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P35822 (PTPRK_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Receptor-type tyrosine-protein phosphatase kappa
Short name=Protein-tyrosine phosphatase kappa
Short name=R-PTP-kappa
EC=3.1.3.48
Gene names
Name:Ptprk
Synonyms:Ptpk
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length1457 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Regulation of processes involving cell contact and adhesion such as growth control, tumor invasion, and metastasis. Negative regulator of EGFR signaling pathway. Forms complexes with beta-catenin and gamma-catenin/plakoglobin. Beta-catenin may be a substrate for the catalytic activity of PTPRK/PTP-kappa.

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Subcellular location

Membrane; Single-pass type I membrane protein.

Tissue specificity

High levels in liver and kidney. Lower levels in lung, brain and heart. Not seen in spleen and testis.

Developmental stage

Developmentally regulated with highest expression found in developing areas or in areas capable of developmental plasticity.

Post-translational modification

This protein undergoes proteolytic processing.

Sequence similarities

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

Contains 4 fibronectin type-III domains.

Contains 1 Ig-like C2-type (immunoglobulin-like) domain.

Contains 1 MAM domain.

Contains 2 tyrosine-protein phosphatase domains.

Ontologies

Keywords
   Cellular componentMembrane
   DomainImmunoglobulin domain
Repeat
Signal
Transmembrane
Transmembrane helix
   Molecular functionHydrolase
Protein phosphatase
Receptor
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell migration

Inferred from electronic annotation. Source: Compara

cellular response to UV

Inferred from electronic annotation. Source: Compara

cellular response to reactive oxygen species

Inferred from electronic annotation. Source: Compara

focal adhesion assembly

Inferred from electronic annotation. Source: Compara

negative regulation of cell cycle

Inferred from electronic annotation. Source: Compara

negative regulation of cell migration

Inferred from electronic annotation. Source: Compara

negative regulation of keratinocyte proliferation

Inferred from electronic annotation. Source: Compara

negative regulation of transcription, DNA-dependent

Inferred from electronic annotation. Source: Compara

protein localization to cell surface

Inferred from electronic annotation. Source: Compara

transforming growth factor beta receptor signaling pathway

Inferred from electronic annotation. Source: Compara

   Cellular_componentaxon

Inferred from direct assay PubMed 18308476. Source: MGI

cell surface

Inferred from electronic annotation. Source: Compara

cell-cell junction

Inferred from electronic annotation. Source: Compara

dendrite

Inferred from direct assay PubMed 18308476. Source: MGI

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

leading edge membrane

Inferred from electronic annotation. Source: Compara

neuronal cell body

Inferred from direct assay PubMed 18308476. Source: MGI

photoreceptor outer segment

Inferred from direct assay PubMed 18308476. Source: MGI

   Molecular_functionprotein tyrosine phosphatase activity

Inferred from direct assay Ref.1. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Potential
Chain26 – 14571432Receptor-type tyrosine-protein phosphatase kappa
PRO_0000025447

Regions

Topological domain26 – 752727Extracellular Potential
Transmembrane753 – 77422Helical; Potential
Topological domain775 – 1457683Cytoplasmic Potential
Domain30 – 193164MAM
Domain195 – 28086Ig-like C2-type
Domain290 – 38293Fibronectin type-III 1
Domain388 – 48497Fibronectin type-III 2
Domain489 – 588100Fibronectin type-III 3
Domain589 – 688100Fibronectin type-III 4
Domain899 – 1159261Tyrosine-protein phosphatase 1
Domain1191 – 1453263Tyrosine-protein phosphatase 2
Region1100 – 11067Substrate binding By similarity

Sites

Active site11001Phosphocysteine intermediate By similarity
Active site13941Phosphocysteine intermediate By similarity
Binding site10681Substrate By similarity
Binding site11441Substrate By similarity

