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 13-SEP-2023, entry version 52. 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; Gyrovirus chickenanemia. 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 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 //