ID L8E7X5_CAEEL Unreviewed; 2224 AA.
AC L8E7X5;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN Name=ptp-3 {ECO:0000313|EMBL:CCQ25649.1,
GN ECO:0000313|WormBase:C09D8.1i};
GN ORFNames=C09D8.1 {ECO:0000313|WormBase:C09D8.1i}, CELE_C09D8.1
GN {ECO:0000313|EMBL:CCQ25649.1};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000313|EMBL:CCQ25649.1, ECO:0000313|Proteomes:UP000001940};
RN [1] {ECO:0000313|EMBL:CCQ25649.1, ECO:0000313|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000313|EMBL:CCQ25649.1,
RC ECO:0000313|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RA Sulson J.E., Waterston R.;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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;
CC Evidence={ECO:0000256|ARBA:ARBA00001490};
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Receptor class 2A subfamily. {ECO:0000256|ARBA:ARBA00010504}.
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DR EMBL; BX284602; CCQ25649.1; -; Genomic_DNA.
DR RefSeq; NP_001263672.1; NM_001276743.1.
DR SMR; L8E7X5; -.
DR EnsemblMetazoa; C09D8.1i.1; C09D8.1i.1; WBGene00004215.
DR GeneID; 174685; -.
DR AGR; WB:WBGene00004215; -.
DR WormBase; C09D8.1i; CE48125; WBGene00004215; ptp-3.
DR HOGENOM; CLU_001645_4_2_1; -.
DR OrthoDB; 2875525at2759; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00004215; Expressed in pharyngeal muscle cell (C elegans) and 4 other cell types or tissues.
DR ExpressionAtlas; L8E7X5; baseline and differential.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR CDD; cd00063; FN3; 8.
DR CDD; cd14553; R-PTPc-LAR-1; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 11.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 2.
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; IPR003598; Ig_sub2.
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:SF7; PROTEIN-TYROSINE-PHOSPHATASE; 1.
DR Pfam; PF00041; fn3; 6.
DR Pfam; PF07679; I-set; 2.
DR Pfam; PF00102; Y_phosphatase; 2.
DR PRINTS; PR00014; FNTYPEIII.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00060; FN3; 9.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 3.
DR SMART; SM00194; PTPc; 2.
DR SMART; SM00404; PTPc_motif; 2.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 2.
DR SUPFAM; SSF49265; Fibronectin type III; 5.
DR SUPFAM; SSF48726; Immunoglobulin; 3.
DR PROSITE; PS50853; FN3; 9.
DR PROSITE; PS50835; IG_LIKE; 3.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 2.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2.
PE 1: Evidence at protein level;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Proteomics identification {ECO:0007829|EPD:L8E7X5,
KW ECO:0007829|PeptideAtlas:L8E7X5};
KW Reference proteome {ECO:0000313|Proteomes:UP000001940};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..2224
FT /note="protein-tyrosine-phosphatase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003987817"
FT DOMAIN 91..183
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 195..284
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 294..378
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 385..478
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 483..579
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 583..672
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 677..792
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 796..900
