ID   PTPRQ_RAT               Reviewed;        2302 AA.
AC   O88488;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   24-JAN-2024, entry version 134.
DE   RecName: Full=Phosphatidylinositol phosphatase PTPRQ;
DE            EC=3.1.3.-;
DE   AltName: Full=Protein-tyrosine phosphatase receptor-type expressed by glomerular mesangial cells protein 1;
DE            Short=rPTP-GMC1;
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; Synonyms=Ptpgmc1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RC   STRAIN=Wistar;
RX   PubMed=9727007; DOI=10.1074/jbc.273.37.23929;
RA   Wright M.B., Hugo C., Seifert R., Disteche C.M., Bowen-Pope D.F.;
RT   "Proliferating and migrating mesangial cells responding to injury express a
RT   novel receptor protein-tyrosine phosphatase in experimental mesangial
RT   proliferative glomerulonephritis.";
RL   J. Biol. Chem. 273:23929-23937(1998).
RN   [2]
RP   FUNCTION, ENZYME ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS
RP   OF GLU-2171 AND CYS-2203.
RX   PubMed=12802008; DOI=10.1073/pnas.1336511100;
RA   Oganesian A., Poot M., Daum G., Coats S.A., Wright M.B., Seifert R.A.,
RA   Bowen-Pope D.F.;
RT   "Protein tyrosine phosphatase RQ is a phosphatidylinositol phosphatase that
RT   can regulate cell survival and proliferation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7563-7568(2003).
RN   [3]
RP   ALTERNATIVE SPLICING.
RX   PubMed=12837292; DOI=10.1016/s0014-4827(03)00121-6;
RA   Seifert R.A., Coats S.A., Oganesian A., Wright M.B., Dishmon M.,
RA   Booth C.J., Johnson R.J., Alpers C.E., Bowen-Pope D.F.;
RT   "PTPRQ is a novel phosphatidylinositol phosphatase that can be expressed as
RT   a cytoplasmic protein or as a subcellularly localized receptor-like
RT   protein.";
RL   Exp. Cell Res. 287:374-386(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:12802008}.
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, ECO:0000269|PubMed:12802008};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=125 uM for diC8-PI(3,4,5)P3 {ECO:0000269|PubMed:12802008};
CC         Vmax=18.3 nmol/min/mg enzyme with diC8-PI(3,4,5)P3 as substrate
CC         {ECO:0000269|PubMed:12802008};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}. Note=A small isoform that lacks the N-
CC       terminal part and starts after the transmembrane region localizes in
CC       the cytoplasm.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced.;
CC       Name=1;
CC         IsoId=O88488-1; Sequence=Displayed;
CC   -!- INDUCTION: Up-regulated during the period of mesangial cell migration
CC       and proliferation that follows mesangial cell injury.
CC       {ECO:0000269|PubMed:9727007}.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       Receptor class 2A subfamily. {ECO:0000305}.
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DR   EMBL; AF063249; AAC34801.1; -; mRNA.
DR   PIR; T14328; T14328.
DR   RefSeq; NP_075214.1; NM_022925.1.
DR   AlphaFoldDB; O88488; -.
DR   SMR; O88488; -.
DR   STRING; 10116.ENSRNOP00000069293; -.
DR   GlyCosmos; O88488; 15 sites, No reported glycans.
DR   GlyGen; O88488; 15 sites.
DR   iPTMnet; O88488; -.
DR   PhosphoSitePlus; O88488; -.
DR   PaxDb; 10116-ENSRNOP00000049245; -.
DR   GeneID; 360417; -.
DR   KEGG; rno:360417; -.
DR   UCSC; RGD:620779; rat. [O88488-1]
DR   AGR; RGD:620779; -.
DR   CTD; 374462; -.
DR   RGD; 620779; Ptprq.
DR   eggNOG; KOG3510; Eukaryota.
DR   InParanoid; O88488; -.
DR   OrthoDB; 2873210at2759; -.
DR   PhylomeDB; O88488; -.
DR   SABIO-RK; O88488; -.
DR   PRO; PR:O88488; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR   GO; GO:0032421; C:stereocilium bundle; ISO:RGD.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   GO; GO:0050910; P:detection of mechanical stimulus involved in sensory perception of sound; ISO:RGD.
DR   GO; GO:0002244; P:hematopoietic progenitor cell differentiation; ISO:RGD.
