ID   PTPH2_MDBVW             Reviewed;         325 AA.
AC   Q5I146;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Tyrosine phosphatase H2;
DE            Short=PTP-H2;
DE            EC=3.1.3.48;
GN   Name=H2;
OS   Microplitis demolitor bracovirus (isolate Webb) (MdBV).
OC   Viruses; Polydnaviridae; Bracovirus.
OX   NCBI_TaxID=654919;
OH   NCBI_TaxID=69319; Microplitis demolitor.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=16380146; DOI=10.1016/j.virol.2005.11.010;
RA   Webb B.A., Strand M.R., Dickey S.E., Beck M.H., Hilgarth R.S., Barney W.E.,
RA   Kadash K., Kroemer J.A., Lindstrom K.G., Rattanadechakul W., Shelby K.S.,
RA   Thoetkiattikul H., Turnbull M.W., Witherell R.A.;
RT   "Polydnavirus genomes reflect their dual roles as mutualists and
RT   pathogens.";
RL   Virology 347:160-174(2006).
RN   [2]
RP   FUNCTION.
RX   PubMed=17121799; DOI=10.1128/jvi.02189-06;
RA   Pruijssers A.J., Strand M.R.;
RT   "PTP-H2 and PTP-H3 from Microplitis demolitor Bracovirus localize to focal
RT   adhesions and are antiphagocytic in insect immune cells.";
RL   J. Virol. 81:1209-1219(2007).
RN   [3]
RP   FUNCTION.
RX   PubMed=18474557; DOI=10.1099/vir.0.2008/000307-0;
RA   Suderman R.J., Pruijssers A.J., Strand M.R.;
RT   "Protein tyrosine phosphatase-H2 from a polydnavirus induces apoptosis of
RT   insect cells.";
RL   J. Gen. Virol. 89:1411-1420(2008).
RN   [4]
RP   SUBCELLULAR LOCATION.
RX   PubMed=20691785; DOI=10.1016/j.ibmb.2010.07.003;
RA   Eum J.H., Bottjen R.C., Pruijssers A.J., Clark K.D., Strand M.R.;
RT   "Characterization and kinetic analysis of protein tyrosine phosphatase-H2
RT   from Microplitis demolitor bracovirus.";
RL   Insect Biochem. Mol. Biol. 40:690-698(2010).
CC   -!- FUNCTION: Suppresses host immune cell adhesion and phagocytosis.
CC       Triggers host mitochondrial membrane depolarization and caspase-
CC       dependent apoptosis. {ECO:0000269|PubMed:17121799,
CC       ECO:0000269|PubMed:18474557}.
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: Host cytoplasm {ECO:0000269|PubMed:20691785}.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       {ECO:0000305}.
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DR   EMBL; AY875685; AAW51786.1; -; Genomic_DNA.
DR   RefSeq; YP_239382.1; NC_007035.1.
DR   SMR; Q5I146; -.
DR   GeneID; 5075819; -.
DR   KEGG; vg:5075819; -.
DR   Proteomes; UP000008168; Genome.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0039651; P:induction by virus of host cysteine-type endopeptidase activity involved in apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR   GO; GO:0039503; P:suppression by virus of host innate immune response; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.190.10; -; 1.
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; PF00102; Y_phosphatase; 1.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00194; PTPc; 1.
DR   SMART; SM00404; PTPc_motif; 1.
DR   SUPFAM; SSF52799; SSF52799; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE   3: Inferred from homology;
KW   Activation of host caspases by virus; Host cytoplasm;
KW   Host-virus interaction; Hydrolase;
KW   Inhibition of host innate immune response by virus;
KW   Modulation of host cell apoptosis by virus; Protein phosphatase;
KW   Reference proteome; Viral immunoevasion.
FT   CHAIN           1..325
FT                   /note="Tyrosine phosphatase H2"
FT                   /id="PRO_0000405352"
FT   DOMAIN          27..295
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   ACT_SITE        236
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160,
FT                   ECO:0000255|PROSITE-ProRule:PRU10044"
SQ   SEQUENCE   325 AA;  37876 MW;  D83B669F822005CF CRC64;
     MSRCKFRSLN YSEFLNLVEK SDFEEVVTRE HEKIMAQKVD GTFNESMKLE NRKLNRYLDM
     LCFDHTRVTL PAEKNRGDYI NANYVDGYEY KKKFICTQAP LQQTAYDFWR TVWMHHTRII
     VMMCKKKENR KQCFAYWNDI EGGDIVFGKF KITTTQIETH LSYIETTLLV TDGTSAIQEV
     THFVFTQWPD YGVPNDVMNL LNFILTVKSA QKDVIRQLAQ ERFKIGDNPP PIVVHCSAGV
     GRTGAYCLLD SAISEFDACA TISIPSTLIN IRNQRYYCIF ILPQYFFCYR VMERYVNLTV
     NKVSKKLIAN VATALFNKVL HLKDN