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E9Q612 (PTPRO_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 31. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Receptor-type tyrosine-protein phosphatase O

Short name=R-PTP-O
EC=3.1.3.48
Alternative name(s):
Glomerular epithelial protein 1
Protein tyrosine phosphatase U2
Short name=PTP-U2
Short name=PTPase U2
Gene names
Name:Ptpro
Synonyms:GLEPP1, Ptpn15, PTPU2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1226 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Possesses tyrosine phosphatase activity. Plays a role in regulating the glomerular pressure/filtration rate relationship through an effect on podocyte structure and function. Ref.3

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Subcellular location

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

Disruption phenotype

Modification of podocyte structure such that the normal octopoid podocyte is simplified to a more amoeboid structure and that the foot processes are shorter and broader than normal. These changes are associated with altered distribution of the podocyte intermediate cytoskeletal protein vimentin/VIM. Mutant animals have a reduced glomerular filtration rate and reduced glomerular nephrin (NPHS1) content. However, there is no evidence of proteinuria. After removal of one or more kidneys, Ptpro-null animals have higher blood pressure than does their wild-type littermates. Ref.3

Sequence similarities

Belongs to the protein-tyrosine phosphatase family. Receptor class 3 subfamily.

Contains 6 fibronectin type-III domains.

Contains 1 tyrosine-protein phosphatase domain.

Ontologies

Keywords
   Cellular componentMembrane
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   Molecular functionHydrolase
Protein phosphatase
Receptor
   PTMGlycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaxon guidance

Inferred from mutant phenotype PubMed 19800005. Source: UniProtKB

cell morphogenesis

Inferred from mutant phenotype PubMed 20398064. Source: UniProtKB

glomerular visceral epithelial cell differentiation

Inferred from mutant phenotype Ref.3. Source: UniProtKB

glomerulus development

Inferred from sequence or structural similarity. Source: UniProtKB

lamellipodium assembly

Inferred from mutant phenotype PubMed 20398064. Source: UniProtKB

monocyte chemotaxis

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of canonical Wnt signaling pathway

Inferred from direct assay PubMed 20804755. Source: UniProtKB

negative regulation of glomerular filtration

Inferred from sequence or structural similarity. Source: UniProtKB

peptidyl-tyrosine dephosphorylation

Inferred from direct assay PubMed 15673668. Source: UniProtKB

regulation of glomerular filtration

Inferred from mutant phenotype Ref.3. Source: UniProtKB

slit diaphragm assembly

Inferred from mutant phenotype Ref.3. Source: UniProtKB

   Cellular_componentapical plasma membrane

Inferred from direct assay PubMed 20633639. Source: UniProtKB

dendritic spine

Inferred from direct assay PubMed 19924828. Source: UniProtKB

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

lateral plasma membrane

Inferred from direct assay PubMed 20633639. Source: UniProtKB

plasma membrane

Inferred from direct assay PubMed 15673668. Source: UniProtKB

   Molecular_functionWnt-protein binding

Inferred from direct assay PubMed 20804755. Source: UniProtKB

protein homodimerization activity

Inferred from direct assay PubMed 19573017. Source: UniProtKB

protein tyrosine phosphatase activity

Inferred from direct assay PubMed 15673668. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Wnt3aP274672EBI-8183885,EBI-2899665

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2929 Potential
Chain30 – 12261197Receptor-type tyrosine-protein phosphatase O
PRO_0000414059

Regions

Topological domain30 – 832803Extracellular Potential
Transmembrane833 – 85321Helical; Potential
Topological domain854 – 1226373Cytoplasmic Potential
Domain30 – 11586Fibronectin type-III 1
Domain339 – 43597Fibronectin type-III 2
Domain445 – 54197Fibronectin type-III 3
Domain542 – 63897Fibronectin type-III 4
Domain641 – 73494Fibronectin type-III 5
Domain735 – 82793Fibronectin type-III 6
Domain948 – 1205258Tyrosine-protein phosphatase
Region1146 – 11527Substrate binding By similarity

Sites

Active site11461Phosphocysteine intermediate By similarity
Binding site11121Substrate By similarity
Binding site11901Substrate By similarity

Amino acid modifications

Modified residue8751Phosphoserine Ref.4
Glycosylation751N-linked (GlcNAc...) Potential
Glycosylation1541N-linked (GlcNAc...) Potential
Glycosylation2271N-linked (GlcNAc...) Potential
Glycosylation2791N-linked (GlcNAc...) Potential
Glycosylation4711N-linked (GlcNAc...) Potential
Glycosylation5001N-linked (GlcNAc...) Potential
Glycosylation7101N-linked (GlcNAc...) Potential
Glycosylation7431N-linked (GlcNAc...) Potential
Glycosylation8001N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict11841Y → H in AAH52743. Ref.2

Sequences

Sequence LengthMass (Da)Tools
E9Q612 [UniParc].

