PTP4_CAEEL
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 03-AUG-2022, entry version 146.
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; -.
DR EPD; P28192; -.
DR PaxDb; P28192; -.
DR PRIDE; P28192; -.
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 CTD; 177898; -.
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; QYIFCHE; -.
DR OrthoDB; 411281at2759; -.
DR PhylomeDB; P28192; -.
DR Reactome; R-CEL-388844; Receptor-type tyrosine-protein phosphatases.
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 tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR CDD; cd00063; FN3; 3.
DR Gene3D; 2.60.40.10; -; 4.
DR Gene3D; 3.90.190.10; -; 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 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; SSF48726; SSF48726; 1.
DR SUPFAM; SSF49265; SSF49265; 2.
DR SUPFAM; SSF52799; SSF52799; 2.
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
