ID A0A158Q6X5_9BILA Unreviewed; 1401 AA.
AC A0A158Q6X5;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
OS Elaeophora elaphi.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Elaeophora.
OX NCBI_TaxID=1147741 {ECO:0000313|Proteomes:UP000050640, ECO:0000313|WBParaSite:EEL_0000084401-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:EEL_0000084401-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
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};
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DR STRING; 1147741.A0A158Q6X5; -.
DR WBParaSite; EEL_0000084401-mRNA-1; EEL_0000084401-mRNA-1; EEL_0000084401.
DR Proteomes; UP000050640; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR CDD; cd00063; FN3; 2.
DR CDD; cd00047; PTPc; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
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; IPR003599; Ig_sub.
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; PTHR19134; RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE; 1.
DR PANTHER; PTHR19134:SF495; TYROSINE-PROTEIN PHOSPHATASE 69D; 1.
DR Pfam; PF00102; Y_phosphatase; 3.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00060; FN3; 2.
DR SMART; SM00409; IG; 1.
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; 2.
DR SUPFAM; SSF48726; Immunoglobulin; 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 2.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 652..677
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 42..152
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 203..293
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 723..1062
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 982..1053
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT DOMAIN 1127..1390
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1305..1381
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
SQ SEQUENCE 1401 AA; 160397 MW; EF88C47856A2FB13 CRC64;
MSMSDDYRDR YLLPEPACHM GICVCPPMFD PWRLEGAIEL LPFKCDRREL MVQGRALPSD
SVYQGTDASL FCCINMDPRS FIDDDGVDFI QNSSIIREPT NTPYDEVFTD GIEPPRCWSL
EIKNAQYSDS GTYLCHVKTT GKHEINTNYT INFFVKDQGN IPIREHSSSK LKFLDLLAER
RKVKEIEEKS HLVANFIVHL FIAPRIIQNV TVKTNATHAE IRWDAQDDGP MLKIDFKLVR
RTDGVEVWSD INAKSGVVIG ELLPATPYTL FISVLDGQNE PFKITEHFTT SESAPDPPTL
GEIRVLNLQG GLYCEVEWMP PKTPNGRITK YYVTVRGQIR HVSPGGILSN DDFPAEEKNQ
CSNYNNNDSS YTSADAIADF YSCRFGPLKP NRNYTAFVWA ENGAGRSENA TFSEQCITNF
AQPDAVDAPA SLSQNGTLFG LTFNSEPDEV NGPVACYYVA IVPLVPDVVI ESLPAPDSLI
VDTFLKTMSN NLQNEQLKQD AKQKRYFAYI AESYMQYPKK TLIGDGNTTA GVEPCNVLYL
SRHRPEDPAL KPGLKYTGFL IARVDRDHAT RGESFRHNDP FLMKRKRRRL HQNTERKFLD
RSRWFSYREN SELPRHFRSS RQLIVSGPAY GFSGYFKPVI LEAFDEQWAQ SWMTVLFSVL
SLVLFIILVS SFVTYILHRR GMIKQLCPMS KDRILLKPHF HATLVDDLPE EYSIRRRDSN
YLCISEFDAL PNYRSMESTA SERLENAHKN RYNDIKAFDA TRVKLPVIGN DPSTDYINAN
FVKGYKGRKM FIASQGPLDA STDDFWRMIW EHKVRVIVMV ANLYERNRCQ CAKYWPDDGP
KAYDKLEVRP VDSIYYSDYA IRNFEVRRIQ PTVANGSISG SPAIILYEVP SVTGDITADP
SAVIMNIKSR PSSVRGSIDS ILNEISSNSK RNSRCSTSNT QLNDVHAETE FVTKTPEVRH
VVQYHYTSWN DLQAPECTTG LLRFLSKLRK LDDYIRGPVV VHCSAGVGRT GTFIAIDSLL
DQCIEEGKAD VFGFVSEMRK QRNTMVQNAE QYLFIYKALA EWYMFGETDI EVSQFREHYR
ILSEPQFREQ QISTNRSAFI AVVKRPVSKL QHVNNDISNT EKISTAMEAE YERLERTLEP
RRMCNFAHKP ENARKNRFEN AVPFDHCRIV LPVVIGSVND STYINASLVK GYFYPYILAQ
DPLDEQTCYD FWCMIGEQNS RAVVMLSSES EFTPAEKYWP SEVGRIKTFG RDGEVSVKLI
GEELFPTFAL RKFTYKFAKE KTYREVVQYV YLCWPADKVL PESTESIIDL ISRVLSLQSD
HQEAGPIILH SRDGSFKTGL YCCVSLLLER LKAENRIDVF QTVRSLQQRR PLMFTKFEQY
AFCYKAVIDY LDTFNNKVTV D
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