PTPRQ_MOUSE
ID PTPRQ_MOUSE Reviewed; 2300 AA.
AC P0C5E4;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Phosphatidylinositol phosphatase PTPRQ;
DE EC=3.1.3.-;
DE AltName: Full=Receptor-type tyrosine-protein phosphatase Q;
DE Short=PTP-RQ;
DE Short=R-PTP-Q;
DE EC=3.1.3.48;
DE Flags: Precursor;
GN Name=Ptprq;
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 [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 [2]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=14534255; DOI=10.1523/jneurosci.23-27-09208.2003;
RA Goodyear R.J., Legan P.K., Wright M.B., Marcotti W., Oganesian A.,
RA Coats S.A., Booth C.J., Kros C.J., Seifert R.A., Bowen-Pope D.F.,
RA Richardson G.P.;
RT "A receptor-like inositol lipid phosphatase is required for the maturation
RT of developing cochlear hair bundles.";
RL J. Neurosci. 23:9208-9219(2003).
CC -!- FUNCTION: Phosphatidylinositol phosphatase required for auditory
CC function. May act by regulating the level of phosphatidylinositol 4,5-
CC bisphosphate (PIP2) level in the basal region of hair bundles. Can
CC dephosphorylate a broad range of phosphatidylinositol phosphates,
CC including phosphatidylinositol 3,4,5-trisphosphate and most
CC phosphatidylinositol monophosphates and diphosphates. Phosphate can be
CC hydrolyzed from the D3 and D5 positions in the inositol ring. Has low
CC tyrosine-protein phosphatase activity; however, the relevance of such
CC activity in vivo is unclear. Plays an important role in adipogenesis of
CC mesenchymal stem cells (MSCs). Regulates the phosphorylation state of
CC AKT1 by suppressing the phosphatidylinositol 3,4,5-trisphosphate (PIP3)
CC level in MSCs and preadipocyte cells (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:14534255}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10044};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: In the inner ear of the early postnatal mouse, it
CC is present in hair bundles in the cochlea and in the vestibule.
CC Restricted to the hair bundles and not detected in any other cell type
CC within the inner ear. Restricted to the basal region of the hair bundle
CC (at protein level). {ECO:0000269|PubMed:14534255}.
CC -!- DISRUPTION PHENOTYPE: Mice show rapid postnatal deterioration in
CC cochlear hair-bundle structure, associated with smaller than normal
CC transducer currents with otherwise normal adaptation properties, a
CC progressive loss of basal-coil cochlear hair cells, and deafness.
CC {ECO:0000269|PubMed:14534255}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Receptor class 2A subfamily. {ECO:0000305}.
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DR EMBL; AC021642; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC123948; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC155168; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS36051.1; -.
DR RefSeq; NP_001074901.1; NM_001081432.1.
DR AlphaFoldDB; P0C5E4; -.
DR SMR; P0C5E4; -.
DR BioGRID; 231884; 16.
DR STRING; 10090.ENSMUSP00000058572; -.
DR GlyGen; P0C5E4; 16 sites.
DR iPTMnet; P0C5E4; -.
DR PhosphoSitePlus; P0C5E4; -.
DR PaxDb; P0C5E4; -.
DR PeptideAtlas; P0C5E4; -.
DR PRIDE; P0C5E4; -.
DR ProteomicsDB; 301977; -.
DR Antibodypedia; 29801; 15 antibodies from 6 providers.
DR DNASU; 237523; -.
DR Ensembl; ENSMUST00000050702; ENSMUSP00000058572; ENSMUSG00000035916.
DR GeneID; 237523; -.
DR KEGG; mmu:237523; -.
DR UCSC; uc007gzb.1; mouse.
DR CTD; 374462; -.
DR MGI; MGI:1096349; Ptprq.
DR VEuPathDB; HostDB:ENSMUSG00000035916; -.
DR eggNOG; KOG3510; Eukaryota.
DR eggNOG; KOG4228; Eukaryota.
DR GeneTree; ENSGT00940000159215; -.
DR HOGENOM; CLU_000621_0_0_1; -.
DR InParanoid; P0C5E4; -.
DR OMA; MMDFLII; -.
DR OrthoDB; 411281at2759; -.
