PTPRJ_CHICK
ID PTPRJ_CHICK Reviewed; 1406 AA.
AC Q9W6V5;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Receptor-type tyrosine-protein phosphatase eta;
DE Short=Protein-tyrosine phosphatase eta;
DE Short=R-PTP-eta;
DE EC=3.1.3.48;
DE AltName: Full=HPTP eta;
DE AltName: Full=Protein-tyrosine phosphatase receptor type J;
DE Short=R-PTP-J;
DE AltName: Full=Supporting-cell antigen;
DE Flags: Precursor;
GN Name=PTPRJ;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Intestine;
RX PubMed=10366616; DOI=10.1523/jneurosci.19-12-04815.1999;
RA Kruger R.P., Goodyear R.J., Legan P.K., Warchol M.E., Raphael Y.,
RA Cotanche D.A., Richardson G.P.;
RT "The supporting-cell antigen: a receptor-like protein tyrosine phosphatase
RT expressed in the sensory epithelia of the avian inner ear.";
RL J. Neurosci. 19:4815-4827(1999).
CC -!- FUNCTION: Tyrosine phosphatase which dephosphorylates or contributes to
CC the dephosphorylation of several substrates. Plays a role in cell
CC adhesion, migration, proliferation and differentiation (By similarity).
CC May influence the potential of nonsensory supporting cells to either
CC proliferate or differentiate into hair cells. {ECO:0000250,
CC ECO:0000269|PubMed:10366616}.
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: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}. Cell projection, ruffle membrane
CC {ECO:0000250}. Cell junction {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Found on the apical surfaces of retinal Mueller
CC cells, renal tubule cells and intestinal brush border cells.
CC {ECO:0000269|PubMed:10366616}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Receptor class 3 subfamily. {ECO:0000305}.
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DR EMBL; AJ238216; CAB41885.2; -; mRNA.
DR RefSeq; NP_989952.1; NM_204621.1.
DR AlphaFoldDB; Q9W6V5; -.
DR SMR; Q9W6V5; -.
DR GeneID; 395330; -.
DR KEGG; gga:395330; -.
DR CTD; 5795; -.
DR VEuPathDB; HostDB:geneid_395330; -.
DR eggNOG; KOG0791; Eukaryota.
DR InParanoid; Q9W6V5; -.
DR OrthoDB; 411281at2759; -.
DR PhylomeDB; Q9W6V5; -.
DR PRO; PR:Q9W6V5; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005911; C:cell-cell junction; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016791; F:phosphatase activity; ISS:UniProtKB.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
DR GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0043407; P:negative regulation of MAP kinase activity; ISS:UniProtKB.
DR GO; GO:0051898; P:negative regulation of protein kinase B signaling; ISS:UniProtKB.
DR GO; GO:0050860; P:negative regulation of T cell receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0045785; P:positive regulation of cell adhesion; ISS:UniProtKB.
DR GO; GO:0051894; P:positive regulation of focal adhesion assembly; ISS:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR CDD; cd00063; FN3; 8.
DR Gene3D; 2.60.40.10; -; 8.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000242; PTP_cat.
DR InterPro; IPR041201; PTPRJ_TM.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR Pfam; PF00041; fn3; 6.
DR Pfam; PF18861; PTP_tm; 1.
DR Pfam; PF00102; Y_phosphatase; 1.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00060; FN3; 9.