Amino acid modifications

Glycosylation1001N-linked (GlcNAc...) Potential
Glycosylation1391N-linked (GlcNAc...) Ref.2
Glycosylation2101N-linked (GlcNAc...) Potential
Glycosylation4151N-linked (GlcNAc...) Ref.2
Glycosylation4231N-linked (GlcNAc...) Potential
Glycosylation4351N-linked (GlcNAc...) Potential
Glycosylation4611N-linked (GlcNAc...) Ref.2
Glycosylation5511N-linked (GlcNAc...) Potential
Glycosylation5851N-linked (GlcNAc...) Potential
Glycosylation5891N-linked (GlcNAc...) Potential
Glycosylation6061N-linked (GlcNAc...) Potential
Glycosylation6891N-linked (GlcNAc...) Potential
Disulfide bond215 ↔ 269 Potential

Sequences

Sequence LengthMass (Da)Tools
P35822 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: 19D4B99B7ECE8605

FASTA1,457164,186
        10         20         30         40         50         60 
MDVAAAALPA FVALWLLYPW PLLGSALGQF SAGGCTFDDG PGACDYHQDL YDDFEWVHVS 

        70         80         90        100        110        120 
AQEPHYLPPE MPQGSYMVVD SSNHDPGEKA RLQLPTMKEN DTHCIDFSYL LYSQKGLNPG 

       130        140        150        160        170        180 
TLNILVRVNK GPLANPIWNV TGFTGRDWLR AELAVSTFWP NEYQVIFEAE VSGGRSGYIA 

       190        200        210        220        230        240 
IDDIQVLSYP CDKSPHFLRL GDVEVNAGQN ATFQCIATGR DAVHNKLWLQ RRNGEDIPVA 

       250        260        270        280        290        300 
QTKNINHRRF AASFRLQEVT KTDQDLYRCV TQSERGSGVS NFAQLIVREP PRPIAPPQLL 

       310        320        330        340        350        360 
GVGPTYLLIQ LNANSIIGDG PIILKEVEYR MTSGSWTETH AVNAPTYKLW HLDPDTEYEI 

       370        380        390        400        410        420 
RVLLTRPGEG GTGLPGPPLI TRTKCAEPMR TPKTLKIAEI QARRIAVDWE SLGYNITRCH 

       430        440        450        460        470        480 
TFNVTICYHY FRGHNESRAD CLDMDPKAPQ HVVNHLPPYT NVSLKMILTN PEGRKESEET 

       490        500        510        520        530        540 
IIQTDEDVPG PVPVKSLQGT SFENKIFLNW KEPLEPNGII TQYEVSYSSI RSFDPAVPVA 

       550        560        570        580        590        600 
GPPQTVSNLW NSTHHVFMHL HPGTTYQFFI RASTVKGFGP ATAINVTTNI SAPSLPDYEG 

       610        620        630        640        650        660 
VDASLNETAT TITVLLRPAQ AKGAPISAYQ IVVEQLHPHR TKREAGAMEC YQVPVTYQNA 

       670        680        690        700        710        720 
LSGGAPYYFA AELPPGNLPE PAPFTVGDNR TYKGFWNPPL APRKGYNIYF QAMSSVEKET 

       730        740        750        760        770        780 
KTQCVRIATK AAATEEPEVI PDPAKQTDRV VKIAGISAGI LVFILLLLVV IVIVKKSKLA 

       790        800        810        820        830        840 
KKRKDAMGNT RQEMTHMVNA MDRSYADQST LHAEDPLSLT FMDQHNFSPR LPNDPLVPTA 

       850        860        870        880        890        900 
VLDENHSATA ESSRLLDVPR YLCEGTESPY QTGQLHPAIR VADLLQHINL MKTSDSYGFK 

       910        920        930        940        950        960 
EEYESFFEGQ SASWDVAKKD QNRAKNRYGN IIAYDHSRVI LQPVEDDPSS DYINANYIDI 

       970        980        990       1000       1010       1020 
WLYRDGYQRP SHYIATQGPV HETVYDFWRM VWQEQSACIV MVTNLVEVGR VKCYKYWPDD 

      1030       1040       1050       1060       1070       1080 
TEVYGDFKVT CVEMEPLAEY VVRTFTLERR GYNEIREVKQ FHFTGWPDHG VPYHATGLLS 

      1090       1100       1110       1120       1130       1140 
FIRRVKLSNP PSAGPIVVHC SAGAGRTGCY IVIDIMLDMA EREGVVDIYN CVKALRSRRI 