DR PhylomeDB; P0C5E4; -.
DR TreeFam; TF351926; -.
DR BioGRID-ORCS; 237523; 2 hits in 71 CRISPR screens.
DR PRO; PR:P0C5E4; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; P0C5E4; protein.
DR Bgee; ENSMUSG00000035916; Expressed in spermatocyte and 12 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0032421; C:stereocilium bundle; IDA:MGI.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0050910; P:detection of mechanical stimulus involved in sensory perception of sound; IMP:MGI.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IMP:MGI.
DR GO; GO:0042472; P:inner ear morphogenesis; IMP:MGI.
DR GO; GO:0050885; P:neuromuscular process controlling balance; IMP:MGI.
DR GO; GO:1990264; P:peptidyl-tyrosine dephosphorylation involved in inactivation of protein kinase activity; IBA:GO_Central.
DR GO; GO:0045598; P:regulation of fat cell differentiation; ISS:UniProtKB.
DR GO; GO:0060116; P:vestibular receptor cell morphogenesis; IMP:MGI.
DR CDD; cd00063; FN3; 15.
DR Gene3D; 2.60.40.10; -; 16.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000242; PTP_cat.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR Pfam; PF00041; fn3; 12.
DR Pfam; PF00102; Y_phosphatase; 1.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00060; FN3; 16.
DR SMART; SM00194; PTPc; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF49265; SSF49265; 9.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS50853; FN3; 16.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE 1: Evidence at protein level;
KW Deafness; Glycoprotein; Hydrolase; Membrane; Protein phosphatase; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..2300
FT /note="Phosphatidylinositol phosphatase PTPRQ"
FT /id="PRO_0000302851"
FT TOPO_DOM 18..1906
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1907..1927
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1928..2300
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 59..154
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 158..253
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 309..397
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 400..495
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 497..564
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 568..663
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 668..757
FT /note="Fibronectin type-III 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 762..852
FT /note="Fibronectin type-III 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 857..946
FT /note="Fibronectin type-III 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 951..1051
FT /note="Fibronectin type-III 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1056..1149
FT /note="Fibronectin type-III 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1154..1241
FT /note="Fibronectin type-III 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1246..1339
FT /note="Fibronectin type-III 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1343..1429
FT /note="Fibronectin type-III 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1433..1537
FT /note="Fibronectin type-III 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1542..1640
FT /note="Fibronectin type-III 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1645..1746
FT /note="Fibronectin type-III 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 2004..2260
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT ACT_SITE 2201
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160,
