STP_SHV24
ID STP_SHV24 Reviewed; 105 AA.
AC P25050;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 23-FEB-2022, entry version 78.
DE RecName: Full=Saimiri transformation-associated protein;
DE AltName: Full=Collagen-like protein;
DE AltName: Full=stpC;
OS Saimiriine herpesvirus 2 (strain 484-77) (SaHV-2) (Herpesvirus saimiri).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Gammaherpesvirinae; Rhadinovirus.
OX NCBI_TaxID=10382;
OH NCBI_TaxID=9521; Saimiri sciureus (Common squirrel monkey).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2161952; DOI=10.1128/jvi.64.7.3509-3515.1990;
RA Geck P., Whitaker S.A., Medveczky M.M., Medveczky P.G.;
RT "Expression of collagenlike sequences by a tumor virus, herpesvirus
RT saimiri.";
RL J. Virol. 64:3509-3515(1990).
RN [2]
RP ERRATUM OF PUBMED:2161952, AND SEQUENCE REVISION.
RX PubMed=1658399;
RA Geck P., Whitaker S.A., Medveczky M.M., Medveczky P.G.;
RL J. Virol. 65:7084-7084(1991).
CC -!- FUNCTION: Acts synergistically with Tip to stimulate NF-kappa-B
CC activity and interleukin-2 gene expression by binding to host TRAF
CC proteins. Activation of NF-kappa-B protects lymphocytes from apoptosis,
CC thereby facilitating viral induced cell transformation.
CC -!- SUBUNIT: Binds to host RAS and TRAF2.
CC -!- SUBCELLULAR LOCATION: Host membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- MISCELLANEOUS: Saimiriine herpesvirus 2 transforms T-lymphocytes,
CC including human, to continuous growth in vitro. Two viral proteins, Tip
CC and StpC, are essential for this function. The virus induced
CC transforming activation is used as an important tool of T-cell biology,
CC including HIV replication.
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DR EMBL; M31964; AAA46152.1; -; Genomic_DNA.
DR PIR; A36770; CGBEHS.
DR SMR; P25050; -.
DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR017095; StpC.
DR Pfam; PF01391; Collagen; 1.
DR PIRSF; PIRSF037035; Transforming_StpC; 1.
PE 4: Predicted;
KW Collagen; Host membrane; Host-virus interaction; Membrane; Oncogene;
KW Repeat; Transmembrane; Transmembrane helix.
FT CHAIN 1..105
FT /note="Saimiri transformation-associated protein"
FT /id="PRO_0000116199"
FT TOPO_DOM 1..75
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 97..105
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 15..74
FT /note="Collagen-like"
FT REGION 1..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..72
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 105 AA; 10260 MW; EF3DF0FE0FB446F0 CRC64;
MASEPNLRYP TEETGDRGPQ GPPGPPGPQG PPGPQGPPGP QGPPGPQGPP GPQGPPGPQG
PPGPPGPPGP SGLPGLFVTN LLLGIIILLL LIIVAILLVS KLVVN