      1150       1160       1170       1180       1190       1200 
NMVQTEEQYI FIHDAILEAC LCGETAIPVC EFKAAYFDMI RIDSQTNSSH LKDEFQTLNS 

      1210       1220       1230       1240       1250       1260 
VTPRLQAEDC SIACLPRNHD KNRFMDMLPP DRCLPFLITI DGESSNYINA ALMDSYRQPA 

      1270       1280       1290       1300       1310       1320 
AFIVTQYPLP NTVKDFWRLV YDYGCTSIVM LNEVDLSQGC PQYWPEEGML RYGPIQVECM 

      1330       1340       1350       1360       1370       1380 
SCSMDCDVIN RIFRICNLTR PQEGYLMVQQ FQYLGWASHR EVPGSKRSFL KLILQVEKWQ 

      1390       1400       1410       1420       1430       1440 
EECEEGEGRT IIHCLNGGGR SGMFCAIGIV VEMVKRQNVV DVFHAVKTLR NSKPNMVEAP 

      1450 
EQYRFCYDVA LEYLESS

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of R-PTP-kappa, a new member of the receptor protein tyrosine phosphatase family with a proteolytically cleaved cellular adhesion molecule-like extracellular region."
Jiang Y.P., Wang H., D'Eustachio P., Musacchio J.M., Schlessinger J., Sap J.
Mol. Cell. Biol. 13:2942-2951(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: RI.
Tissue: Brain.
[2]"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-139; ASN-415 AND ASN-461, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L10106 mRNA. Translation: AAA40021.1.
IPIIPI00123040.
PIRA48066.
RefSeqNP_033009.1. NM_008983.2.
UniGeneMm.332303.

3D structure databases

ProteinModelPortalP35822.
SMRP35822. Positions 32-595, 876-1456.
ModBaseSearch...

Protein-protein interaction databases

MINTMINT-4109163.

PTM databases

PhosphoSiteP35822.

Proteomic databases

PaxDbP35822.
PRIDEP35822.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000166468; ENSMUSP00000126279; ENSMUSG00000019889.
GeneID19272.
KEGGmmu:19272.
UCSCuc007esk.1. mouse.

Organism-specific databases

CTD5796.
MGIMGI:103310. Ptprk.

Phylogenomic databases

eggNOGCOG5599.
GeneTreeENSGT00640000091300.
HOGENOMHOG000049029.
HOVERGENHBG062785.
InParanoidP35822.
KOK06776.
OMAYRDGYQR.
OrthoDBEOG4ZW595.

Gene expression databases

ArrayExpressP35822.
BgeeP35822.
CleanExMM_PTPRK.
GenevestigatorP35822.
GermOnlineENSMUSG00000019889. Mus musculus.

Family and domain databases

Gene3D2.60.40.10. 4 hits.
InterProIPR008985. ConA-like_lec_gl_sf.
IPR003961. Fibronectin_type3.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR000998. MAM_dom.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
PfamPF00041. fn3. 2 hits.
PF00629. MAM. 1 hit.
PF00102. Y_phosphatase. 2 hits.
[Graphical view]
PRINTSPR00020. MAMDOMAIN.
PR00700. PRTYPHPHTASE.
SMARTSM00060. FN3. 3 hits.
SM00409. IG. 1 hit.
SM00137. MAM. 1 hit.
SM00194. PTPc. 2 hits.
[Graphical view]
SUPFAMSSF49899. ConA_like_lec_gl. 1 hit.
SSF49265. FN_III-like. 3 hits.
PROSITEPS50853. FN3. 4 hits.
PS50835. IG_LIKE. 1 hit.
PS00740. MAM_1. 1 hit.
PS50060. MAM_2. 1 hit.
PS00383. TYR_PHOSPHATASE_1. 2 hits.
PS50056. TYR_PHOSPHATASE_2. 2 hits.
PS50055. TYR_PHOSPHATASE_PTP. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPTPRK. mouse.
NextBio296162.
PMAP-CutDBP35822.
SOURCESearch...

Entry information

Entry namePTPRK_MOUSE
AccessionPrimary (citable) accession number: P35822
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: May 29, 2013
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents