TIO_ATHV3
ID TIO_ATHV3 Reviewed; 269 AA.
AC Q9YJQ8;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Protein tio;
OS Ateline herpesvirus 3 (AtHV-3) (Herpesvirus ateles).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Gammaherpesvirinae; Rhadinovirus.
OX NCBI_TaxID=85618;
OH NCBI_TaxID=9506; Ateles.
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=73;
RX PubMed=10233922; DOI=10.1128/jvi.73.6.4631-4639.1999;
RA Albrecht J.-C., Friedrich U., Kardinal C., Koehn J., Fleckenstein B.,
RA Feller S.M., Biesinger B.;
RT "Herpesvirus ateles gene product Tio interacts with nonreceptor protein
RT tyrosine kinases.";
RL J. Virol. 73:4631-4639(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=73;
RX PubMed=10623770; DOI=10.1128/jvi.74.2.1033-1037.2000;
RA Albrecht J.-C.;
RT "Primary structure of the Herpesvirus ateles genome.";
RL J. Virol. 74:1033-1037(2000).
RN [3]
RP FUNCTION.
RC STRAIN=73;
RX PubMed=15331715; DOI=10.1128/jvi.78.18.9814-9819.2004;
RA Albrecht J.-C., Biesinger B., Mueller-Fleckenstein I., Lengenfelder D.,
RA Schmidt M., Fleckenstein B., Ensser A.;
RT "Herpesvirus ateles Tio can replace herpesvirus saimiri StpC and Tip
RT oncoproteins in growth transformation of monkey and human T cells.";
RL J. Virol. 78:9814-9819(2004).
RN [4]
RP PHOSPHORYLATION AT TYR-136, AND MUTAGENESIS OF TYR-49; TYR-136; TYR-167;
RP TYR-171 AND 192-PRO--ARG-194.
RC STRAIN=73;
RX PubMed=16051843; DOI=10.1128/jvi.79.16.10507-10513.2005;
RA Albrecht J.-C., Mueller-Fleckenstein I., Schmidt M., Fleckenstein B.,
RA Biesinger B.;
RT "Tyrosine phosphorylation of the Tio oncoprotein is essential for
RT transformation of primary human T cells.";
RL J. Virol. 79:10507-10513(2005).
CC -!- FUNCTION: Transforms host T-cells, inducing T-cell lymphomia in the
CC host. Activates at least SRC and LCK tyrosines kinases, thereby
CC activating signaling pathway transforming host T-cells. Human T-cells
CC transformed ex vivo display a IL2 indenpendent growth phenotype.
CC {ECO:0000269|PubMed:15331715}.
CC -!- SUBUNIT: Homodimer. Binds SH3 domain of host LYN, HCK, LCK, SRC, FYN or
CC YES. When tyrosine-phosphorylated, binds to the SH2 domain of host LCK,
CC SRC, or FYN.
CC -!- INTERACTION:
CC Q9YJQ8; P06239: LCK; Xeno; NbExp=2; IntAct=EBI-7709835, EBI-1348;
CC -!- SUBCELLULAR LOCATION: Host cell membrane {ECO:0000250}; Single-pass
CC membrane protein {ECO:0000250}. Note=Associated with plasma membrane,
CC presumably via its putative transmembrane domain.
CC -!- DOMAIN: The SH3B/LBD1 (SH3-binding) region binds LCK SH3 domain and
CC CSKH (C-terminal Src-related kinase homology) region binds the kinase
CC domains of LCK. Both motif are required to activate LCK (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated by host LCK, SRC and less efficiently by FYN.
CC {ECO:0000269|PubMed:16051843}.
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DR EMBL; AF083423; AAC95349.1; -; mRNA.
DR EMBL; AF083424; AAC95538.1; -; Genomic_DNA.
DR PIR; T42919; T42919.
DR RefSeq; NP_047977.1; NC_001987.1.
DR SMR; Q9YJQ8; -.
DR IntAct; Q9YJQ8; 1.
DR MINT; Q9YJQ8; -.
DR iPTMnet; Q9YJQ8; -.
DR PRIDE; Q9YJQ8; -.
DR GeneID; 1450415; -.
DR KEGG; vg:1450415; -.
DR Proteomes; UP000008287; Genome.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Host cell membrane; Host membrane; Host-virus interaction; Membrane;
KW Oncogene; Phosphoprotein; Transmembrane; Transmembrane helix.
FT CHAIN 1..269
FT /note="Protein tio"
FT /id="PRO_0000116195"
FT TOPO_DOM 1..246
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 247..267
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 268..269
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 1..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 158..167
FT /note="CSKH/LBD2"
FT /evidence="ECO:0000250"
FT REGION 186..195
FT /note="SH3B/LBD1"
FT /evidence="ECO:0000250"
FT COMPBIAS 28..59
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 136
FT /note="Phosphotyrosine; by host LCK"
FT /evidence="ECO:0000269|PubMed:16051843"
FT MUTAGEN 49
FT /note="Y->F: No effect on tyrosine phosphorylation and
FT viral ability to transform human T-cell."
FT /evidence="ECO:0000269|PubMed:16051843"
FT MUTAGEN 136
FT /note="Y->F: Complete loss of tyrosine phosphorylation and
FT viral ability to transform human T-cell."
FT /evidence="ECO:0000269|PubMed:16051843"
FT MUTAGEN 167
FT /note="Y->F: No effect on tyrosine phosphorylationand viral
FT ability to transform human T-cell."
FT /evidence="ECO:0000269|PubMed:16051843"
FT MUTAGEN 171
FT /note="Y->F: No effect on tyrosine phosphorylationand viral
FT ability to transform human T-cell."
FT /evidence="ECO:0000269|PubMed:16051843"
FT MUTAGEN 192..194
FT /note="PPR->ARG: Complete loss of tyrosine phosphorylation
FT and viral ability to transform human T-cell."
FT /evidence="ECO:0000269|PubMed:16051843"
SQ SEQUENCE 269 AA; 29197 MW; 4C6D8020BDA5543D CRC64;
MANEPQEHEE GKPFFPPLGD SGEEGPPNIP QDPTPGTPPG PINSKNEDYP PPLENPGPNK
SEGPPDGSGN SSPPVTMLVK NNGDRTKQDV SESGGNNSAP NSVESKHTSS SSSAGNGNET
KCPDEQNTQE CITTIYIPWE DAKPKLMGLV KLDSSDSEEE RSPFNKYPKN YKKLRVDMGE
NWPPGIPPPQ LPPRPANLGQ KQSATSKNGP QIILREATEV ESQQATDGQL NHRVEKVEKK
LTCVICLLIG ILVLLILLFM LGFLFLLMK
