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   27-MAR-2024, entry version 197.
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   GlyCosmos; P35822; 12 sites, 4 glycans.
DR   GlyGen; P35822; 12 sites, 4 N-linked glycans (2 sites).
DR   iPTMnet; P35822; -.
DR   PhosphoSitePlus; P35822; -.
DR   MaxQB; P35822; -.
DR   PaxDb; 10090-ENSMUSP00000126279; -.
DR   ProteomicsDB; 301946; -.
DR   Pumba; P35822; -.
DR   Antibodypedia; 32782; 66 antibodies from 21 providers.
DR   DNASU; 19272; -.
DR   Ensembl; ENSMUST00000166468.2; ENSMUSP00000126279.2; ENSMUSG00000019889.11.
DR   GeneID; 19272; -.
DR   KEGG; mmu:19272; -.
DR   UCSC; uc007esk.1; mouse.
DR   AGR; MGI:103310; -.
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; 2875525at2759; -.
DR   PhylomeDB; P35822; -.
DR   TreeFam; TF312900; -.
DR   Reactome; R-MMU-182971; EGFR downregulation.
DR   BioGRID-ORCS; 19272; 3 hits in 80 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 299 other cell types or tissues.
DR   ExpressionAtlas; P35822; baseline and differential.
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: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:0016311; P:dephosphorylation; IEA:InterPro.
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:0045892; P:negative regulation of DNA-templated transcription; ISO:MGI.
DR   GO; GO:0010839; P:negative regulation of keratinocyte proliferation; ISO:MGI.
DR   GO; GO:0031175; P:neuron projection development; ISO: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   CDD; cd14636; R-PTPc-K-2; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 4.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 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   PANTHER; PTHR24051:SF11; PROTEIN-TYROSINE-PHOSPHATASE; 1.
DR   PANTHER; PTHR24051; SUSHI DOMAIN-CONTAINING PROTEIN 1; 1.
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; SSF52799; (Phosphotyrosine protein) phosphatases II; 2.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 2.
DR   SUPFAM; SSF48726; Immunoglobulin; 1.
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.
DR   Genevisible; P35822; MM.
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
//