DR   GO; GO:0042472; P:inner ear morphogenesis; ISO:RGD.
DR   GO; GO:0050885; P:neuromuscular process controlling balance; ISO:RGD.
DR   GO; GO:0045598; P:regulation of fat cell differentiation; ISS:UniProtKB.
DR   GO; GO:0060116; P:vestibular receptor cell morphogenesis; ISO:RGD.
DR   CDD; cd00063; FN3; 16.
DR   CDD; cd14616; R-PTPc-Q; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 16.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 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   PANTHER; PTHR46957; CYTOKINE RECEPTOR; 1.
DR   PANTHER; PTHR46957:SF1; PHOSPHATIDYLINOSITOL PHOSPHATASE PTPRQ; 1.
DR   Pfam; PF00041; fn3; 14.
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; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 9.
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   Alternative splicing; Cell membrane; Glycoprotein; Hydrolase; Membrane;
KW   Protein phosphatase; Receptor; Reference proteome; Repeat; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..2302
FT                   /note="Phosphatidylinositol phosphatase PTPRQ"
FT                   /id="PRO_5000054322"
FT   TOPO_DOM        19..1908
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1909..1929
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1930..2302
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          60..155
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          159..254
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          310..398
FT                   /note="Fibronectin type-III 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          401..501
FT                   /note="Fibronectin type-III 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          474..566
FT                   /note="Fibronectin type-III 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          570..665
FT                   /note="Fibronectin type-III 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          670..759
FT                   /note="Fibronectin type-III 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          764..854
FT                   /note="Fibronectin type-III 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          859..948
FT                   /note="Fibronectin type-III 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          953..1053
FT                   /note="Fibronectin type-III 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          1058..1151
FT                   /note="Fibronectin type-III 11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          1156..1243
FT                   /note="Fibronectin type-III 12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          1248..1341
FT                   /note="Fibronectin type-III 13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          1345..1431
FT                   /note="Fibronectin type-III 14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          1435..1539
FT                   /note="Fibronectin type-III 15"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          1544..1642
FT                   /note="Fibronectin type-III 16"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          1647..1748
FT                   /note="Fibronectin type-III 17"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          2006..2262
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   ACT_SITE        2203
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160,
FT                   ECO:0000255|PROSITE-ProRule:PRU10044"
FT   CARBOHYD        54
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        162
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        169
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        318
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        354
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        389
