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O88488 (PTPRQ_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphatidylinositol phosphatase PTPRQ
EC=3.1.3.-
Alternative name(s):
Protein-tyrosine phosphatase receptor-type expressed by glomerular mesangial cells protein 1
Short name=rPTP-GMC1
Receptor-type tyrosine-protein phosphatase Q
Short name=PTP-RQ
Short name=R-PTP-Q
EC=3.1.3.48
Gene names
Name:Ptprq
Synonyms:Ptpgmc1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length2302 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.2

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate. Ref.2

Subcellular location

Cell membrane; Single-pass type I membrane protein By similarity. Note: A small isoform that lacks the N-terminal part and starts after the transmembrane region localizes in the cytoplasm.

Induction

Up-regulated during the period of mesangial cell migration and proliferation that follows mesangial cell injury. Ref.1

Sequence similarities

Belongs to the protein-tyrosine phosphatase family. Receptor class 2A subfamily.

Contains 17 fibronectin type-III domains.

Contains 1 tyrosine-protein phosphatase domain.

Biophysicochemical properties

Kinetic parameters:

KM=125 µM for diC8-PI(3,4,5)P3 Ref.2

Vmax=18.3 nmol/min/mg enzyme with diC8-PI(3,4,5)P3 as substrate

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced.
Isoform 1 (identifier: O88488-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 23022284Phosphatidylinositol phosphatase PTPRQ
PRO_5000054322

Regions

Topological domain19 – 19081890Extracellular Potential
Transmembrane1909 – 192921Helical; Potential
Topological domain1930 – 2302373Cytoplasmic Potential
Domain58 – 15295Fibronectin type-III 1
Domain157 – 25195Fibronectin type-III 2
Domain307 – 39488Fibronectin type-III 3
Domain399 – 49092Fibronectin type-III 4
Domain474 – 56693Fibronectin type-III 5
Domain567 – 66094Fibronectin type-III 6
Domain667 – 75690Fibronectin type-III 7
Domain761 – 85191Fibronectin type-III 8
Domain856 – 94590Fibronectin type-III 9
Domain950 – 104899Fibronectin type-III 10
Domain1055 – 114894Fibronectin type-III 11
Domain1153 – 124088Fibronectin type-III 12
Domain1245 – 133894Fibronectin type-III 13
Domain1343 – 142785Fibronectin type-III 14
Domain1433 – 1536104Fibronectin type-III 15
Domain1541 – 163999Fibronectin type-III 16
Domain1644 – 1743100Fibronectin type-III 17
Domain2006 – 2262257Tyrosine-protein phosphatase

Sites

Active site22031Phosphocysteine intermediate By similarity

Amino acid modifications

Glycosylation541N-linked (GlcNAc...) Potential
Glycosylation1621N-linked (GlcNAc...) Potential
Glycosylation1691N-linked (GlcNAc...) Potential
Glycosylation3181N-linked (GlcNAc...) Potential
Glycosylation3541N-linked (GlcNAc...) Potential
Glycosylation3891N-linked (GlcNAc...) Potential
Glycosylation7331N-linked (GlcNAc...) Potential
Glycosylation7461N-linked (GlcNAc...) Potential
Glycosylation9041N-linked (GlcNAc...) Potential
Glycosylation9981N-linked (GlcNAc...) Potential
Glycosylation10101N-linked (GlcNAc...) Potential
Glycosylation10401N-linked (GlcNAc...) Potential
Glycosylation12511N-linked (GlcNAc...) Potential
Glycosylation12561N-linked (GlcNAc...) Potential
Glycosylation18051N-linked (GlcNAc...) Potential

Experimental info

Mutagenesis21711E → D: Enhances the tyrosine-protein phosphatase activity but abolishes the phosphatidylinositol phosphatase activity. Ref.2
Mutagenesis22031C → S: Abolishes the weak tyrosine-protein phosphatase activity. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: F0FA703022EB25D5

FASTA2,302256,824
        10         20         30         40         50         60 
MMDFHFSFLF LLIGTSESQV DVSSSFDGTG YDITLSSVSA TTYSSPVSRT LATNVTKPGP 

        70         80         90        100        110        120 
PVFLAGERVG SAGILLSWNT PPNPNGRIIS YVVKYKEVCP WMQTAYTRAR AKPDSLEVLL 

       130        140        150        160        170        180 
TNLNPGTTYE IKVAAENNAG IGVFSDPFLF QTAESAPGKV VNLTVEALNY SAVNLIWYLP 

       190        200        210        220        230        240 
RQPNGKITSF KISVKHARSG IVVKDVSLRV EDILSGKLPE CNENSESFLW STTSPSPTLG 

