PTPRQ_RAT
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 25-MAY-2022, entry version 129.
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. [O88488-1]
DR AlphaFoldDB; O88488; -.
DR SMR; O88488; -.
DR STRING; 10116.ENSRNOP00000049245; -.
DR GlyGen; O88488; 15 sites.
DR iPTMnet; O88488; -.
DR PhosphoSitePlus; O88488; -.
DR PaxDb; O88488; -.
DR PRIDE; O88488; -.
DR GeneID; 360417; -.
DR KEGG; rno:360417; -.
DR UCSC; RGD:620779; rat. [O88488-1]
DR CTD; 374462; -.
DR RGD; 620779; Ptprq.
DR eggNOG; KOG3510; Eukaryota.
DR InParanoid; O88488; -.
DR OrthoDB; 411281at2759; -.
DR PhylomeDB; O88488; -.
DR SABIO-RK; O88488; -.
DR PRO; PR:O88488; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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: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: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; ISO:RGD.
DR CDD; cd00063; FN3; 16.
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 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
