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P0C5E4 (PTPRQ_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·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):
Receptor-type tyrosine-protein phosphatase Q
Short name=PTP-RQ
Short name=R-PTP-Q
EC=3.1.3.48
Gene names
Name:Ptprq
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length2300 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.

Subcellular location

Membrane; Single-pass type I membrane protein By similarity.

Tissue specificity

In the inner ear of the early postnatal mouse, it is present in hair bundles in the cochlea and in the vestibule. Restricted to the hair bundles and not detected in any other cell type within the inner ear. Restricted to the basal region of the hair bundle (at protein level). Ref.2

Disruption phenotype

Mice show rapid postnatal deterioration in cochlear hair-bundle structure, associated with smaller than normal transducer currents with otherwise normal adaptation properties, a progressive loss of basal-coil cochlear hair cells, and deafness. Ref.2

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Chain18 – 23002283Phosphatidylinositol phosphatase PTPRQ
PRO_0000302851

Regions

Topological domain18 – 19061889Extracellular Potential
Transmembrane1907 – 192721Helical; Potential
Topological domain1928 – 2300373Cytoplasmic Potential
Domain59 – 15496Fibronectin type-III 1
Domain158 – 25396Fibronectin type-III 2
Domain309 – 39789Fibronectin type-III 3
Domain400 – 49596Fibronectin type-III 4
Domain497 – 56468Fibronectin type-III 5
Domain568 – 66396Fibronectin type-III 6
Domain668 – 75790Fibronectin type-III 7
Domain762 – 85291Fibronectin type-III 8
Domain857 – 94690Fibronectin type-III 9
Domain951 – 1051101Fibronectin type-III 10
Domain1056 – 114994Fibronectin type-III 11
Domain1154 – 124188Fibronectin type-III 12
Domain1246 – 133994Fibronectin type-III 13
Domain1343 – 142987Fibronectin type-III 14
Domain1433 – 1537105Fibronectin type-III 15
Domain1542 – 164099Fibronectin type-III 16
Domain1645 – 1746102Fibronectin type-III 17
Domain2004 – 2260257Tyrosine-protein phosphatase

Sites

Active site22011Phosphocysteine intermediate By similarity

Amino acid modifications

Glycosylation531N-linked (GlcNAc...) Potential
Glycosylation1611N-linked (GlcNAc...) Potential
Glycosylation1681N-linked (GlcNAc...) Potential
Glycosylation3171N-linked (GlcNAc...) Potential
Glycosylation3531N-linked (GlcNAc...) Potential
Glycosylation3881N-linked (GlcNAc...) Potential
Glycosylation7181N-linked (GlcNAc...) Potential
Glycosylation7311N-linked (GlcNAc...) Potential
Glycosylation7441N-linked (GlcNAc...) Potential
Glycosylation9961N-linked (GlcNAc...) Potential
Glycosylation10081N-linked (GlcNAc...) Potential
Glycosylation10381N-linked (GlcNAc...) Potential
Glycosylation10591N-linked (GlcNAc...) Potential
Glycosylation12491N-linked (GlcNAc...) Potential
Glycosylation12541N-linked (GlcNAc...) Potential
Glycosylation18031N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
P0C5E4 [UniParc].

Last modified September 11, 2007. Version 1.
Checksum: 1866AE48D19FAB09

FASTA2,300256,785
        10         20         30         40         50         60 
MDFLFFFLFS LIGTSESQVD VSGSFDDTVY DITLSSISAT TYSSPVSRTL ATNVSKPGPP 

        70         80         90        100        110        120 
VFLAGERVGS AGILLSWNTP PNPNGRIISY VVKYKEVCPW MQTAYTRVRA KPDSLEVLLT 

       130        140        150        160        170        180 
NLNPGTTYEI KVAAENSAGI GVFSDPFLFQ TAESAPGKVV NLTVEALNYS AVNLIWYLPR 

       190        200        210        220        230        240 
QPNGKITSFK ISVKHARSGI VVKDVSIKVE DLLSGKLPEC NENSDSFLWS TTSPSPTLSR 

       250        260        270        280        290        300 
ATPPLRTTHL SNTLARNKIS SVWKEPISFV VTHLRPYTTY LFEVSAVTTE AGYIDSTIVR 

