ID   PTP4_CAEEL              Reviewed;        1159 AA.
AC   P28192; D3YT39; Q21214;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 3.
DT   27-MAR-2024, entry version 154.
DE   RecName: Full=Tyrosine-protein phosphatase 4;
DE            EC=3.1.3.48;
DE   AltName: Full=Protein-tyrosine phosphatase 4;
DE   Flags: Precursor;
GN   Name=ptp-4; ORFNames=K04D7.4;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 735-842.
RX   PubMed=1704870; DOI=10.1007/bf00211693;
RA   Matthews R.J., Flores E., Thomas M.L.;
RT   "Protein tyrosine phosphatase domains from the protochordate Styela
RT   plicata.";
RL   Immunogenetics 33:33-41(1991).
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 {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=a;
CC         IsoId=P28192-1; Sequence=Displayed;
CC       Name=b;
CC         IsoId=P28192-2; Sequence=VSP_047522;
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       Receptor class subfamily. {ECO:0000305}.
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DR   EMBL; Z69664; CAA93513.2; -; Genomic_DNA.
DR   EMBL; Z69664; CBK19459.1; -; Genomic_DNA.
DR   EMBL; M38014; AAA28128.1; -; mRNA.
DR   PIR; T23308; T23308.
DR   RefSeq; NP_001255470.1; NM_001268541.1. [P28192-1]
DR   RefSeq; NP_001255471.1; NM_001268542.1. [P28192-2]
DR   AlphaFoldDB; P28192; -.
DR   SMR; P28192; -.
DR   STRING; 6239.K04D7.4a.1; -.
DR   GlyCosmos; P28192; 9 sites, No reported glycans.
DR   EPD; P28192; -.
DR   PaxDb; 6239-K04D7-4a; -.
DR   EnsemblMetazoa; K04D7.4a.1; K04D7.4a.1; WBGene00010558. [P28192-1]
DR   EnsemblMetazoa; K04D7.4b.1; K04D7.4b.1; WBGene00010558. [P28192-2]
DR   GeneID; 177898; -.
DR   KEGG; cel:CELE_K04D7.4; -.
DR   UCSC; F59G1.5.1; c. elegans. [P28192-1]
DR   AGR; WB:WBGene00010558; -.
DR   WormBase; K04D7.4a; CE40655; WBGene00010558; ptp-4. [P28192-1]
DR   WormBase; K04D7.4b; CE44709; WBGene00010558; ptp-4. [P28192-2]
DR   eggNOG; KOG4228; Eukaryota.
DR   GeneTree; ENSGT00940000166600; -.
DR   InParanoid; P28192; -.
DR   OMA; FSDFWSM; -.
DR   OrthoDB; 2903434at2759; -.
DR   PhylomeDB; P28192; -.
DR   SignaLink; P28192; -.
DR   PRO; PR:P28192; -.
DR   Proteomes; UP000001940; Chromosome IV.
DR   Bgee; WBGene00010558; Expressed in pharyngeal muscle cell (C elegans) and 3 other cell types or tissues.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   CDD; cd00063; FN3; 3.
DR   CDD; cd00096; Ig; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 4.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
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; 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; PTHR46957; CYTOKINE RECEPTOR; 1.
DR   PANTHER; PTHR46957:SF3; PROTEIN-TYROSINE-PHOSPHATASE; 1.
DR   Pfam; PF00041; fn3; 3.
DR   Pfam; PF00102; Y_phosphatase; 1.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00060; FN3; 3.
DR   SMART; SM00194; PTPc; 1.
DR   SMART; SM00404; PTPc_motif; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 2.
DR   SUPFAM; SSF49265; Fibronectin type III; 2.
DR   SUPFAM; SSF48726; Immunoglobulin; 1.
