DUSP_VACCW
ID DUSP_VACCW Reviewed; 171 AA.
AC P07239; Q80HW5;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Dual specificity protein phosphatase H1;
DE EC=3.1.3.-;
DE EC=3.1.3.48;
DE AltName: Full=Late protein H1;
GN ORFNames=H1L;
OS Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain
OS WR)).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX NCBI_TaxID=10254;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3517852; DOI=10.1073/pnas.83.10.3141;
RA Broyles S.S., Moss B.;
RT "Homology between RNA polymerases of poxviruses, prokaryotes, and
RT eukaryotes: nucleotide sequence and transcriptional analysis of vaccinia
RT virus genes encoding 147-kDa and 22-kDa subunits.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:3141-3145(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3021979; DOI=10.1128/jvi.60.2.436-449.1986;
RA Rosel J.L., Earl P.L., Weir J.P., Moss B.;
RT "Conserved TAAATG sequence at the transcriptional and translational
RT initiation sites of vaccinia virus late genes deduced by structural and
RT functional analysis of the HindIII H genome fragment.";
RL J. Virol. 60:436-449(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Esposito J.J., Frace A.M., Sammons S.A., Olsen-Rasmussen M., Osborne J.,
RA Wohlhueter R.;
RT "Sequencing of the coding region of Vaccinia-WR to an average 9-fold
RT redundancy and an error rate of 0.16/10kb.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, ACTIVE SITE, AND MUTAGENESIS OF CYS-110.
RX PubMed=1848923; DOI=10.1038/350359a0;
RA Guan K., Broyels S.S., Dixon J.E.;
RT "A Tyr/Ser protein phosphatase encoded by vaccinia virus.";
RL Nature 350:359-362(1991).
RN [5]
RP FUNCTION, AND INTERACTION WITH A17.
RX PubMed=10438817; DOI=10.1128/jvi.73.9.7287-7296.1999;
RA Derrien M., Punjabi A., Khanna M., Grubisha O., Traktman P.;
RT "Tyrosine phosphorylation of A17 during vaccinia virus infection:
RT involvement of the H1 phosphatase and the F10 kinase.";
RL J. Virol. 73:7287-7296(1999).
RN [6]
RP FUNCTION.
RX PubMed=11238845; DOI=10.1128/jvi.75.7.3185-3196.2001;
RA Najarro P., Traktman P., Lewis J.A.;
RT "Vaccinia virus blocks gamma interferon signal transduction: viral VH1
RT phosphatase reverses Stat1 activation.";
RL J. Virol. 75:3185-3196(2001).
RN [7]
RP FUNCTION, AND INDUCTION.
RX PubMed=18593332; DOI=10.1089/jir.2007.0113;
RA Mann B.A., Huang J.H., Li P., Chang H.C., Slee R.B., O'Sullivan A.,
RA Anita M., Yeh N., Klemsz M.J., Brutkiewicz R.R., Blum J.S., Kaplan M.H.;
RT "Vaccinia virus blocks Stat1-dependent and Stat1-independent gene
RT expression induced by type I and type II interferons.";
RL J. Interferon Cytokine Res. 28:367-380(2008).
RN [8]
RP FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RX PubMed=21362620; DOI=10.1074/jbc.m111.226357;
RA Koksal A.C., Cingolani G.;
RT "Dimerization of Vaccinia virus VH1 is essential for dephosphorylation of
RT STAT1 at tyrosine 701.";
RL J. Biol. Chem. 286:14373-14382(2011).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.32 ANGSTROMS).
RX PubMed=19211553; DOI=10.1074/jbc.m808362200;
RA Koksal A.C., Nardozzi J.D., Cingolani G.;
RT "Dimeric quaternary structure of the prototypical dual specificity
RT phosphatase VH1.";
RL J. Biol. Chem. 284:10129-10137(2009).
CC -!- FUNCTION: Serine/Tyrosine phosphatase which down-regulates cellular
CC antiviral response by dephosphorylating activated host STAT1 and
CC blocking interferon (IFN)-stimulated innate immune responses.
