RT "The global gene expression profiling of the hematopoietic stem cell.";
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC STRAIN=C57BL/6J; TISSUE=Fetal cerebellum, and Fetal eye;
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] (ISOFORM 2).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [LARGE SCALE MRNA] OF 560-1034 (ISOFORM 1).
RC TISSUE=Natural killer cell;
RX PubMed=15449545; DOI=10.1093/dnares/11.2.127;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of FLJ genes: the
RT complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs identified
RT by screening of terminal sequences of cDNA clones randomly sampled from
RT size-fractionated libraries.";
RL DNA Res. 11:127-135(2004).
CC -!- FUNCTION: When overexpressed, reduces the number of both early and late
CC non-adherent myeloid progenitor cells. {ECO:0000269|PubMed:17226770}.
CC -!- SUBUNIT: Interacts with SHC2 upon its aggregation-induced tyrosine
CC phosphorylation. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane
CC protein {ECO:0000250}. Note=Detected on the cell surface in resting
CC platelets. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q8VIK5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8VIK5-2; Sequence=VSP_029261;
CC Name=3; Synonyms=Jedi-736;
CC IsoId=Q8VIK5-3; Sequence=VSP_029262, VSP_029263;
CC Name=4;
CC IsoId=Q8VIK5-4; Sequence=VSP_029260;
CC -!- TISSUE SPECIFICITY: Expressed in thymocytes, bone marrow stromal and
CC osteogenic cells (at protein level). Strongly expressed in kidney and
CC heart. Moderately expressed in lung, spleen, thymus, liver, brain,
CC testis, skin and stomach. Expressed in hematopoietic stem progenitor
CC cells. {ECO:0000269|PubMed:17226770}.
CC -!- PTM: Phosphorylated on tyrosine residues by SRC. Tyrosine
CC phosphorylation is detected upon platelet aggregation stimulated by
CC collagen, TRAP and thrombin and platelet-platelet contacts but not
CC after platelet activation. Tyrosine phosphorylation enhanced its
CC association with SHC1 and SHC2 (By similarity). Phosphorylated in the
CC intracellular domain on tyrosine residues. {ECO:0000250,
CC ECO:0000269|PubMed:17226770}.
CC -!- SIMILARITY: Belongs to the MEGF family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE24560.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF461685; AAL66380.1; -; mRNA.
DR EMBL; AF444274; AAL38571.1; -; mRNA.
DR EMBL; AF440279; AAL33583.1; -; mRNA.
DR EMBL; AK141082; BAE24560.1; ALT_INIT; mRNA.
DR EMBL; AK053551; BAC35426.1; -; mRNA.
DR EMBL; BC042490; AAH42490.1; -; mRNA.
DR EMBL; AK131151; BAD21401.1; -; Transcribed_RNA.
DR CCDS; CCDS38474.1; -. [Q8VIK5-1]
DR RefSeq; NP_001027585.1; NM_001032413.1. [Q8VIK5-1]
DR RefSeq; NP_001027586.1; NM_001032414.1. [Q8VIK5-1]
DR RefSeq; NP_001276529.1; NM_001289600.1.
DR RefSeq; NP_001276530.1; NM_001289601.1.
DR RefSeq; NP_082736.1; NM_028460.2. [Q8VIK5-1]
DR RefSeq; NP_690012.2; NM_152799.2. [Q8VIK5-1]
DR AlphaFoldDB; Q8VIK5; -.
DR SMR; Q8VIK5; -.
DR STRING; 10090.ENSMUSP00000133474; -.
DR GlyGen; Q8VIK5; 3 sites.
DR iPTMnet; Q8VIK5; -.
DR PhosphoSitePlus; Q8VIK5; -.
DR EPD; Q8VIK5; -.
DR MaxQB; Q8VIK5; -.
DR PaxDb; Q8VIK5; -.
DR PeptideAtlas; Q8VIK5; -.
DR PRIDE; Q8VIK5; -.
DR ProteomicsDB; 287666; -. [Q8VIK5-1]
DR ProteomicsDB; 287667; -. [Q8VIK5-2]
DR ProteomicsDB; 287668; -. [Q8VIK5-3]
DR ProteomicsDB; 287669; -. [Q8VIK5-4]
DR Antibodypedia; 49426; 178 antibodies from 29 providers.
DR DNASU; 73182; -.
