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Database: UniProt
Entry: A0A2A4JFD6_HELVI
LinkDB: A0A2A4JFD6_HELVI
Original site: A0A2A4JFD6_HELVI 
ID   A0A2A4JFD6_HELVI        Unreviewed;      1619 AA.
AC   A0A2A4JFD6;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE            EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN   ORFNames=B5V51_2598 {ECO:0000313|EMBL:PCG70777.1};
OS   Heliothis virescens (Tobacco budworm moth).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC   Noctuidae; Heliothinae; Heliothis.
OX   NCBI_TaxID=7102 {ECO:0000313|EMBL:PCG70777.1, ECO:0000313|Proteomes:UP000218220};
RN   [1] {ECO:0000313|EMBL:PCG70777.1, ECO:0000313|Proteomes:UP000218220}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HvINT- {ECO:0000313|EMBL:PCG70777.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:PCG70777.1};
RA   Fritz M.L., Deyonke A.M., Papanicolaou A., Micinski S., Westbrook J.,
RA   Gould F.;
RT   "Contemporary evolution of a Lepidopteran species, Heliothis virescens, in
RT   response to modern agricultural practices.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PCG70777.1}.
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DR   EMBL; NWSH01001588; PCG70777.1; -; Genomic_DNA.
DR   STRING; 7102.A0A2A4JFD6; -.
DR   Proteomes; UP000218220; Unassembled WGS sequence.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009653; P:anatomical structure morphogenesis; IEA:UniProt.
DR   GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   GO; GO:0048666; P:neuron development; IEA:UniProt.
DR   CDD; cd00063; FN3; 2.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 2.
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; 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:SF449; RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE GAMMA; 1.
DR   Pfam; PF00102; Y_phosphatase; 2.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00060; FN3; 2.
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; 1.
DR   PROSITE; PS50853; FN3; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW   Reference proteome {ECO:0000313|Proteomes:UP000218220};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..1619
FT                   /note="protein-tyrosine-phosphatase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012856441"
FT   DOMAIN          321..430
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          567..950
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          871..941
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   DOMAIN          1125..1309
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   REGION          76..115
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          664..685
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          985..1070
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1259..1306
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1339..1394
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        77..96
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        990..1033
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1034..1057
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1278..1292
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1339..1365
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1619 AA;  180699 MW;  F95AD09CDB4B449E CRC64;
     MYIHYTVGAI FIVFILCVHC DNVANDNEIK EIYVPSAPQN LTANNVTTDE VHLSWAPPLT
     FTLRTLPNTN LDLKSQTLVP DHDKSTSNKK LEPQGDEPVN DVLSQDLPSD TITPERQKDF
     EYTSYNWYKN DKHKYNDDYS SHVLIDDYRN KRDVRTHRHR KRWPENDTDT KLHFEKNLEV
     LEAHPVEQKE VVKKSFTQAK HKETTQVAYV LYYEQGVPRY DVNIVNGTQN SADVKRKNVF
     PSDLGMEDYS RATKNLTLLN TSGKVTKVVG FRLRNLKPFT PYKIWVRAFY NFSLDGVKSS
     DLLDRLGPKS DPLYVLTDVR PPSAPIILNL TCDQTKRTLY LQWRQPLEYN NSLDQYVVTL
     RKIPEQQPRT RLTLPTNKND IETTIPIEVD LWNVTRYEVK VYAVTQSVAR EKSFINGEES
     NPEEVSSEWC AAHSEAMSPR DVPESDGVSN AALLAVCPLL VFAVAVAVLY WRCRARLSKC
     ISAAYNYLEE GGERAVRAPL NSYKKPVVNC SPLVSCTSGA AAEGGAGDAC GEAARPPRMA
     GAAQPAVPAL AFPAHVAALH ADGDIGFSKE YEIVVAKSAA LGHTSHHSHR PENRLKNRYL
     NITAYDHSRV CVSAGTRCGA AGCVGGGGGG GGRSAACDYV NANFIDGMLP QLQPHHVARI
     RRKLERRNRP HRQSSVKPTK PPPNLAEGIE SAFLNIEFSG IVESDEQNSD SDSDRSDSDS
     DLDDVYVDIE GVSTRVKLEW LVWRRRYIAT QGPTPATLDA FWRMIWQHRV HTVVMITNLV
     ERGRRKCDMY WPAGGAGSSA EFGGVRVTLL HEDVRAAYTV RHMRVQYCRT DAAGGSTPTS
     GDSSTSGTEG RTVVQYHYTV WPDHGTPRHP LAVLPFVKAA GKHSSTVLVH CSAGVGRTGT
     YIVLDAQLNQ LKLTGTLSPL GFLCRARTQR NHLVQTEEQY VFVHDALLEH VRSGDTEVEF
     PKARQYLAKL LEPISDEELA VLDLNPPKHK SMNDLSNGVE NGETSSIKSS QNASEKEVLE
     NGSQMSIKTD DLNSEQSKSV KDSEGTDEPK EGMVNGEENE GVYDLAPRST DTYSKKMQAY
     NNMTDTEKEE MRRANRAENY ALLERMRSLA NRHHTYQGPP PVNLLEKQFL LITRSCVEAS
     VCARAPHNAE KNRPGGILPS DSARVMLVPK PGVEGSEYVN ASWVCGRRRV REYAVAQHPA
     TGADLWRLLW DHTAQLVLLL SDTSDPECEI FWPTEEEKEL FVANFRASFV SKETYVAHRK
     VDRKTPAESP VEPETNGYRR QESSDCADDE RLIPENGSPV ADTEPAYRFD RTELRLERLS
     AGNRDLSARK SIANGDLFSS LSEKKNGPKS PRSPSKMSLK NFKLSSPTKF KFPDWGNRTA
     GSPPDTAPPP PPVAPALSVE EEAELRRPCY YFEKVEKVPE DVPLDRVIEV TNVSVHSLQD
     DYQLSVKFIK CSRWLDGETT DYVQGRPDDN EFVRAVRHAA GDSEREQAID RLIEPYKDSF
     ALVEYVAGCQ MEYKNGPVVV VDKYGGWKAM NFCTMSAACG GARAVSAHDP GAAYRAPHDA
     RASLYCWAAL GAHARTAPDH ARAHHHAALL AAYCALASYG DLLTHTNQRF PETPEQESR
//
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