Last modified April 5, 2011. Version 1.
Checksum: 3FF0BE298354BC32

FASTA1,226138,589
        10         20         30         40         50         60 
MGHLPRGTLG GRRLLPLLGL FVLLKIVTTF HVAVQDDNNI VVSLEASDIV SPASVYVVRV 

        70         80         90        100        110        120 
AGESKNYFFE FEEFNSTLPP PVVFKATYHG LYYIITLVVV NGNVVTKPSR SITVLTKPLP 

       130        140        150        160        170        180 
VTSVSIYDYK PSPETGVLFE IHYPEKYNVF SRVNISYWEG RDFRTMLYKD FFKGKTVFNH 

       190        200        210        220        230        240 
WLPGLCYSNI TFQLVSEATF NKSTLVEYSG VSHEPKQHRT APYPPRNISV RFVNLNKNNW 

       250        260        270        280        290        300 
EEPSGSFPED SFIKPPQDSI GRDRRFHFPE ETPETPPSNV SSGSPPSNVS SAWPDPNSTD 

       310        320        330        340        350        360 
YESTSQPFWW DSASAAPENE EDFVSALPAD YDTETTLDRT EKPTADPFSA FPVQMTLSWL 

       370        380        390        400        410        420 
PPKPPTAFDG FNILIEREEN FTDYLTVDEE AHEFVAELKE PGKYKLSVTT FSSSGACETR 

       430        440        450        460        470        480 
KSQSAKSLSF YISPTGEWIE ELTEKPQHVS VHVLSSTTAL MSWTSSQENY NSTIVSVVSL 

       490        500        510        520        530        540 
TCQKQKESQR LEKQYCTQVN SSKPVIENLV PGAQYQVVMY LRKGPLIGPP SDPVTFAIVP 

       550        560        570        580        590        600 
TGIKDLMLYP LGPTAVVLSW TRPILGVFRK YVVEMFYFNP TTMTSEWTTY YEIAATVSLT 

       610        620        630        640        650        660 
ASVRIASLLP AWYYNFRVTM VTWGDPELSC CDSSTISFIT APVAPEITSV EYFNSLLYIS 

       670        680        690        700        710        720 
WTYGDATTDL SHSRMLHWMV VAEGRKKIKK SVTRNVMTAI LSLPPGDIYN LSVTACTERG 

       730        740        750        760        770        780 
SNTSLPRLVK LEPAPPKSLF AVNKTQTSVT LLWVEEGVAD FFEVFCQQLG SGHNGKLQEP 

       790        800        810        820        830        840 
VAVSSHVVTI SSLLPATAYN CSVTSFSHDT PSVPTFIAVS TMVTEVNPNV VVISVLAILS 

       850        860        870        880        890        900 
TLLIGLLLVT LVILRKKHLQ MARECGAGTF VNFASLEREG KLPYSWRRSV FALLTLLPSC 

       910        920        930        940        950        960 
LWTDYLLAFY INPWSKNGLK KRKLTNPVQL DDFDSYIKDM AKDSDYKFSL QFEELKLIGL 

       970        980        990       1000       1010       1020 
DIPHFAADLP LNRCKNRYTN ILPYDFSRVR LVSMNEEEGA DYINANYIPG YNSPQEYIAT 

      1030       1040       1050       1060       1070       1080 
QGPLPETRND FWKMVLQQKS HIIVMLTQCN EKRRVKCDHY WPFTEEPIAY GDITVEMVSE 

      1090       1100       1110       1120       1130       1140 
EEEEDWASRH FRINYADEAQ DVMHFNYTAW PDHGVPPANA AESILQFVFT VRQQAAKSKG 

      1150       1160       1170       1180       1190       1200 
PMIIHCSAGV GRTGTFIALD RLLQHIRDHE FVDILGLVSE MRSYRMSMVQ TEEQYIFIHQ 

      1210       1220 
CVQLMWLRKK QQFCISDVIY ENVSKS 

« 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]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]"Altered podocyte structure in GLEPP1 (Ptpro)-deficient mice associated with hypertension and low glomerular filtration rate."
Wharram B.L., Goyal M., Gillespie P.J., Wiggins J.E., Kershaw D.B., Holzman L.B., Dysko R.C., Saunders T.L., Samuelson L.C., Wiggins R.C.
J. Clin. Invest. 106:1281-1290(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[4]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-875, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC093120 Genomic DNA. No translation available.
AC144767 Genomic DNA. No translation available.
AC163627 Genomic DNA. No translation available.
BC052743 mRNA. Translation: AAH52743.1.
RefSeqNP_035346.3. NM_011216.3.
UniGeneMm.186361.
Mm.491536.

3D structure databases

ProteinModelPortalE9Q612.
SMRE9Q612. Positions 926-1218.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActE9Q612. 1 interaction.

PTM databases

PhosphoSiteE9Q612.

Proteomic databases

PRIDEE9Q612.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000077115; ENSMUSP00000076364; ENSMUSG00000030223.
GeneID19277.
KEGGmmu:19277.
UCSCuc009emv.2. mouse.

Organism-specific databases

CTD5800.
MGIMGI:1097152. Ptpro.

Phylogenomic databases

GeneTreeENSGT00750000117631.
HOGENOMHOG000115792.
HOVERGENHBG053763.
InParanoidQ7TSY7.
KOK18035.
OMASTMVTEM.
OrthoDBEOG7PCJFZ.
TreeFamTF351926.

Gene expression databases

BgeeE9Q612.

Family and domain databases

Gene3D2.60.40.10. 3 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. 2 hits.
PF00102. Y_phosphatase. 1 hit.
[Graphical view]
PRINTSPR00700. PRTYPHPHTASE.
SMARTSM00060. FN3. 4 hits.
SM00194. PTPc. 1 hit.
[Graphical view]
SUPFAMSSF49265. SSF49265. 3 hits.
PROSITEPS50853. FN3. 5 hits.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio296184.
PROE9Q612.
SOURCESearch...

Entry information

Entry namePTPRO_MOUSE
AccessionPrimary (citable) accession number: E9Q612
Secondary accession number(s): Q7TSY7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 14, 2011
Last sequence update: April 5, 2011
Last modified: April 16, 2014
This is version 31 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