CC Dephosphorylates the A17 protein. {ECO:0000269|PubMed:10438817,
CC ECO:0000269|PubMed:11238845, ECO:0000269|PubMed:1848923,
CC ECO:0000269|PubMed:18593332, ECO:0000269|PubMed:21362620}.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=87 uM for 3-O-methylfluorescein phosphate
CC {ECO:0000269|PubMed:21362620};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:21362620}.
CC -!- INTERACTION:
CC P07239; P42224: STAT1; Xeno; NbExp=2; IntAct=EBI-7789600, EBI-1057697;
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:21362620}. Host
CC cytoplasm {ECO:0000269|PubMed:21362620}. Note=Approximately 200
CC molecules of H1 are packaged within the virion and are essential for
CC the viability of the virus.
CC -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC {ECO:0000269|PubMed:18593332}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class dual specificity subfamily. {ECO:0000305}.
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DR EMBL; M13209; AAB59836.1; -; Genomic_DNA.
DR EMBL; AY243312; AAO89378.1; -; Genomic_DNA.
DR PIR; A24481; QQVZH1.
DR PDB; 2Q05; X-ray; 2.57 A; A/B/C/D=1-171.
DR PDB; 2RF6; X-ray; 1.95 A; A=1-171.
DR PDB; 3CM3; X-ray; 1.32 A; A=1-171.
DR PDBsum; 2Q05; -.
DR PDBsum; 2RF6; -.
DR PDBsum; 3CM3; -.
DR SMR; P07239; -.
DR IntAct; P07239; 1.
DR MINT; P07239; -.
DR SABIO-RK; P07239; -.
DR EvolutionaryTrace; P07239; -.
DR Proteomes; UP000000344; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:RHEA.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR GO; GO:0039563; P:suppression by virus of host JAK-STAT cascade via inhibition of STAT1 activity; IEA:UniProtKB-KW.
DR GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR Pfam; PF00782; DSPc; 1.
DR SMART; SM00195; DSPc; 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; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Host cytoplasm; Host-virus interaction; Hydrolase;
KW Inhibition of host innate immune response by virus;
KW Inhibition of host interferon signaling pathway by virus;
KW Inhibition of host STAT1 by virus; Late protein; Protein phosphatase;
KW Reference proteome; Viral immunoevasion; Virion.
FT CHAIN 1..171
FT /note="Dual specificity protein phosphatase H1"
FT /id="PRO_0000094868"
FT DOMAIN 23..171
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 1..27
FT /note="Dimerization"
FT ACT_SITE 110
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160,
FT ECO:0000269|PubMed:1848923"
FT MUTAGEN 110
FT /note="C->S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:1848923"
FT CONFLICT 20
FT /note="K -> R (in Ref. 3; AAO89378)"
FT /evidence="ECO:0000305"
FT HELIX 6..14
FT /evidence="ECO:0007829|PDB:3CM3"
FT STRAND 31..37
FT /evidence="ECO:0007829|PDB:3CM3"
FT HELIX 39..43
FT /evidence="ECO:0007829|PDB:3CM3"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:3CM3"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:3CM3"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:3CM3"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:3CM3"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:3CM3"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:3CM3"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:3CM3"
FT HELIX 89..102
FT /evidence="ECO:0007829|PDB:3CM3"
FT STRAND 106..109
FT /evidence="ECO:0007829|PDB:3CM3"
FT STRAND 111..115
FT /evidence="ECO:0007829|PDB:3CM3"
FT HELIX 116..128
FT /evidence="ECO:0007829|PDB:3CM3"
FT HELIX 134..149
FT /evidence="ECO:0007829|PDB:3CM3"
FT HELIX 156..166
FT /evidence="ECO:0007829|PDB:3CM3"
SQ SEQUENCE 171 AA; 19698 MW; 65DE6E875C7AD47E CRC64;
MDKKSLYKYL LLRSTGDMHK AKSPTIMTRV TNNVYLGNYK NAMDAPSSEV KFKYVLNLTM
DKYTLPNSNI NIIHIPLVDD TTTDISKYFD DVTAFLSKCD QRNEPVLVHC AAGVNRSGAM
ILAYLMSKNK ESLPMLYFLY VYHSMRDLRG AFVENPSFKR QIIEKYVIDK N