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 901..1000
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1001..1097
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1102..1203
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1205..1311
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1671..1926
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1846..1917
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT DOMAIN 1957..2216
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 2131..2207
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 40..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1379..1416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..56
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1390..1416
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2224 AA; 249121 MW; B770541E162AFAB8 CRC64;
MNRIARHLRN VARRKGSSLL LFLMLSTVLV AAKEDGKLGE EDEDFGWNDE EPPDNQDVQD
GGIPLVRKEE FTNNQLYAEA YQSYIQALAY PARLVVRPDS STVVDESKIS FFCRADGNPL
PSVIWRVNGK SITDHNRISI KSLATGLSTL RFERVSLDDN ATVVSCSADN GVANPVVAEA
SLTVVPRDKV PIGFPQIELH PSLKSVEQGK TAYVSCRVRG DPRAKVLWLR DLIPLDIRAD
GRYSVSTIGN PGALMIQHAR EEDQGKYECI ARNTLGVAHS KAANLYVKVR RVPPYFSYKL
ERQYVVGVGG NINLTCVAVG YPMPRVFWKK TDLMVLDDPS TAPIGKNVLT LTHVESTENF
TCVAVSALGN IEATTTVIAK ELPPPPVNIV VSSVTSESVV ITWKPPKYNE AINKYVVNYR
LKYSEGRSSR GKTMETLENS LVIDGLVAFQ TYEFTVRSAG PVGVGLESLP VEAQTKPSKP
ATAPVSPQAR SLNRDSILVK WGPCEQPNGL ITGYKVYYTN DLVTTPIREW KQHDAKSDEF
MTTINGLEPD SRYFVRVIAQ NSEGDSPLST LVTVATRQGI PGQPPMLTVK ALDSRRMQLT
WDKPLYSSPV VGYTVRYNTS DGEKELTLTS PHEKHVVTGL HPDKYYYFRV AAYSDRGQGE
FTEPMISKTI ASIPLSSPTI VSAAATSSKS VEIRWKGPEQ KKLNGVLTAY RINYFRLEDS
KTANLESVEY DEDMDDSSSF LDRMSVVVPS DATSYVLSDL LPYSSYEITV AASTMDGYGP
ESSIRVVKTL EDVPSAPRNF NAELTSATSV KLTWDAPAAA NGALLGYYVY LDRMVNGEPV
VEKGSKKRIV MIRDSSKRYF ELDSLDPNTE YSFRLNAFNR NGDGEFSERK SIITQGIPPE
APEIVSVSLD RDEPPVVARI EWKMPKMKPN ETPIEKYNLW LRAQGYPDSY VKAKTVDGTD
LSTTISGLWM GVVYDVLLAA ENREGRSQNA TETIATPVGS PDGEPIDVQY EVMKGKIVVS
WRPPSEEKRN GNITSYKAIL SAMDATADRY EQPVPAPSTS STFEVNVRRA YLFKVAAATM
KGIGPYSPVL TINPDPAALV GPPTNVRVEA TSNSTAVVQW DFESQKADSF VVKYMHEPGN
RMDTEKWKQL PVVSIDKENP KRFAVVSDLN AHKPYAFCVL AVKNNRQGPC SDPPTVLESV
TPTYMVQNLR VLWKTSNSVQ LTWEYNGPRN VGFYVNHTGR KDYVNHELQE KTMSTPGFGQ
DVDEKHREYL WTNLRPHMMY TIHVGVRTLP PGARKYWPQE VVTITDPTGP PFVDVPKLVD
SSGTQPGQQM IRLTPATEEY GPISHYWIIL VPANYSTEDV VNLDPIELEK ATAEKRAQLA
RSLSVSPSKK LKRKASEVGD DSQSASYHPK EKRARRATVP GAYVTARLSA DRVKQQYRNN
QPFIVGDSQL YDGFTNYPLE HNLHYRLMMR AFAKNDVRTK DSFEQRAPMS EKLSRMYSDS
VLTEPFTIKS ALRGASQKSS PWVGACIAFL VLFSIVGMLI CWWLRCNKKS AGRHPRHGSI
TKVALTGNIM NGGGGIPGET SKLLSTSNEY GRQIMNPYEQ MNGNHHMESS MDLYPLPTSH
SRSNGYAPVP VAIPSLPNNG NNMTTVSHPA VPIAELANHI ERLRMNNNAG FQSEFESIET
GQHFTWEHSS ADMNKHKNRY ANVAAYDHSR VVLSNVEGYP GMDYINANYV DGYDKPRSYI
ATQGPLPETF SDFWRMVWEE QSVTIVMLTN LEERSRVKCD QYWPSRGTAT YGDIEVTLLE
SVHLAHYTMR TMRLKMVGEP EVREIKHLQY TAWPDHGVPD HPTPFLIFLK RVKTLNPNDA
GPIISHCSAG IGRTGAFIVI DCMLERLRYD NTVDIYGCVT ALRAQRSYMV QTEEQYIFIH
DAVLDAVNSG STEVPASRLH QHLHILSQPS ADQLSGIDME FRHLTTLKWT SNRCTVANLP
VNRPKNRMLS AVPYDSNRVI MRLLPGADGS DYINASWIDG YKERGAYIAT QAPTNETAAD
FWRAIWEHNS PIIAMLVRTN ERGQEQCSDY WPLETGVQVG MLVVEPMAEY DMKHYHLREF
RISDINTREV RTVRQFHFME WPDVGKPHTA DHFLDFVTQV HNTYAQFGCT GPITVHCCSG
AGRTAVFIAL SIILDRMRAE HVVDVFTTVK LLRTERQNMI QEPEQYHFLY LAAYEYLAAY
DNFS
//