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        733
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        746
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        904
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        998
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1010
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1040
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1251
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1256
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1805
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         2171
FT                   /note="E->D: Enhances the tyrosine-protein phosphatase
FT                   activity but abolishes the phosphatidylinositol phosphatase
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:12802008"
FT   MUTAGEN         2203
FT                   /note="C->S: Abolishes the weak tyrosine-protein
FT                   phosphatase activity."
FT                   /evidence="ECO:0000269|PubMed:12802008"
SQ   SEQUENCE   2302 AA;  256824 MW;  F0FA703022EB25D5 CRC64;
     MMDFHFSFLF LLIGTSESQV DVSSSFDGTG YDITLSSVSA TTYSSPVSRT LATNVTKPGP
     PVFLAGERVG SAGILLSWNT PPNPNGRIIS YVVKYKEVCP WMQTAYTRAR AKPDSLEVLL
     TNLNPGTTYE IKVAAENNAG IGVFSDPFLF QTAESAPGKV VNLTVEALNY SAVNLIWYLP
     RQPNGKITSF KISVKHARSG IVVKDVSLRV EDILSGKLPE CNENSESFLW STTSPSPTLG
     RVTPTVRTTQ SSSTAARSKI SSVWKEPISF VVTHLRPYTT YLFEVSAVTT EAGYIDSTIV
     RTPESVPEGP PQNCIMGNVT GKAFSISWDP PTIVTGKFSY RVELYGPSGR ILDNSTKDLR
     FAFTHLTPFT MYDVYVAAET SAGVGPKSNL SVFTPPDVPG AVFDLQIAEV EATEIRITWR
     KPRQPNGIIS QYRVKVSVLE TGVVLENTLL TGQDESISNP MSPEIMNLVD PMIGFYEGSG
     EMSSDLHSPA SFIYNSHPHN DFPASTRAEE QSSPVVTTRN QYMTDITAEQ LSYVVRRLVP
     FTEHTISVSA FTIMGEGPPT VLTVRTREQV PSSIQIINYK NISSSSILLY WDPPEYPNGK
     ITHYTIYATE LDTNRAFQMT TVDNSFLITG LKKYTRYKMR VAASTHVGES SLSEENDIFV
     RTPEDEPESS PQDVQVTGVS PSELRLKWSP PEKPNGIIIA YEVLYQNADT LFVKNTSTTD
     IIISDLKPYT LYNISIRSYT RLGHGNQSSS LLSVRTSETV PDSAPENITY KNISSGEIEI
     SFLPPRSPNG IIQKYTIYLK RSNSHEARTI NTTSLTQTIG GLKKYTHYVI EVSASTLKGE
     GIRSRPISIL TEEDAPDSPP QNFSVKQLSG VTVMLSWQPP LEPNGIILYY TVYVWDKSSL
     RAINATEASL VLSDLDYNVD YGACVTASTR FGDGNARSSI INFRTPEGEP SDPPNDVHYV
     NLSSSSIILF WTPPVKPNGI IQYYSVYYQN TSGTFVQNFT LLQVTKESDN VTVSARIYRL
     AIFSYYTFWL TASTSVGNGN KSSDIIHVYT DQDIPEGPVG NLTFESISST AIHVSWEPPS
     QPNGLVFYYL SLNLQQSPPR HMIPPLVTYE NSIDFDDLEK YTDYIFKITP STEKGFSETY
     TTQLHIKTEE DVPDTPPIIN TFKNLSSTSI LLSWDPPLKP NGAILGYHLT LQGPHANHTF
     VTSGNHIVLE ELSPFTLYSF FAAARTMKGL GPSSILFFYT DESAPLAPPQ NLTLINYTSD
     FVWLTWSPSP LPGGIVKVYS FKIHEHETDT VFYKNISGLQ TDAKLEGLEP VSTYSVSVSA
     FTKVGNGNQY SNVVEFTTQE SVPEAVRNIE CVARDWQSVS VRWDPPRKTN GIIIHYMITV
     GGNSTKVSPR DPTYTFTKLL PNTSYVFEVR ASTSAGEGNE SRCDISTLPE TVPSAPTNVA
     FSNVQSTSAT LTWTKPDTIF GYFQNYKITT QLRAQKCREW EPEECIEHQK DQYLYEANQT
     EETVHGLKKF RWYRFQVAAS TNVGYSNASE WISTQTLPGP PDGPPENVHV VATSPFGINI
     SWSEPAVITG PTFYLIDVKS VDDDDFNISF LKSNEENKTT EINNLEVFTR YSVVITAFVG
     NVSRAYTDGK SSAEVIITTL ESVPKDPPNN MTFQKIPDEV TKFQLTFLPP SQPNGNIRVY
     QALVYREDDP TAVQIHNFSI IQKTDTSIIA MLEGLKGGHT YNISVYAINS AGAGPKVQMR
     ITMDIKAPAR PKSKPIPIRD ATGKLLVTST TITIRMPICY YNDDHGPIRN VQVLVAETGA
     QQDGNVTKWY DAYFNKARPY FTNEGFPNPP CIEGKTKFSG NEEIYVIGAD NACMIPGNEE
     KICNGPLKPK KQYLFKFRAT NVMGQFTDSE YSDPIKTLGE GLSERTVEII LSVTLCILSI
     ILLGTAIFAF VRIRQKQKEG GTYSPRDAEI IDTKFKLDQL ITVADLELKD ERLTRLLSYR
     KSIKPISKKS FLQHVEELCT NSNLKFQEEF SELPKFLQDL SSTDADLPWN RAKNRFPNIK
     PYNNNRVKLI ADVSLPGSDY INASYVSGYL CPNEFIATQG PLPGTVGDFW RMVWETRTKT
     LVMLTQCFEK GRIRCHQYWP EDNKPVTVFG DIVITKLMED IQIDWTIRDL KIERHGDCMT
     VRQCNFTGWP EHGVPENTTP LIHFVKLVRT SRAHDTTPMV VHCSAGVGRT GVFIALDHLT
     QHINNHDFVD IYGLVAELRS ERMCMVQNLA QYIFLHQCIL DLLSNKGGHQ PVCFVNYSTL
     QKMDSLDAME GDVELEWEET TM
//