       310        320        330        340        350        360 
TPESVPEGPP QNCITGNVTG KAFSISWDPP AIVTGKFSYR VELYGPTGRI LDNSTKDLRF 

       370        380        390        400        410        420 
VFTHLTPFTM YDVYVAAETS AGVGPKSNLS VFTPPDVPGA VFDLQIVEVE ATEIRVSWRK 

       430        440        450        460        470        480 
PRQPNGIISQ YRVKVSVLES GVILENTLLT GQDEYINNPM TPEIMNLVDP MIGFYEGSGE 

       490        500        510        520        530        540 
MSSDLHSLAS FIYNSHPHDF PARTRVEDQR SPVVATRNQY MTDIAAEHLS YVIRRLVPFT 

       550        560        570        580        590        600 
EHTISVSAFT VMGEGPPTVL TVRTREQVPS SIQIINYKNI SSSSILLYWD PPEYPNGKIT 

       610        620        630        640        650        660 
HYTIYAMELD TNRAFQMTTV DNSFLITGLK KYTRYKMRVA ASTHVGESSL SEENDLFVRT 

       670        680        690        700        710        720 
PEDEPESSPQ DVKVTDVSPS ELSLTWSPPE KPNGIIIAYE VFYQNADALF VKNTSTTNIT 

       730        740        750        760        770        780 
LSDLKPYTLY NISIQSYTRL GHGNQSSSLL SVRTSETVPD SAPENITYKN ISSEEIEIFF 

       790        800        810        820        830        840 
LPPRSPNGII QKYTIYLKRS NSHEARTIET TSLTLTIGGL KKYTHYVIEV SASTLKGEGV 

       850        860        870        880        890        900 
RSMPISILTE EDAPDSPPQN FSVKQLSGVT VMLSWQPPLE PNGIILYYTV YVWDKVSLKT 

       910        920        930        940        950        960 
INATEVSLEL SDLDYHADYS AYVTASTRFG DGKTRSSVIN FRTPEGEPSD PPKDVHYVNL 

       970        980        990       1000       1010       1020 
SSSSIILFWT PPVKPNGIIQ YYSVYYQNTS STFVQNFTLL EVTQEPGNVT VSARIYKLAV 

      1030       1040       1050       1060       1070       1080 
FSYYTFWLTA STLVGNGNKS SDVIHVYTDQ DIPEGGVGNL TYESLSSTAI NVSWTPPSQP 

      1090       1100       1110       1120       1130       1140 
NGLVFYYVSL NLQQSPPRHR RPPLTTYENS IYFDNLEKYT DYIFKITPST EKGFSETYTA 

      1150       1160       1170       1180       1190       1200 
QLHIKTEEDV PDTPPIINTF KNLSSTSILL SWDPPLKPNG AILSYHLTLQ GTHANRTFVT 

      1210       1220       1230       1240       1250       1260 
SGNHIVLEEL SPFTLYSFLA AARTMKGLGP SSILFFYTDE SAPLAPPQNL TLINYTSDFV 

      1270       1280       1290       1300       1310       1320 
WLTWSPSPLP GGIVKVYSFK IHEHETDTVF YKNISGFQTD AKLAGLEPVS TYSISVSAFT 

      1330       1340       1350       1360       1370       1380 
KVGNGNQFSN VVKFTTQESV PDAVQNIACV ARDWQSVSVM WDPPRKANGI IIHYMITVEG 

      1390       1400       1410       1420       1430       1440 
NSTKVSPRDP MYTFTKLLAN TSYIFEVRAS TSAGEGNESQ CNVSTLPETV PSVPTNTAFS 

      1450       1460       1470       1480       1490       1500 
NVQSTSVTLR WIKPDTILGY FQNYKITTQL RAQKCREWEP EECVEHQEVQ YLYEANQTED 

      1510       1520       1530       1540       1550       1560 
TVRGLKKFQW YRFQVAASTN AGYGNASSWI STQTLPGPPD GPPENVRVVA TSPFGINISW 

      1570       1580       1590       1600       1610       1620 
NEPAIITGPT FYLIDVKSVD NDNFNISFVK SNEENKTTEI NDLEVFTRYS VVITAFVGNV 

      1630       1640       1650       1660       1670       1680 
SGAYTDGKSS AEVIITTLES VPKDPPNNMT FQKIPDEVTK FQLSFLPPSQ PNGNIQVYQA 

