PTPRK_MOUSE
ID PTPRK_MOUSE Reviewed; 1457 AA.
AC P35822;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Receptor-type tyrosine-protein phosphatase kappa;
DE Short=Protein-tyrosine phosphatase kappa;
DE Short=R-PTP-kappa;
DE EC=3.1.3.48;
DE Flags: Precursor;
GN Name=Ptprk; Synonyms=Ptpk;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=RI; TISSUE=Brain;
RX PubMed=8474452; DOI=10.1128/mcb.13.5.2942-2951.1993;
RA Jiang Y.P., Wang H., D'Eustachio P., Musacchio J.M., Schlessinger J.,
RA Sap J.;
RT "Cloning and characterization of R-PTP-kappa, a new member of the receptor
RT protein tyrosine phosphatase family with a proteolytically cleaved cellular
RT adhesion molecule-like extracellular region.";
RL Mol. Cell. Biol. 13:2942-2951(1993).
RN [2]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-139; ASN-415 AND ASN-461.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-868, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Regulation of processes involving cell contact and adhesion
CC such as growth control, tumor invasion, and metastasis. Negative
CC regulator of EGFR signaling pathway. Forms complexes with beta-catenin
CC and gamma-catenin/plakoglobin. Beta-catenin may be a substrate for the
CC catalytic activity of PTPRK/PTP-kappa.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10044};
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- TISSUE SPECIFICITY: High levels in liver and kidney. Lower levels in
CC lung, brain and heart. Not seen in spleen and testis.
CC -!- DEVELOPMENTAL STAGE: Developmentally regulated with highest expression
CC found in developing areas or in areas capable of developmental
CC plasticity.
CC -!- PTM: This protein undergoes proteolytic processing.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Receptor class 2B subfamily. {ECO:0000305}.
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DR EMBL; L10106; AAA40021.1; -; mRNA.
DR CCDS; CCDS35874.1; -.
DR PIR; A48066; A48066.
DR RefSeq; NP_033009.1; NM_008983.2.
DR AlphaFoldDB; P35822; -.
DR SMR; P35822; -.
DR BioGRID; 202500; 10.
DR IntAct; P35822; 1.
DR MINT; P35822; -.
DR STRING; 10090.ENSMUSP00000126279; -.
DR GlyConnect; 2671; 4 N-Linked glycans (2 sites).
DR GlyGen; P35822; 12 sites, 4 N-linked glycans (2 sites).
DR iPTMnet; P35822; -.
DR PhosphoSitePlus; P35822; -.
DR MaxQB; P35822; -.
DR PaxDb; P35822; -.
DR PRIDE; P35822; -.
DR ProteomicsDB; 301946; -.
DR Antibodypedia; 32782; 57 antibodies from 20 providers.
DR DNASU; 19272; -.
DR Ensembl; ENSMUST00000166468; ENSMUSP00000126279; ENSMUSG00000019889.
DR GeneID; 19272; -.
DR KEGG; mmu:19272; -.
DR UCSC; uc007esk.1; mouse.
DR CTD; 5796; -.
DR MGI; MGI:103310; Ptprk.
DR VEuPathDB; HostDB:ENSMUSG00000019889; -.
DR eggNOG; KOG4228; Eukaryota.
DR GeneTree; ENSGT00940000156249; -.
DR HOGENOM; CLU_001645_0_2_1; -.
DR InParanoid; P35822; -.
DR OMA; RIATKXK; -.
DR OrthoDB; 411281at2759; -.
DR PhylomeDB; P35822; -.
DR TreeFam; TF312900; -.
DR Reactome; R-MMU-182971; EGFR downregulation.
DR BioGRID-ORCS; 19272; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Ptprk; mouse.
DR PRO; PR:P35822; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; P35822; protein.
DR Bgee; ENSMUSG00000019889; Expressed in embryonic post-anal tail and 296 other tissues.
DR ExpressionAtlas; P35822; baseline and differential.
DR Genevisible; P35822; MM.
DR GO; GO:0030424; C:axon; IDA:MGI.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005911; C:cell-cell junction; ISO:MGI.
DR GO; GO:0030425; C:dendrite; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0031256; C:leading edge membrane; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR GO; GO:0001750; C:photoreceptor outer segment; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0008013; F:beta-catenin binding; ISO:MGI.
DR GO; GO:0045295; F:gamma-catenin binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:MGI.
DR GO; GO:0007155; P:cell adhesion; ISO:MGI.
DR GO; GO:0016477; P:cell migration; ISO:MGI.
DR GO; GO:0034614; P:cellular response to reactive oxygen species; ISO:MGI.
DR GO; GO:0034644; P:cellular response to UV; ISO:MGI.
DR GO; GO:0048041; P:focal adhesion assembly; ISO:MGI.
DR GO; GO:0045786; P:negative regulation of cell cycle; ISO:MGI.
DR GO; GO:0030336; P:negative regulation of cell migration; ISO:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0010839; P:negative regulation of keratinocyte proliferation; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0031175; P:neuron projection development; ISO:MGI.
DR GO; GO:0006470; P:protein dephosphorylation; IDA:MGI.
DR GO; GO:0034394; P:protein localization to cell surface; ISO:MGI.
DR GO; GO:0007165; P:signal transduction; ISO:MGI.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISO:MGI.
DR CDD; cd00063; FN3; 2.
DR CDD; cd06263; MAM; 1.
