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DUSP_VARV
ID   DUSP_VARV               Reviewed;         171 AA.
AC   P0DOQ6; P33064;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   16-OCT-2019, sequence version 1.
DT   03-AUG-2022, entry version 15.
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, I1L;
OS   Variola virus.
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus.
OX   NCBI_TaxID=10255;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Bangladesh-1975;
RX   PubMed=8264798; DOI=10.1038/366748a0;
RA   Massung R.F., Esposito J.J., Liu L.I., Qi J., Utterback T.R., Knight J.C.,
RA   Aubin L., Yuran T.E., Parsons J.M., Loparev V.N., Selivanov N.A.,
RA   Cavallaro K.F., Kerlavage A.R., Mahy B.W.J., Venter J.C.;
RT   "Potential virulence determinants in terminal regions of variola smallpox
RT   virus genome.";
RL   Nature 366:748-751(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Garcia-1966;
RA   Shchelkunov S.N., Balkin I.V., Totmenin A.V., Resenchuk S.M., Blinov V.M.,
RA   Sandakhchiev L.S.;
RL   Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {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; L22579; AAA60832.1; -; Genomic_DNA.
DR   EMBL; X76264; CAA53838.1; -; Genomic_DNA.
DR   PIR; B72161; B72161.
DR   PIR; T28522; T28522.
DR   RefSeq; NP_042128.1; NC_001611.1.
DR   SMR; P0DOQ6; -.
DR   GeneID; 1486439; -.
DR   KEGG; vg:1486439; -.
DR   Proteomes; UP000119805; 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   2: Evidence at transcript 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   Viral immunoevasion; Virion.
FT   CHAIN           1..171
FT                   /note="Dual specificity protein phosphatase H1"
FT                   /id="PRO_0000448116"
FT   DOMAIN          23..171
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"
SQ   SEQUENCE   171 AA;  19746 MW;  1D58C54FF17BADF7 CRC64;
     MDKKSLYKYL LLRSTGDMRR AKSPTIMTRV TNNVYLGNYK NAMNAPSSEV KFKYVLNLTM
     DKYTLPNSNI NIIHIPLVDD TTTDISKYFD DVTAFLSKCD QRNEPVLVHC VAGVNRSGAM
     ILAYLMSKNK ESSPMLYFLY VYHSMRDLRG AFVENPSFKR QIIEKYVIDK N
 
 
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