FT ECO:0000255|PROSITE-ProRule:PRU10044"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 317
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 353
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 388
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 718
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 731
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 744
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 996
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1008
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1038
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1059
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1249
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1254
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1803
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 2300 AA; 256785 MW; 1866AE48D19FAB09 CRC64;
MDFLFFFLFS LIGTSESQVD VSGSFDDTVY DITLSSISAT TYSSPVSRTL ATNVSKPGPP
VFLAGERVGS AGILLSWNTP PNPNGRIISY VVKYKEVCPW MQTAYTRVRA KPDSLEVLLT
NLNPGTTYEI KVAAENSAGI GVFSDPFLFQ TAESAPGKVV NLTVEALNYS AVNLIWYLPR
QPNGKITSFK ISVKHARSGI VVKDVSIKVE DLLSGKLPEC NENSDSFLWS TTSPSPTLSR
ATPPLRTTHL SNTLARNKIS SVWKEPISFV VTHLRPYTTY LFEVSAVTTE AGYIDSTIVR
TPESVPEGPP QNCITGNVTG KAFSISWDPP AIVTGKFSYR VELYGPTGRI LDNSTKDLRF
VFTHLTPFTM YDVYVAAETS AGVGPKSNLS VFTPPDVPGA VFDLQIVEVE ATEIRVSWRK
PRQPNGIISQ YRVKVSVLES GVILENTLLT GQDEYINNPM TPEIMNLVDP MIGFYEGSGE
MSSDLHSLAS FIYNSHPHDF PARTRVEDQR SPVVATRNQY MTDIAAEHLS YVIRRLVPFT
EHTISVSAFT VMGEGPPTVL TVRTREQVPS SIQIINYKNI SSSSILLYWD PPEYPNGKIT
HYTIYAMELD TNRAFQMTTV DNSFLITGLK KYTRYKMRVA ASTHVGESSL SEENDLFVRT
PEDEPESSPQ DVKVTDVSPS ELSLTWSPPE KPNGIIIAYE VFYQNADALF VKNTSTTNIT
LSDLKPYTLY NISIQSYTRL GHGNQSSSLL SVRTSETVPD SAPENITYKN ISSEEIEIFF
LPPRSPNGII QKYTIYLKRS NSHEARTIET TSLTLTIGGL KKYTHYVIEV SASTLKGEGV
RSMPISILTE EDAPDSPPQN FSVKQLSGVT VMLSWQPPLE PNGIILYYTV YVWDKVSLKT
INATEVSLEL SDLDYHADYS AYVTASTRFG DGKTRSSVIN FRTPEGEPSD PPKDVHYVNL
SSSSIILFWT PPVKPNGIIQ YYSVYYQNTS STFVQNFTLL EVTQEPGNVT VSARIYKLAV
FSYYTFWLTA STLVGNGNKS SDVIHVYTDQ DIPEGGVGNL TYESLSSTAI NVSWTPPSQP
NGLVFYYVSL NLQQSPPRHR RPPLTTYENS IYFDNLEKYT DYIFKITPST EKGFSETYTA
QLHIKTEEDV PDTPPIINTF KNLSSTSILL SWDPPLKPNG AILSYHLTLQ GTHANRTFVT
SGNHIVLEEL SPFTLYSFLA AARTMKGLGP SSILFFYTDE SAPLAPPQNL TLINYTSDFV
WLTWSPSPLP GGIVKVYSFK IHEHETDTVF YKNISGFQTD AKLAGLEPVS TYSISVSAFT
KVGNGNQFSN VVKFTTQESV PDAVQNIACV ARDWQSVSVM WDPPRKANGI IIHYMITVEG
NSTKVSPRDP MYTFTKLLAN TSYIFEVRAS TSAGEGNESQ CNVSTLPETV PSVPTNTAFS
NVQSTSVTLR WIKPDTILGY FQNYKITTQL RAQKCREWEP EECVEHQEVQ YLYEANQTED
TVRGLKKFQW YRFQVAASTN AGYGNASSWI STQTLPGPPD GPPENVRVVA TSPFGINISW
NEPAIITGPT FYLIDVKSVD NDNFNISFVK SNEENKTTEI NDLEVFTRYS VVITAFVGNV
SGAYTDGKSS AEVIITTLES VPKDPPNNMT FQKIPDEVTK FQLSFLPPSQ PNGNIQVYQA
LVYREDDPTA VQIHNLSIIQ KTDTSVIAML EGLKGGHTYN ISVYAINSAG AGPKVQMRIT
MDIKAPARPK TKPIPIHDAT GKLLVTSTTI TIRMPICYYN DDHGPIRNVQ VLVAEAGAQQ
DGNVTKWYDA YFNKARPYFT NEGFPNPPCI EGKTKFSGNE EIYVIGADNA CMIPGNEEKI
CNGPLKPKKQ YLFKFRATNV MGQFTDSEYS DPIKTLGEGL SERTVEIILS VTLCILSIIL
LGTAIFAFAR IRQKQKEGGT YSPRDAEIID TKFKLDQLIT VADLELKDER LTRLLSYRKS
IKPVSKKSFL QHVEELCTNN NLKFQEEFSE LPKFLQDLSS TDADLPWNRA KNRFPNIKPY
NNNRVKLIAD VSIPGSDYIN ASYVSGYLCP NEFIATQGPL PGTVGDFWRM VWETRAKTLV
MLTQCFEKGR IRCHQYWPED NKPVTVFGDI LITKLMEDIQ IDWTIRDLKI ERHGDCMTVR
QCNFTGWPEH GVPENTTPLI HFVKLVRTSR AHDATPMVVH CSAGVGRTGV FIALDHLTQH
IHDHDFVDIY GLVAELRSER MCMVQNLAQY IFLHQCILDL LSNKGGHQPV CFVNYSTLQK
MDSLDAMEGD VELEWEETTM