DR Ensembl; ENSMUST00000029714; ENSMUSP00000029714; ENSMUSG00000028073. [Q8VIK5-1]
DR Ensembl; ENSMUST00000079083; ENSMUSP00000078090; ENSMUSG00000028073. [Q8VIK5-1]
DR Ensembl; ENSMUST00000090981; ENSMUSP00000088503; ENSMUSG00000028073. [Q8VIK5-1]
DR Ensembl; ENSMUST00000172621; ENSMUSP00000133474; ENSMUSG00000028073. [Q8VIK5-1]
DR Ensembl; ENSMUST00000174759; ENSMUSP00000133323; ENSMUSG00000028073. [Q8VIK5-1]
DR GeneID; 73182; -.
DR KEGG; mmu:73182; -.
DR UCSC; uc008psq.1; mouse. [Q8VIK5-1]
DR CTD; 375033; -.
DR MGI; MGI:1920432; Pear1.
DR VEuPathDB; HostDB:ENSMUSG00000028073; -.
DR eggNOG; KOG1218; Eukaryota.
DR GeneTree; ENSGT00940000154225; -.
DR HOGENOM; CLU_008281_1_0_1; -.
DR InParanoid; Q8VIK5; -.
DR OMA; CNNHSSC; -.
DR OrthoDB; 561378at2759; -.
DR PhylomeDB; Q8VIK5; -.
DR TreeFam; TF332598; -.
DR BioGRID-ORCS; 73182; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Pear1; mouse.
DR PRO; PR:Q8VIK5; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q8VIK5; protein.
DR Bgee; ENSMUSG00000028073; Expressed in external carotid artery and 205 other tissues.
DR ExpressionAtlas; Q8VIK5; baseline and differential.
DR Genevisible; Q8VIK5; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0001891; C:phagocytic cup; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0038023; F:signaling receptor activity; IDA:MGI.
DR GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; IMP:MGI.
DR GO; GO:0070527; P:platelet aggregation; IDA:MGI.
DR GO; GO:0043491; P:protein kinase B signaling; IMP:MGI.
DR GO; GO:0043654; P:recognition of apoptotic cell; IDA:MGI.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR011489; EMI_domain.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR002049; LE_dom.
DR Pfam; PF00053; Laminin_EGF; 4.
DR SMART; SM00181; EGF; 15.
DR SMART; SM00180; EGF_Lam; 13.
DR SUPFAM; SSF57184; SSF57184; 1.
DR PROSITE; PS00022; EGF_1; 13.
DR PROSITE; PS01186; EGF_2; 12.
DR PROSITE; PS50026; EGF_3; 9.
DR PROSITE; PS51041; EMI; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disulfide bond; EGF-like domain;
KW Glycoprotein; Membrane; Phosphoprotein; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..1034
FT /note="Platelet endothelial aggregation receptor 1"
FT /id="PRO_0000309738"
FT TOPO_DOM 19..754
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 755..775
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 776..1034
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 23..101
FT /note="EMI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00384"
FT DOMAIN 181..215
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 223..258
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 266..301
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 309..344
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 398..433
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 484..519
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 575..605
FT /note="EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 613..648
FT /note="EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 656..691
FT /note="EGF-like 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 823..883
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 925..1034
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 852..882
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 968..990
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 923
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q5VY43"
FT MOD_RES 951
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VY43"
FT MOD_RES 1026
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VY43"
FT CARBOHYD 150
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 474