DR   PROSITE; PS50853; FN3; 4.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Disulfide bond; Glycoprotein; Hydrolase; Membrane;
KW   Protein phosphatase; Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..1159
FT                   /note="Tyrosine-protein phosphatase 4"
FT                   /id="PRO_0000094884"
FT   TOPO_DOM        22..564
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        565..585
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        586..1159
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          22..135
FT                   /note="Ig-like C2-type"
FT   DOMAIN          142..235
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          240..335
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          337..438
FT                   /note="Fibronectin type-III 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          439..538
FT                   /note="Fibronectin type-III 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          643..903
FT                   /note="Tyrosine-protein phosphatase 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   DOMAIN          888..1153
FT                   /note="Tyrosine-protein phosphatase 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   REGION          656..677
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        844
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160,
FT                   ECO:0000255|PROSITE-ProRule:PRU10044"
FT   CARBOHYD        28
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        153
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        194
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        248
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        279
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        362
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        480
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        488
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        519
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        36..115
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   VAR_SEQ         1..46
FT                   /note="Missing (in isoform b)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_047522"
FT   CONFLICT        836
FT                   /note="S -> T (in Ref. 2; AAA28128)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1159 AA;  131423 MW;  0F6EEEF312799E16 CRC64;
     MPRKHFIFLI FLFWKFDSAE SISVTSKNAT EALLRCPPAE NFIRTHMAPD FETPRLVRRL
     DWFQDDSLVA SYQQDILADS SRQWWVSDGR YQLIRPFYTL RVSPVTPEDS GTYRCRLETD
     PLFSSPQSTA TQELAVMVKP VAPSSPEIKT FTNRSITLVW THNAARAHRP ILRFSVSVRT
     VSDNTRFVMA APSNATTVIV DNLSPYTLYA FSVRAENSAG SSDFGPETTF RTLGESPNRP
     PQIQKIRNIT SECVEVTITP PDEMNGELDK YLVLIQAVNE TIPRKMTFDK PTSTPLTICA
     LSPSTDYALA IEADNGFGTS PQATLVFHTE DSVPNWSPST ITTLPVVGKP EITVLWPAPP
     LNATEKVIKY HLYYKAKNED QWKIEHLNVS PNGVKSKLFK YRLVDLNPNT QYRIRVSAST
     IKGEGAQSAD SVAQTDVGEP GTVTFKDLNF DCKNGVKLRW NYEPSVNSKK SPTFTVKVTN
     QTTSLQFNTT MLSLDIIDLS LYDEYTLRII VLERSTIDNS TILIGKYSDS HQFILKDKCS
     YQSSFCSPGE KCAKLTSSAG NPRYISVLIV IFAIIIFAFI CFVIVHFARG SMNFKHLLKK
     KEKCVYLEEI SPLVYDSAGQ EDIPVELFYG YVEDLNRNDS LKFKTQFQIL ESQTSGIDSV
     DSGESNSSSD ENSQKNRYNN IGAIEATRIR LNSPTGNDYI NANYVDSCNE RNAYIATQAP
     LPSTFSDFWS MIWQERSNII VCITNMVEDG KRKCDQYWPS QQDSPQTFGN YQVTLVSEST
     NAHFSHRILD LKIAKAVPAV ERKVHQLHFM GWPDHGVPSS VFPLLSFVHY TSDIHSTGPV
     VVHCSAGVGR SGSYILVDSM RRHLISFRRL NVQGHLTHMR RQRAKLVQTL EQYIFCHEAI
     RQLIRHGITR VHSDLFMRYL HYLSEENLNG KTRMQLQFED ICDCKHQPRC LIESDVITLP
     GYHRSDEFMV GSWGNECEDL WRLTWQQKVQ TIVILNQRDS FWRKLPSCIY DGEIQLQHGD
     NFVLLQKDDQ QLCVRIVNVS RADLDTDFWR EIENVQKQRI TYHDAPLLIL AHKYPPSVPS
     PTDSTSTLSL SILFNDDTAL AFSICAATTL ACQLETTGCV DVVQVLSSYT EIQCGIFASK
     QEIEIIYEKM SQLVGGTRV
//