DR Gene3D; 2.60.40.10; -; 4.
DR Gene3D; 3.90.190.10; -; 2.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR000998; MAM_dom.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000242; PTP_cat.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF00629; MAM; 1.
DR Pfam; PF00102; Y_phosphatase; 2.
DR PRINTS; PR00020; MAMDOMAIN.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00060; FN3; 3.
DR SMART; SM00409; IG; 1.
DR SMART; SM00137; MAM; 1.
DR SMART; SM00194; PTPc; 2.
DR SMART; SM00404; PTPc_motif; 2.
DR SUPFAM; SSF48726; SSF48726; 1.
DR SUPFAM; SSF49265; SSF49265; 2.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF52799; SSF52799; 2.
DR PROSITE; PS50853; FN3; 3.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS00740; MAM_1; 1.
DR PROSITE; PS50060; MAM_2; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 2.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 2.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Hydrolase; Immunoglobulin domain; Membrane;
KW Phosphoprotein; Protein phosphatase; Receptor; Reference proteome; Repeat;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..1457
FT /note="Receptor-type tyrosine-protein phosphatase kappa"
FT /id="PRO_0000025447"
FT TOPO_DOM 26..752
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 753..774
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 775..1457
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 30..193
FT /note="MAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT DOMAIN 195..280
FT /note="Ig-like C2-type"
FT DOMAIN 293..388
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 391..487
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 490..594
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 595..688
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 899..1159
FT /note="Tyrosine-protein phosphatase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT DOMAIN 1191..1453
FT /note="Tyrosine-protein phosphatase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT ACT_SITE 1100
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 1394
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 1068
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1100..1106
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1144
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 868
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 415
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 423
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 435
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 461
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 551
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 585
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 589
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 606
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 689
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 215..269
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 1457 AA; 164186 MW; 19D4B99B7ECE8605 CRC64;
MDVAAAALPA FVALWLLYPW PLLGSALGQF SAGGCTFDDG PGACDYHQDL YDDFEWVHVS
AQEPHYLPPE MPQGSYMVVD SSNHDPGEKA RLQLPTMKEN DTHCIDFSYL LYSQKGLNPG
TLNILVRVNK GPLANPIWNV TGFTGRDWLR AELAVSTFWP NEYQVIFEAE VSGGRSGYIA
IDDIQVLSYP CDKSPHFLRL GDVEVNAGQN ATFQCIATGR DAVHNKLWLQ RRNGEDIPVA
QTKNINHRRF AASFRLQEVT KTDQDLYRCV TQSERGSGVS NFAQLIVREP PRPIAPPQLL
GVGPTYLLIQ LNANSIIGDG PIILKEVEYR MTSGSWTETH AVNAPTYKLW HLDPDTEYEI
RVLLTRPGEG GTGLPGPPLI TRTKCAEPMR TPKTLKIAEI QARRIAVDWE SLGYNITRCH
TFNVTICYHY FRGHNESRAD CLDMDPKAPQ HVVNHLPPYT NVSLKMILTN PEGRKESEET
IIQTDEDVPG PVPVKSLQGT SFENKIFLNW KEPLEPNGII TQYEVSYSSI RSFDPAVPVA
GPPQTVSNLW NSTHHVFMHL HPGTTYQFFI RASTVKGFGP ATAINVTTNI SAPSLPDYEG
VDASLNETAT TITVLLRPAQ AKGAPISAYQ IVVEQLHPHR TKREAGAMEC YQVPVTYQNA
LSGGAPYYFA AELPPGNLPE PAPFTVGDNR TYKGFWNPPL APRKGYNIYF QAMSSVEKET
KTQCVRIATK AAATEEPEVI PDPAKQTDRV VKIAGISAGI LVFILLLLVV IVIVKKSKLA
KKRKDAMGNT RQEMTHMVNA MDRSYADQST LHAEDPLSLT FMDQHNFSPR LPNDPLVPTA
VLDENHSATA ESSRLLDVPR YLCEGTESPY QTGQLHPAIR VADLLQHINL MKTSDSYGFK
EEYESFFEGQ SASWDVAKKD QNRAKNRYGN IIAYDHSRVI LQPVEDDPSS DYINANYIDI
WLYRDGYQRP SHYIATQGPV HETVYDFWRM VWQEQSACIV MVTNLVEVGR VKCYKYWPDD
TEVYGDFKVT CVEMEPLAEY VVRTFTLERR GYNEIREVKQ FHFTGWPDHG VPYHATGLLS
FIRRVKLSNP PSAGPIVVHC SAGAGRTGCY IVIDIMLDMA EREGVVDIYN CVKALRSRRI
NMVQTEEQYI FIHDAILEAC LCGETAIPVC EFKAAYFDMI RIDSQTNSSH LKDEFQTLNS
VTPRLQAEDC SIACLPRNHD KNRFMDMLPP DRCLPFLITI DGESSNYINA ALMDSYRQPA
AFIVTQYPLP NTVKDFWRLV YDYGCTSIVM LNEVDLSQGC PQYWPEEGML RYGPIQVECM
SCSMDCDVIN RIFRICNLTR PQEGYLMVQQ FQYLGWASHR EVPGSKRSFL KLILQVEKWQ
EECEEGEGRT IIHCLNGGGR SGMFCAIGIV VEMVKRQNVV DVFHAVKTLR NSKPNMVEAP
EQYRFCYDVA LEYLESS