DR SMART; SM00194; PTPc; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF49265; SSF49265; 6.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS50853; FN3; 9.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE 2: Evidence at transcript level;
KW Cell junction; Cell membrane; Cell projection; Glycoprotein; Hydrolase;
KW Membrane; Protein phosphatase; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..1406
FT /note="Receptor-type tyrosine-protein phosphatase eta"
FT /id="PRO_5000065173"
FT TOPO_DOM 25..1044
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1045..1065
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1066..1406
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 82..170
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 171..259
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 260..343
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 346..437
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 438..523
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 524..614
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 615..703
FT /note="Fibronectin type-III 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 704..793
FT /note="Fibronectin type-III 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 794..888
FT /note="Fibronectin type-III 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 887..979
FT /note="Fibronectin type-III 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1110..1367
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 39..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1308
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160,
FT ECO:0000255|PROSITE-ProRule:PRU10044"
FT BINDING 1274
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1308..1314
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1352
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 36
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 281
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 302
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 331
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 332
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 364
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 385
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 391
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 453
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 459
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 484
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 500
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 510
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 547
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 568
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 630
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 636
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 651
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 657
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 719
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 745
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 750
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 766
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 776
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 804
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 828
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1010
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1406 AA; 154214 MW; 2D609885CC0F367B CRC64;
MRRLPLLPPC PLLLLLLLPA EVRCTTACTD DCSLKNVTEE MGTSSNDELS VNATSGNRRL
SEDVSLPGRA MSDQNSVAQP RAVLDLKTEY VGVTSVNLTW TVNDTASDSY TYRIEVRNGS
SINNKTSDIT DAEITGLIPG TLYTFTVFAV AADGQTAGEG ASISLYTKPS PVLDLKAEYV
GVTSVNLTWT VNDTASASYT YRIEVTSDSS IDSLTSSVTM AEITGLIPGT LYSFKVFAVA
ADNRTEADGA SISLYTKPSP VLDLKAEYVG VTSVNLTWTV NGTALTAYTY RIEVRNATSI
RNETSNINKI EITGLIPGTS YNFKVFATPV NNTTEEEGLS LNLYTKPSPV LRVVTEYVGV
TSVNLTWMVD DTASDSYTYR IEVRNGSSIN NKTSDITDAE ITGLIPGTLY TFTVFAVAAD
GQTAGEGASI SLYTKPSPVL DLKAEYVGVT SVNLTWTVND TASASYTYRI EVTSDSSIDS
LTSNVTMAEI TGLIPGTLYN FTVFAVAADN RTEADGAFTS LYTKPTPVTD LKAEHGVTSV
SLNWMVNDTA SDSYTYRIEV RNGHSVNNKT SNIPETEITG LNPGTLYTFT VFAVAADGET
EGEGASISVY TKPRAVLHLK TEYVGVTSVN LTWTVNDTDS ASYTYRIEVR NGSSINNKTS
DITDAEITGL DPGTLYIFTV FAVAADGQTA GEGASISLYT KPSMVLNLKA EYVTMTSVNL
TWMVNDAESA SYTYRIEVAH ESLINETMSN VTKSIVTYLI PGTSYNFTVF AIAADNQTEG
EGASISQNTV PSSVNAFQCE AVANMSYLTL KWNCPYGGYS GFDIEIFNGT WTKKQQSQFC
GREGSEEIFK TEPLDYYKTY TVSVTTVSDG LTSLPVQKIC KTSITDPPVP NKAPLVKAVS
HNSLSVEFPD FESVNGPLKA YAVMIVTEAE GCLPSKSDLD YTYNDFKQKM TATYVTYVID
VEEISSSSHS QNGHNIVDVG KGNTMYGYEN GPLIPLHSYR ASVAGFTNIN FTVANKIMGE
QSYVSFSPCS EVVSLPQDPG VIAGAVIGCL LAILAVVAIG GYIFWRRRRK DKRNTEVSFS
PIKIKKSKMI KVENFESYFK KQQADSNCGF AEEYEELKSA GVHQPKFAAE IAENRGKNRY
NNVLPYDISR VKLSNPSCTT DDYINANYMP GYSSKKAFIA AQGPLPNTIE DFWRMIWEKN
IYSIVMLTKC VEQARTKCEQ YWPDKQSKSY GDIIVTMVSE VVLPEWTIRD FNVENADTME
SHTVRQFHFT SWPDHGVPET TDLLINFRHL VHEYSSQNPI DSPILVHCSA GVGRTGTFIA
IDRLIQQIEM ENTVDVYGVV YDLRMHRPLM VQTEDQYVFL NQCVMDIIRS QKEKKTDLIY
QNTTAMAIYE NFTPGPAFGK ANGYHA