      1690       1700       1710       1720       1730       1740 
LVYREDDPTA VQIHNLSIIQ KTDTSVIAML EGLKGGHTYN ISVYAINSAG AGPKVQMRIT 

      1750       1760       1770       1780       1790       1800 
MDIKAPARPK TKPIPIHDAT GKLLVTSTTI TIRMPICYYN DDHGPIRNVQ VLVAEAGAQQ 

      1810       1820       1830       1840       1850       1860 
DGNVTKWYDA YFNKARPYFT NEGFPNPPCI EGKTKFSGNE EIYVIGADNA CMIPGNEEKI 

      1870       1880       1890       1900       1910       1920 
CNGPLKPKKQ YLFKFRATNV MGQFTDSEYS DPIKTLGEGL SERTVEIILS VTLCILSIIL 

      1930       1940       1950       1960       1970       1980 
LGTAIFAFAR IRQKQKEGGT YSPRDAEIID TKFKLDQLIT VADLELKDER LTRLLSYRKS 

      1990       2000       2010       2020       2030       2040 
IKPVSKKSFL QHVEELCTNN NLKFQEEFSE LPKFLQDLSS TDADLPWNRA KNRFPNIKPY 

      2050       2060       2070       2080       2090       2100 
NNNRVKLIAD VSIPGSDYIN ASYVSGYLCP NEFIATQGPL PGTVGDFWRM VWETRAKTLV 

      2110       2120       2130       2140       2150       2160 
MLTQCFEKGR IRCHQYWPED NKPVTVFGDI LITKLMEDIQ IDWTIRDLKI ERHGDCMTVR 

      2170       2180       2190       2200       2210       2220 
QCNFTGWPEH GVPENTTPLI HFVKLVRTSR AHDATPMVVH CSAGVGRTGV FIALDHLTQH 

      2230       2240       2250       2260       2270       2280 
IHDHDFVDIY GLVAELRSER MCMVQNLAQY IFLHQCILDL LSNKGGHQPV CFVNYSTLQK 

      2290       2300 
MDSLDAMEGD VELEWEETTM 

« Hide

References

« Hide 'large scale' references
[1]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[2]"A receptor-like inositol lipid phosphatase is required for the maturation of developing cochlear hair bundles."
Goodyear R.J., Legan P.K., Wright M.B., Marcotti W., Oganesian A., Coats S.A., Booth C.J., Kros C.J., Seifert R.A., Bowen-Pope D.F., Richardson G.P.
J. Neurosci. 23:9208-9219(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC021642 Genomic DNA. No translation available.
AC123948 Genomic DNA. No translation available.
AC155168 Genomic DNA. No translation available.
RefSeqNP_001074901.1. NM_001081432.1.
UniGeneMm.391418.

3D structure databases

ProteinModelPortalP0C5E4.
SMRP0C5E4. Positions 13-191, 268-437, 512-1577, 1707-1735, 1983-2296.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid231884. 9 interactions.
STRING10090.ENSMUSP00000058572.

PTM databases

PhosphoSiteP0C5E4.

Proteomic databases

PRIDEP0C5E4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000050702; ENSMUSP00000058572; ENSMUSG00000035916.
GeneID237523.
KEGGmmu:237523.
UCSCuc007gzb.1. mouse.

Organism-specific databases

CTD374462.
MGIMGI:1096349. Ptprq.

Phylogenomic databases

eggNOGCOG5599.
GeneTreeENSGT00750000117483.
HOGENOMHOG000115793.
HOVERGENHBG108308.
InParanoidP0C5E4.
KOK16910.
OMADVELEWE.
OrthoDBEOG7FXZXD.
PhylomeDBP0C5E4.
TreeFamTF351926.

Gene expression databases

BgeeP0C5E4.
CleanExMM_PTPRQ.
GenevestigatorP0C5E4.

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. SSF49265. 11 hits.
PROSITEPS50853. FN3. 16 hits.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio383394.
PROP0C5E4.
SOURCESearch...

Entry information

Entry namePTPRQ_MOUSE
AccessionPrimary (citable) accession number: P0C5E4
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: September 11, 2007
Last modified: April 16, 2014
This is version 60 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot