DUSP_MYXVL
ID DUSP_MYXVL Reviewed; 178 AA.
AC Q85297; Q9Q8N1;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2002, sequence version 2.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Probable dual specificity protein phosphatase H1 homolog;
DE EC=3.1.3.-;
DE EC=3.1.3.48;
GN OrderedLocusNames=m069L; ORFNames=I1L;
OS Myxoma virus (strain Lausanne) (MYXV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Leporipoxvirus.
OX NCBI_TaxID=31530;
OH NCBI_TaxID=9986; Oryctolagus cuniculus (Rabbit).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION, AND MUTAGENESIS OF
RP CYS-110.
RX PubMed=7831813; DOI=10.1016/s0042-6822(95)80074-3;
RA Mossman K., Ostergaard H., Upton C., McFadden G.;
RT "Myxoma virus and Shope fibroma virus encode dual-specificity
RT tyrosine/serine phosphatases which are essential for virus viability.";
RL Virology 206:572-582(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10562494; DOI=10.1006/viro.1999.0001;
RA Cameron C., Hota-Mitchell S., Chen L., Barrett J.W., Cao J.-X.,
RA Macaulay C., Willer D.O., Evans D.H., McFadden G.;
RT "The complete DNA sequence of myxoma virus.";
RL Virology 264:298-318(1999).
CC -!- FUNCTION: Serine/Tyrosine phosphatase which down-regulates cellular
CC antiviral response by dephosphorylating activated STAT1 and blocking
CC interferon (IFN)-stimulated innate immune responses. {ECO:0000250}.
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 -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000250}. Host cytoplasm
CC {ECO:0000250}. Note=Approximately 200 molecules of H1 are packaged
CC within the virion and are essential for the viability of the virus.
CC {ECO:0000250}.
CC -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class dual specificity subfamily. {ECO:0000305}.
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DR EMBL; L31960; AAA66956.1; -; Genomic_DNA.
DR EMBL; AF170726; AAF14957.1; -; Genomic_DNA.
DR RefSeq; NP_051783.1; NC_001132.2.
DR SMR; Q85297; -.
DR GeneID; 932088; -.
DR KEGG; vg:932088; -.
DR Proteomes; UP000000867; 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 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..178
FT /note="Probable dual specificity protein phosphatase H1
FT homolog"
FT /id="PRO_0000094871"
FT DOMAIN 23..172
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT ACT_SITE 110
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT MUTAGEN 110
FT /note="C->S: Complete loss of activity."
FT /evidence="ECO:0000269|PubMed:7831813"
FT CONFLICT 172..178
FT /note="HKLKLFG -> T (in Ref. 1; AAA66956)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 178 AA; 20627 MW; 318C99B3400A885F CRC64;
MDKKSLYENV LLKSTGALPK ARVPTKMMRV TDYVYLGNYN DAKAAPTSGI GFKYILNLTT
EKYTIKNSSI TIIHMPLVDD EYTDLTKYFD YATTFLSNCE DKHYPVLVHC MAGVNRSGAI
IMAYLMSRKS KDIPAFMYFL YIYHSIREQR GAFLENPSFR RQIIEKYIIN EHKLKLFG
