TRAP_TGMVY
ID TRAP_TGMVY Reviewed; 129 AA.
AC P03562;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 23-FEB-2022, entry version 76.
DE RecName: Full=Transcriptional activator protein;
DE Short=TrAP;
DE AltName: Full=Protein AC2;
DE AltName: Full=Protein AL2;
GN ORFNames=AC2, AL2;
OS Tomato golden mosaic virus (strain Yellow vein) (TGMV).
OC Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Repensiviricetes;
OC Geplafuvirales; Geminiviridae; Begomovirus.
OX NCBI_TaxID=223341;
OH NCBI_TaxID=4081; Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=16453557; DOI=10.1002/j.1460-2075.1984.tb02114.x;
RA Hamilton W.D.O., Stein V.E., Coutts R.H.A., Buck K.W.;
RT "Complete nucleotide sequence of the infectious cloned DNA components of
RT tomato golden mosaic virus: potential coding regions and regulatory
RT sequences.";
RL EMBO J. 3:2197-2205(1984).
RN [2]
RP FUNCTION.
RX PubMed=9191840; DOI=10.1006/viro.1997.8549;
RA Sunter G., Bisaro D.M.;
RT "Regulation of a geminivirus coat protein promoter by AL2 protein (TrAP):
RT evidence for activation and derepression mechanisms.";
RL Virology 232:269-280(1997).
RN [3]
RP DNA-BINDING, TRANSACTIVATION REGION, AND PHOSPHORYLATION.
RX PubMed=10544077; DOI=10.1006/viro.1999.9925;
RA Hartitz M.D., Sunter G., Bisaro D.M.;
RT "The tomato golden mosaic virus transactivator (TrAP) is a single-stranded
RT DNA and zinc-binding phosphoprotein with an acidic activation domain.";
RL Virology 263:1-14(1999).
RN [4]
RP FUNCTION, AND INTERACTION WITH ARABIDOPSIS THALIANA SNF1.
RX PubMed=12671096; DOI=10.1105/tpc.009530;
RA Hao L., Wang H., Sunter G., Bisaro D.M.;
RT "Geminivirus AL2 and L2 proteins interact with and inactivate SNF1
RT kinase.";
RL Plant Cell 15:1034-1048(2003).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND INTERACTION WITH
RP ARABIDOPSIS THALIANA ADK1 AND ADK2.
RX PubMed=14615595; DOI=10.1105/tpc.015180;
RA Wang H., Hao L., Shung C.-Y., Sunter G., Bisaro D.M.;
RT "Adenosine kinase is inactivated by geminivirus AL2 and L2 proteins.";
RL Plant Cell 15:3020-3032(2003).
RN [6]
RP FUNCTION.
RX PubMed=15919897; DOI=10.1128/jvi.79.12.7410-7418.2005;
RA Wang H., Buckley K.J., Yang X., Buchmann R.C., Bisaro D.M.;
RT "Adenosine kinase inhibition and suppression of RNA silencing by
RT geminivirus AL2 and L2 proteins.";
RL J. Virol. 79:7410-7418(2005).
RN [7]
RP SUBUNIT, SUBCELLULAR LOCATION, INTERACTION WITH ARABIDOPSIS THALIANA ADK2,
RP AND MUTAGENESIS OF CYS-33; CYS-35; HIS-40 AND CYS-43.
RX PubMed=17715241; DOI=10.1128/jvi.00617-07;
RA Yang X., Baliji S., Buchmann R.C., Wang H., Lindbo J.A., Sunter G.,
RA Bisaro D.M.;
RT "Functional modulation of the geminivirus AL2 transcription factor and
RT silencing suppressor by self-interaction.";
RL J. Virol. 81:11972-11981(2007).