       250        260        270        280        290        300 
RVTPTVRTTQ SSSTAARSKI SSVWKEPISF VVTHLRPYTT YLFEVSAVTT EAGYIDSTIV 

       310        320        330        340        350        360 
RTPESVPEGP PQNCIMGNVT GKAFSISWDP PTIVTGKFSY RVELYGPSGR ILDNSTKDLR 

       370        380        390        400        410        420 
FAFTHLTPFT MYDVYVAAET SAGVGPKSNL SVFTPPDVPG AVFDLQIAEV EATEIRITWR 

       430        440        450        460        470        480 
KPRQPNGIIS QYRVKVSVLE TGVVLENTLL TGQDESISNP MSPEIMNLVD PMIGFYEGSG 

       490        500        510        520        530        540 
EMSSDLHSPA SFIYNSHPHN DFPASTRAEE QSSPVVTTRN QYMTDITAEQ LSYVVRRLVP 

       550        560        570        580        590        600 
FTEHTISVSA FTIMGEGPPT VLTVRTREQV PSSIQIINYK NISSSSILLY WDPPEYPNGK 

       610        620        630        640        650        660 
ITHYTIYATE LDTNRAFQMT TVDNSFLITG LKKYTRYKMR VAASTHVGES SLSEENDIFV 

       670        680        690        700        710        720 
RTPEDEPESS PQDVQVTGVS PSELRLKWSP PEKPNGIIIA YEVLYQNADT LFVKNTSTTD 

       730        740        750        760        770        780 
IIISDLKPYT LYNISIRSYT RLGHGNQSSS LLSVRTSETV PDSAPENITY KNISSGEIEI 

       790        800        810        820        830        840 
SFLPPRSPNG IIQKYTIYLK RSNSHEARTI NTTSLTQTIG GLKKYTHYVI EVSASTLKGE 

       850        860        870        880        890        900 
GIRSRPISIL TEEDAPDSPP QNFSVKQLSG VTVMLSWQPP LEPNGIILYY TVYVWDKSSL 

       910        920        930        940        950        960 
RAINATEASL VLSDLDYNVD YGACVTASTR FGDGNARSSI INFRTPEGEP SDPPNDVHYV 

       970        980        990       1000       1010       1020 
NLSSSSIILF WTPPVKPNGI IQYYSVYYQN TSGTFVQNFT LLQVTKESDN VTVSARIYRL 

      1030       1040       1050       1060       1070       1080 
AIFSYYTFWL TASTSVGNGN KSSDIIHVYT DQDIPEGPVG NLTFESISST AIHVSWEPPS 

      1090       1100       1110       1120       1130       1140 
QPNGLVFYYL SLNLQQSPPR HMIPPLVTYE NSIDFDDLEK YTDYIFKITP STEKGFSETY 

      1150       1160       1170       1180       1190       1200 
TTQLHIKTEE DVPDTPPIIN TFKNLSSTSI LLSWDPPLKP NGAILGYHLT LQGPHANHTF 

      1210       1220       1230       1240       1250       1260 
VTSGNHIVLE ELSPFTLYSF FAAARTMKGL GPSSILFFYT DESAPLAPPQ NLTLINYTSD 

      1270       1280       1290       1300       1310       1320 
FVWLTWSPSP LPGGIVKVYS FKIHEHETDT VFYKNISGLQ TDAKLEGLEP VSTYSVSVSA 

      1330       1340       1350       1360       1370       1380 
FTKVGNGNQY SNVVEFTTQE SVPEAVRNIE CVARDWQSVS VRWDPPRKTN GIIIHYMITV 

      1390       1400       1410       1420       1430       1440 
GGNSTKVSPR DPTYTFTKLL PNTSYVFEVR ASTSAGEGNE SRCDISTLPE TVPSAPTNVA 

      1450       1460       1470       1480       1490       1500 
FSNVQSTSAT LTWTKPDTIF GYFQNYKITT QLRAQKCREW EPEECIEHQK DQYLYEANQT 

      1510       1520       1530       1540       1550       1560 
EETVHGLKKF RWYRFQVAAS TNVGYSNASE WISTQTLPGP PDGPPENVHV VATSPFGINI 

      1570       1580       1590       1600       1610       1620 
SWSEPAVITG PTFYLIDVKS VDDDDFNISF LKSNEENKTT EINNLEVFTR YSVVITAFVG 

      1630       1640       1650       1660       1670       1680 
NVSRAYTDGK SSAEVIITTL ESVPKDPPNN MTFQKIPDEV TKFQLTFLPP SQPNGNIRVY 

