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VP2_CAVC1
ID   VP2_CAVC1               Reviewed;         216 AA.
AC   P69484; P54091; Q99151;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 51.
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 Germany Cuxhaven-1) (CAV).
OC   Viruses; Anelloviridae; Gyrovirus.
OX   NCBI_TaxID=73475;
OH   NCBI_TaxID=9031; Gallus gallus (Chicken).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1851873; DOI=10.1128/jvi.65.6.3131-3139.1991;
RA   Noteborn M.H.M., de Boer G.F., van Roozelaar D.J., Karreman C.,
RA   Kranenburg O., Vos J.G., Jeurissen S.H.M., Hoeben R.C., Zantema A.,
RA   Koch G., van Ormondt H., van der Eb A.J.;
RT   "Characterization of cloned chicken anemia virus DNA that contains all
RT   elements for the infectious replication cycle.";
RL   J. Virol. 65:3131-3139(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1605740; DOI=10.1007/bf01309811;
RA   Meehan B.M., Todd D., Creelan J.L., Earle J.A.P., Hoey E.M., McNulty M.S.;
RT   "Characterization of viral DNAs from cells infected with chicken anaemia
RT   agent: sequence analysis of the cloned replicative form and transfection
RT   capabilities of cloned genome fragments.";
RL   Arch. Virol. 124:301-319(1992).
RN   [3]
RP   INDUCTION.
RX   PubMed=9049362; DOI=10.1099/0022-1317-76-7-1557;
RA   Douglas A.J., Phenix K., Mawhinney K.A., Todd D., Mackie D.P., Curran W.L.;
RT   "Identification of a 24 kDa protein expressed by chicken anaemia virus.";
RL   J. Gen. Virol. 76:1557-1562(1995).
RN   [4]
RP   FUNCTION.
RX   PubMed=9880024; DOI=10.1099/0022-1317-79-12-3073;
RA   Noteborn M.H., Verschueren C.A., Koch G., Van der Eb A.J.;
RT   "Simultaneous expression of recombinant baculovirus-encoded chicken anaemia
RT   virus (CAV) proteins VP1 and VP2 is required for formation of the CAV-
RT   specific neutralizing epitope.";
RL   J. Gen. Virol. 79:3073-3077(1998).
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:9880024}.
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. {ECO:0000269|PubMed:9049362}.
CC   -!- SIMILARITY: Belongs to the gyrovirus protein VP2 family. {ECO:0000305}.
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DR   EMBL; M55918; AAA91822.1; -; Genomic_DNA.
DR   EMBL; M81223; AAA42882.1; -; Genomic_DNA.
DR   PIR; A39926; A39926.
DR   PIR; A48343; A48343.
DR   RefSeq; NP_056773.1; NC_001427.1.
DR   GeneID; 1494446; -.
DR   Proteomes; UP000007528; 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   2: Evidence at transcript level;
KW   Early protein; Hydrolase; Protein phosphatase; Reference proteome.
FT   CHAIN           1..216
FT                   /note="Dual specificity protein phosphatase VP2"
FT                   /id="PRO_0000223004"
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:0000250"
FT   CONFLICT        153
FT                   /note="V -> A (in Ref. 1; AAA91822)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        187
FT                   /note="D -> N (in Ref. 2; AAA42882)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   216 AA;  24139 MW;  F82B69EF88BDDE52 CRC64;
     MHGNGGQPAA GGSESALSRE GQPGPSGAAQ GQVISNERSP RRYSTRTING VQATNKFTAV
     GNPSLQRDPD WYRWNYNHSI AVWLRECSRS HAKICNCGQF RKHWFQECAG LEDRSTQASL
     EEAILRPLRV QGKRAKRKLD YHYSQPTPNR KKVYKTVRWQ DELADREADF TPSEEDGGTT
     SSDFDEDINF DIGGDSGIVD ELLGRPFTTP APVRIV
 
 
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