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Phosphatidylinositol phosphatase PTPRQ (EC 3.1.3.-) (Protein-tyrosine phosphatase receptor-type expressed by glomerular mesangial cells protein 1) (rPTP-GMC1) (Receptor-type tyrosine-protein phosphatase Q) (PTP-RQ) (R-PTP-Q) (EC 3.1.3.48)

 PTPRQ_RAT               Reviewed;        2302 AA.
O88488;
11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
23-MAY-2018, entry version 117.
RecName: Full=Phosphatidylinositol phosphatase PTPRQ;
EC=3.1.3.-;
AltName: Full=Protein-tyrosine phosphatase receptor-type expressed by glomerular mesangial cells protein 1;
Short=rPTP-GMC1;
AltName: Full=Receptor-type tyrosine-protein phosphatase Q;
Short=PTP-RQ;
Short=R-PTP-Q;
EC=3.1.3.48;
Flags: Precursor;
Name=Ptprq; Synonyms=Ptpgmc1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
STRAIN=Wistar;
PubMed=9727007; DOI=10.1074/jbc.273.37.23929;
Wright M.B., Hugo C., Seifert R., Disteche C.M., Bowen-Pope D.F.;
"Proliferating and migrating mesangial cells responding to injury
express a novel receptor protein-tyrosine phosphatase in experimental
mesangial proliferative glomerulonephritis.";
J. Biol. Chem. 273:23929-23937(1998).
[2]
FUNCTION, ENZYME ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
MUTAGENESIS OF GLU-2171 AND CYS-2203.
PubMed=12802008; DOI=10.1073/pnas.1336511100;
Oganesian A., Poot M., Daum G., Coats S.A., Wright M.B., Seifert R.A.,
Bowen-Pope D.F.;
"Protein tyrosine phosphatase RQ is a phosphatidylinositol phosphatase
that can regulate cell survival and proliferation.";
Proc. Natl. Acad. Sci. U.S.A. 100:7563-7568(2003).
[3]
ALTERNATIVE SPLICING.
PubMed=12837292; DOI=10.1016/S0014-4827(03)00121-6;
Seifert R.A., Coats S.A., Oganesian A., Wright M.B., Dishmon M.,
Booth C.J., Johnson R.J., Alpers C.E., Bowen-Pope D.F.;
"PTPRQ is a novel phosphatidylinositol phosphatase that can be
expressed as a cytoplasmic protein or as a subcellularly localized
receptor-like protein.";
Exp. Cell Res. 287:374-386(2003).
-!- FUNCTION: Phosphatidylinositol phosphatase required for auditory
function. May act by regulating the level of phosphatidylinositol
4,5-bisphosphate (PIP2) level in the basal region of hair bundles.
Can dephosphorylate a broad range of phosphatidylinositol
phosphates, including phosphatidylinositol 3,4,5-trisphosphate and
most phosphatidylinositol monophosphates and diphosphates.
Phosphate can be hydrolyzed from the D3 and D5 positions in the
inositol ring. Has low tyrosine-protein phosphatase activity;
however, the relevance of such activity in vivo is unclear. Plays
an important role in adipogenesis of mesenchymal stem cells
(MSCs). Regulates the phosphorylation state of AKT1 by suppressing
the phosphatidylinositol 3,4,5-trisphosphate (PIP3) level in MSCs
and preadipocyte cells (By similarity). {ECO:0000250,
ECO:0000269|PubMed:12802008}.
-!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
tyrosine + phosphate. {ECO:0000255|PROSITE-ProRule:PRU10044,
ECO:0000269|PubMed:12802008}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=125 uM for diC8-PI(3,4,5)P3 {ECO:0000269|PubMed:12802008};
Vmax=18.3 nmol/min/mg enzyme with diC8-PI(3,4,5)P3 as substrate
{ECO:0000269|PubMed:12802008};
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass
type I membrane protein {ECO:0000250}. Note=A small isoform that
lacks the N-terminal part and starts after the transmembrane
region localizes in the cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=1;
Comment=A number of isoforms are produced.;
Name=1;
IsoId=O88488-1; Sequence=Displayed;
-!- INDUCTION: Up-regulated during the period of mesangial cell
migration and proliferation that follows mesangial cell injury.