      1690       1700       1710       1720       1730       1740 
QALVYREDDP TAVQIHNFSI IQKTDTSIIA MLEGLKGGHT YNISVYAINS AGAGPKVQMR 

      1750       1760       1770       1780       1790       1800 
ITMDIKAPAR PKSKPIPIRD ATGKLLVTST TITIRMPICY YNDDHGPIRN VQVLVAETGA 

      1810       1820       1830       1840       1850       1860 
QQDGNVTKWY DAYFNKARPY FTNEGFPNPP CIEGKTKFSG NEEIYVIGAD NACMIPGNEE 

      1870       1880       1890       1900       1910       1920 
KICNGPLKPK KQYLFKFRAT NVMGQFTDSE YSDPIKTLGE GLSERTVEII LSVTLCILSI 

      1930       1940       1950       1960       1970       1980 
ILLGTAIFAF VRIRQKQKEG GTYSPRDAEI IDTKFKLDQL ITVADLELKD ERLTRLLSYR 

      1990       2000       2010       2020       2030       2040 
KSIKPISKKS FLQHVEELCT NSNLKFQEEF SELPKFLQDL SSTDADLPWN RAKNRFPNIK 

      2050       2060       2070       2080       2090       2100 
PYNNNRVKLI ADVSLPGSDY INASYVSGYL CPNEFIATQG PLPGTVGDFW RMVWETRTKT 

      2110       2120       2130       2140       2150       2160 
LVMLTQCFEK GRIRCHQYWP EDNKPVTVFG DIVITKLMED IQIDWTIRDL KIERHGDCMT 

      2170       2180       2190       2200       2210       2220 
VRQCNFTGWP EHGVPENTTP LIHFVKLVRT SRAHDTTPMV VHCSAGVGRT GVFIALDHLT 

      2230       2240       2250       2260       2270       2280 
QHINNHDFVD IYGLVAELRS ERMCMVQNLA QYIFLHQCIL DLLSNKGGHQ PVCFVNYSTL 

      2290       2300 
QKMDSLDAME GDVELEWEET TM

« Hide

References

[1]"Proliferating and migrating mesangial cells responding to injury express a novel receptor protein-tyrosine phosphatase in experimental mesangial proliferative glomerulonephritis."
Wright M.B., Hugo C., Seifert R., Disteche C.M., Bowen-Pope D.F.
J. Biol. Chem. 273:23929-23937(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION.
Strain: Wistar.
[2]"Protein tyrosine phosphatase RQ is a phosphatidylinositol phosphatase that can regulate cell survival and proliferation."
Oganesian A., Poot M., Daum G., Coats S.A., Wright M.B., Seifert R.A., Bowen-Pope D.F.
Proc. Natl. Acad. Sci. U.S.A. 100:7563-7568(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ENZYME ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF GLU-2171 AND CYS-2203.
[3]"PTPRQ is a novel phosphatidylinositol phosphatase that can be expressed as a cytoplasmic protein or as a subcellularly localized receptor-like protein."
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.
Exp. Cell Res. 287:374-386(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF063249 mRNA. Translation: AAC34801.1.
IPIIPI00209764.
PIRT14328.
RefSeqNP_075214.1. NM_022925.1.
UniGeneRn.30011.

3D structure databases

HSSPHSSP built from PDB template 2HC1 based on UniProtKB P23467.
ProteinModelPortalO88488.
ModBaseSearch...

Proteomic databases

PaxDbO88488.
PRIDEO88488.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID360417.
KEGGrno:360417.
UCSCRGD:620779. rat.

Organism-specific databases

CTD374462.
RGD620779. Ptprq.

Phylogenomic databases

eggNOGNOG12793.
HOGENOMHOG000214125.
HOVERGENHBG108308.

Gene expression databases

GenevestigatorO88488.

Family and domain databases

Gene3D2.60.40.10. 18 hits.
InterProIPR003961. Fibronectin_type3.
IPR013783. Ig-like_fold.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
PfamPF00041. fn3. 14 hits.
PF00102. Y_phosphatase. 1 hit.
[Graphical view]
PRINTSPR00700. PRTYPHPHTASE.
SMARTSM00060. FN3. 16 hits.
SM00194. PTPc. 1 hit.
[Graphical view]
SUPFAMSSF49265. FN_III-like. 16 hits.
PROSITEPS50853. FN3. 17 hits.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio672803.

Entry information

Entry namePTPRQ_RAT
AccessionPrimary (citable) accession number: O88488
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: November 1, 1998
Last modified: April 3, 2013
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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