CC -!- FUNCTION: Strong activator of the late viral genes promoters. Enhances
CC the expression of the capsid protein and nuclear shuttle protein. Acts
CC as a suppressor of RNA-mediated gene silencing, also known as post-
CC transcriptional gene silencing (PTGS), a mechanism of plant viral
CC defense that limits the accumulation of viral RNAs. Suppresses the host
CC RNA silencing by inhibiting adenosine kinase (ADK), a kinase involved
CC in a general methylation pathway. Also suppresses the host basal
CC defense by interacting with and inhibiting SNF1 kinase, a key regulator
CC of cell metabolism implicated in innate antiviral defense. Determines
CC pathogenicity. {ECO:0000269|PubMed:12671096,
CC ECO:0000269|PubMed:14615595, ECO:0000269|PubMed:15919897,
CC ECO:0000269|PubMed:9191840}.
CC -!- SUBUNIT: Monomer. Homodimer. Homooligomer. Self-interaction correlates
CC with nuclear localization and efficient activation of transcription.
CC Monomers suppress local silencing by interacting with and inactivating
CC host adenosine kinase (ADK) in the cytoplasm. Interacts with and
CC inhibits host SNF1 kinase. Binds to ssDNA.
CC {ECO:0000269|PubMed:12671096, ECO:0000269|PubMed:14615595,
CC ECO:0000269|PubMed:17715241}.
CC -!- INTERACTION:
CC P03562; Q96703: AL2; Xeno; NbExp=2; IntAct=EBI-16175508, EBI-16175606;
CC P03562; Q8GZB6: SUVH4; Xeno; NbExp=4; IntAct=EBI-16175508, EBI-16175525;
CC -!- SUBCELLULAR LOCATION: Host nucleus. Host cytoplasm. Note=The
CC phosphorylated form appears to accumulate almost exclusively in the
CC nucleus, whereas the non-phosphorylated form is found in both nucleus
CC and cytoplasm.
CC -!- DOMAIN: The zinc finger and the transactivation region are involved in
CC PTGS suppression. {ECO:0000250}.
CC -!- PTM: Phosphorylated. {ECO:0000305|PubMed:10544077,
CC ECO:0000305|PubMed:14615595}.
CC -!- SIMILARITY: Belongs to the geminiviridae transcriptional activator
CC protein family. {ECO:0000305}.
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DR EMBL; K02029; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A04165; QQCVL2.
DR DIP; DIP-62056N; -.
DR IntAct; P03562; 6.
DR Proteomes; UP000007405; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0019028; C:viral capsid; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR InterPro; IPR000942; Gemini_AL2.
DR Pfam; PF01440; Gemini_AL2; 1.
DR PRINTS; PR00230; GEMCOATAL2.
PE 1: Evidence at protein level;
KW Activator; DNA-binding; Host cytoplasm; Host nucleus;
KW Host-virus interaction; Metal-binding; Phosphoprotein; Reference proteome;
KW Suppressor of RNA silencing; Zinc; Zinc-finger.
FT CHAIN 1..129
FT /note="Transcriptional activator protein"
FT /id="PRO_0000222230"
FT ZN_FING 33..50
FT /evidence="ECO:0000250"
FT REGION 73..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..129
FT /note="Transactivation"
FT MOTIF 13..28
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 87..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 33
FT /note="C->A: 66% loss of transactivation."
FT /evidence="ECO:0000269|PubMed:17715241"
FT MUTAGEN 35
FT /note="C->A: 95% loss of transactivation."
FT /evidence="ECO:0000269|PubMed:17715241"
FT MUTAGEN 40
FT /note="H->A: Enhances transactivation."
FT /evidence="ECO:0000269|PubMed:17715241"
FT MUTAGEN 43
FT /note="C->A: 72% loss of transactivation."
FT /evidence="ECO:0000269|PubMed:17715241"
SQ SEQUENCE 129 AA; 14888 MW; 001759FB17963B9E CRC64;
MRNSSSSTPP SIKAQHRAAK RRAIRRRRID LNCGCSIYIH IDCRNNGFTH RGTYHCASSR
EWRLYLGDNK SPLFQDNQRR GSPLHQHQDI PLTNQVQPQP EESIGSPQGI SQLPSMDDID
DSFWENLFK