{ECO:0000269|PubMed:9727007}.
-!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
Receptor class 2A subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AF063249; AAC34801.1; -; mRNA.
PIR; T14328; T14328.
RefSeq; NP_075214.1; NM_022925.1. [O88488-1]
UniGene; Rn.30011; -.
ProteinModelPortal; O88488; -.
SMR; O88488; -.
STRING; 10116.ENSRNOP00000049245; -.
iPTMnet; O88488; -.
PhosphoSitePlus; O88488; -.
PaxDb; O88488; -.
PRIDE; O88488; -.
GeneID; 360417; -.
KEGG; rno:360417; -.
UCSC; RGD:620779; rat. [O88488-1]
CTD; 374462; -.
RGD; 620779; Ptprq.
eggNOG; KOG0791; Eukaryota.
eggNOG; COG5599; LUCA.
HOGENOM; HOG000214125; -.
HOVERGEN; HBG108308; -.
InParanoid; O88488; -.
KO; K16910; -.
PhylomeDB; O88488; -.
PRO; PR:O88488; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
GO; GO:0045598; P:regulation of fat cell differentiation; ISS:UniProtKB.
CDD; cd00063; FN3; 16.
Gene3D; 2.60.40.10; -; 14.
Gene3D; 3.90.190.10; -; 1.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
InterPro; IPR000242; PTPase_domain.
InterPro; IPR016130; Tyr_Pase_AS.
InterPro; IPR003595; Tyr_Pase_cat.
InterPro; IPR000387; TYR_PHOSPHATASE_dom.
Pfam; PF00041; fn3; 14.
Pfam; PF00102; Y_phosphatase; 1.
PRINTS; PR00700; PRTYPHPHTASE.
SMART; SM00060; FN3; 16.
SMART; SM00194; PTPc; 1.
SMART; SM00404; PTPc_motif; 1.
SUPFAM; SSF49265; SSF49265; 11.
SUPFAM; SSF52799; SSF52799; 1.
PROSITE; PS50853; FN3; 16.
PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Complete proteome; Glycoprotein;
Hydrolase; Membrane; Protein phosphatase; Receptor;
Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 18 {ECO:0000255}.
CHAIN 19 2302 Phosphatidylinositol phosphatase PTPRQ.
/FTId=PRO_5000054322.
TOPO_DOM 19 1908 Extracellular. {ECO:0000255}.
TRANSMEM 1909 1929 Helical. {ECO:0000255}.
TOPO_DOM 1930 2302 Cytoplasmic. {ECO:0000255}.
DOMAIN 60 155 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 159 254 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 310 398 Fibronectin type-III 3.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 401 501 Fibronectin type-III 4.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 474 566 Fibronectin type-III 5.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 570 665 Fibronectin type-III 6.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 670 759 Fibronectin type-III 7.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 764 854 Fibronectin type-III 8.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 859 948 Fibronectin type-III 9.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 953 1053 Fibronectin type-III 10.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 1058 1151 Fibronectin type-III 11.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 1156 1243 Fibronectin type-III 12.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 1248 1341 Fibronectin type-III 13.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 1345 1431 Fibronectin type-III 14.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 1435 1539 Fibronectin type-III 15.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 1544 1642 Fibronectin type-III 16.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 1647 1748 Fibronectin type-III 17.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 2006 2262 Tyrosine-protein phosphatase.
{ECO:0000255|PROSITE-ProRule:PRU00160}.
ACT_SITE 2203 2203 Phosphocysteine intermediate.
{ECO:0000255|PROSITE-ProRule:PRU00160,
ECO:0000255|PROSITE-ProRule:PRU10044}.
CARBOHYD 54 54 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 162 162 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 169 169 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 318 318 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 354 354 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 389 389 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 733 733 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 746 746 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 904 904 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 998 998 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1010 1010 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1040 1040 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1251 1251 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1256 1256 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1805 1805 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
MUTAGEN 2171 2171 E->D: Enhances the tyrosine-protein
phosphatase activity but abolishes the
phosphatidylinositol phosphatase
activity. {ECO:0000269|PubMed:12802008}.
MUTAGEN 2203 2203 C->S: Abolishes the weak tyrosine-protein
phosphatase activity.
{ECO:0000269|PubMed:12802008}.
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


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