ID   VP2_CAVCA               Reviewed;         216 AA.
AC   Q9IZU7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=Dual specificity protein phosphatase VP2;
DE            EC=3.1.3.16;
DE            EC=3.1.3.48;
GN   Name=VP2;
OS   Chicken anemia virus (isolate Australia/CAU269-7/2000) (CAV).
OC   Viruses; Anelloviridae; Gyrovirus.
OX   NCBI_TaxID=486492;
OH   NCBI_TaxID=9031; Gallus gallus (Chicken).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11022294; DOI=10.1111/j.1751-0813.2000.tb11942.x;
RA   Brown H.K., Browning G.F., Scott P.C., Crabb B.S., Brown K.;
RT   "Full-length infectious clone of a pathogenic Australian isolate of chicken
RT   anaemia virus.";
RL   Aust. Vet. J. 78:637-640(2000).
RN   [2]
RP   FUNCTION, AND MUTAGENESIS OF CYS-95.
RX   PubMed=12151384; DOI=10.1074/jbc.m201752200;
RA   Peters M.A., Jackson D.C., Crabb B.S., Browning G.F.;
RT   "Chicken anemia virus VP2 is a novel dual specificity protein
RT   phosphatase.";
RL   J. Biol. Chem. 277:39566-39573(2002).
RN   [3]
RP   MUTAGENESIS OF CYS-97.
RX   PubMed=15722522; DOI=10.1099/vir.0.80197-0;
RA   Peters M.A., Jackson D.C., Crabb B.S., Browning G.F.;
RT   "Mutation of chicken anemia virus VP2 differentially affects
RT   serine/threonine and tyrosine protein phosphatase activities.";
RL   J. Gen. Virol. 86:623-630(2005).
CC   -!- FUNCTION: May act as a scaffold protein in virion assembly. May also
CC       play a role in intracellular signaling during viral replication.
CC       {ECO:0000269|PubMed:12151384}.
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   -!- 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; EC=3.1.3.16;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:61977; EC=3.1.3.16;
CC   -!- INDUCTION: VP1 and VP2 are detected 12 hours post infection, while VP3
CC       only after 24 hours.
CC   -!- SIMILARITY: Belongs to the gyrovirus protein VP2 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF227982; AAF34787.1; -; Genomic_DNA.
DR   PRIDE; Q9IZU7; -.
DR   Proteomes; UP000007539; Genome.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR   InterPro; IPR004118; HEV_TT_virus_Orf2/Gyrovir_Vp2.
DR   Pfam; PF02957; TT_ORF2; 1.
PE   1: Evidence at protein level;
KW   Early protein; Hydrolase; Protein phosphatase.
FT   CHAIN           1..216
FT                   /note="Dual specificity protein phosphatase VP2"
FT                   /id="PRO_0000314474"
FT   REGION          1..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          165..187
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..50
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        95
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000305"
FT   MUTAGEN         95
FT                   /note="C->S: Complete loss of phosphatase activity. Reduced
FT                   cytopathogenicity and marked inhibition of viral growth in
FT                   cell culture."
FT                   /evidence="ECO:0000269|PubMed:12151384"
FT   MUTAGEN         97
FT                   /note="C->S: 70% loss of phosphotyrosine activity. 700%
FT                   increase of phosphoserine/phosphothreonine phosphatase
FT                   activity. Reduced cytopathogenicity and marked inhibition
FT                   of viral growth in cell culture."
FT                   /evidence="ECO:0000269|PubMed:15722522"
SQ   SEQUENCE   216 AA;  24112 MW;  F83EB3D07B97F752 CRC64;
     MHGNGGQPAA GGSESALSRE GQPGPSGAAQ GQVISNERSP RRYSTRTING VQATNKFTAV
     GNPSLQRDPD WYRWNYSHSI AVWLRECSRS HAKICNCGQF RKHWFQECAG LEDRSTQASL
     EEAILRPLRV QGKRAKRKLD YHYSQPTPNR KKVYKTVRWQ DELADREADF TPSEEDGGTT
     SSDFDEDINF DIGGDSGIVD ELLGRPFTTP APVRIV