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 27..89
FT /evidence="ECO:0000255"
FT DISULFID 53..63
FT /evidence="ECO:0000255"
FT DISULFID 88..99
FT /evidence="ECO:0000255"
FT DISULFID 185..196
FT /evidence="ECO:0000250"
FT DISULFID 189..203
FT /evidence="ECO:0000250"
FT DISULFID 205..214
FT /evidence="ECO:0000250"
FT DISULFID 233..246
FT /evidence="ECO:0000250"
FT DISULFID 248..257
FT /evidence="ECO:0000250"
FT DISULFID 270..282
FT /evidence="ECO:0000250"
FT DISULFID 276..289
FT /evidence="ECO:0000250"
FT DISULFID 291..300
FT /evidence="ECO:0000250"
FT DISULFID 313..325
FT /evidence="ECO:0000250"
FT DISULFID 319..332
FT /evidence="ECO:0000250"
FT DISULFID 334..343
FT /evidence="ECO:0000250"
FT DISULFID 402..414
FT /evidence="ECO:0000250"
FT DISULFID 408..421
FT /evidence="ECO:0000250"
FT DISULFID 423..432
FT /evidence="ECO:0000250"
FT DISULFID 488..500
FT /evidence="ECO:0000250"
FT DISULFID 494..507
FT /evidence="ECO:0000250"
FT DISULFID 509..518
FT /evidence="ECO:0000250"
FT DISULFID 578..586
FT /evidence="ECO:0000250"
FT DISULFID 580..593
FT /evidence="ECO:0000250"
FT DISULFID 595..604
FT /evidence="ECO:0000250"
FT DISULFID 617..629
FT /evidence="ECO:0000250"
FT DISULFID 622..636
FT /evidence="ECO:0000250"
FT DISULFID 638..647
FT /evidence="ECO:0000250"
FT DISULFID 660..672
FT /evidence="ECO:0000250"
FT DISULFID 666..679
FT /evidence="ECO:0000250"
FT DISULFID 681..690
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..136
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_029260"
FT VAR_SEQ 375..404
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029261"
FT VAR_SEQ 737..747
FT /note="SQESFTIMPTS -> ESFAPLTLVFL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17226770"
FT /id="VSP_029262"
FT VAR_SEQ 748..1034
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17226770"
FT /id="VSP_029263"
FT CONFLICT 160
FT /note="T -> A (in Ref. 1; AAL38571/AAL66380 and 4;
FT AAH42490)"
FT /evidence="ECO:0000305"
FT CONFLICT 718
FT /note="E -> K (in Ref. 5; BAD21401)"
FT /evidence="ECO:0000305"
FT CONFLICT 718
FT /note="E -> Q (in Ref. 1; AAL38571/AAL66380)"
FT /evidence="ECO:0000305"
FT CONFLICT 862
FT /note="V -> T (in Ref. 4; AAH42490)"
FT /evidence="ECO:0000305"
FT CONFLICT 876
FT /note="E -> D (in Ref. 4; AAH42490)"
FT /evidence="ECO:0000305"
FT CONFLICT 993
FT /note="P -> S (in Ref. 4; AAH42490)"
FT /evidence="ECO:0000305"
FT CONFLICT 1003
FT /note="H -> Q (in Ref. 1; AAL38571)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1034 AA; 110580 MW; 714E5016848E4E4C CRC64;
MPLCPLLLLA LGLRLTGTLN SNDPNVCTFW ESFTTTTKES HLRPFSLLPA ESCHRPWEDP
HTCAQPTVVY RTVYRQVVKM DSRPRLQCCR GYYESRGACV PLCAQECVHG RCVAPNQCQC
APGWRGGDCS SECAPGMWGP QCDKFCHCGN NSSCDPKSGT CFCPSGLQPP NCLQPCPAGH
YGPACQFDCQ CYGASCDPQD GACFCPPGRA GPSCNVPCSQ GTDGFFCPRT YPCQNGGVPQ
GSQGSCSCPP GWMGVICSLP CPEGFHGPNC TQECRCHNGG LCDRFTGQCH CAPGYIGDRC
QEECPVGRFG QDCAETCDCA PGARCFPANG ACLCEHGFTG DRCTERLCPD GRYGLSCQEP
CTCDPEHSLS CHPMHGECSC QPGWAGLHCN ESCPQDTHGP GCQEHCLCLH GGLCLADSGL
CRCAPGYTGP HCANLCPPDT YGINCSSRCS CENAIACSPI DGTCICKEGW QRGNCSVPCP
LGTWGFNCNA SCQCAHDGVC SPQTGACTCT PGWHGAHCQL PCPKGQFGEG CASVCDCDHS
DGCDPVHGQC RCQAGWMGTR CHLPCPEGFW GANCSNTCTC KNGGTCVSEN GNCVCAPGFR
GPSCQRPCPP GRYGKRCVQC KCNNNHSSCH PSDGTCSCLA GWTGPDCSEA CPPGHWGLKC
SQLCQCHHGG TCHPQDGSCI CTPGWTGPNC LEGCPPRMFG VNCSQLCQCD LGEMCHPETG
ACVCPPGHSG ADCKMGSQES FTIMPTSPVT HNSLGAVIGI AVLGTLVVAL IALFIGYRQW
QKGKEHEHLA VAYSTGRLDG SDYVMPDVSP SYSHYYSNPS YHTLSQCSPN PPPPNKVPGS
QLFVSSQAPE RPSRAHGREN HVTLPADWKH RREPHERGAS HLDRSYSCSY SHRNGPGPFC
HKGPISEEGL GASVMSLSSE NPYATIRDLP SLPGEPRESG YVEMKGPPSV SPPRQSLHLR
DRQQRQLQPQ RDSGTYEQPS PLSHNEESLG STPPLPPGLP PGHYDSPKNS HIPGHYDLPP
VRHPPSPPSR RQDR
