ID   TSTP_SHV21              Reviewed;         164 AA.
AC   P18347;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   02-JUN-2021, entry version 59.
DE   RecName: Full=Transforming protein STP;
GN   Name=1; Synonyms=STP;
OS   Saimiriine herpesvirus 2 (strain 11) (SaHV-2) (Herpesvirus saimiri).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Gammaherpesvirinae; Rhadinovirus.
OX   NCBI_TaxID=10383;
OH   NCBI_TaxID=9521; Saimiri sciureus (Common squirrel monkey).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2545905; DOI=10.1128/jvi.63.8.3307-3314.1989;
RA   Murthy S.C.S., Trimble J.J., Desrosiers R.C.;
RT   "Deletion mutants of herpesvirus saimiri define an open reading frame
RT   necessary for transformation.";
RL   J. Virol. 63:3307-3314(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=1321287; DOI=10.1128/jvi.66.8.5047-5058.1992;
RA   Albrecht J.-C., Nicholas J., Biller D., Cameron K.R., Biesinger B.,
RA   Newman C., Wittmann S., Craxton M.A., Coleman H., Fleckenstein B.,
RA   Honess R.W.;
RT   "Primary structure of the herpesvirus saimiri genome.";
RL   J. Virol. 66:5047-5058(1992).
CC   -!- FUNCTION: Stp is required for transformation, but it is not required
CC       for replication of the virus. The T-lymphocyte is the target cell for
CC       transformation by herpesvirus saimiri.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
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DR   EMBL; X64346; CAA45623.1; -; Genomic_DNA.
DR   EMBL; M28071; AAA58725.1; -; Genomic_DNA.
DR   RefSeq; NP_040202.1; NC_001350.1.
DR   SMR; P18347; -.
DR   ELM; P18347; -.
DR   GeneID; 1488260; -.
DR   KEGG; vg:1488260; -.
DR   Proteomes; UP000000587; Genome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR016318; Transforming_StpA/StpB.
DR   PIRSF; PIRSF001786; Transform_StpA/StpB; 1.
PE   4: Predicted;
KW   Membrane; Metal-binding; Oncogene; Reference proteome; Transmembrane;
KW   Transmembrane helix; Zinc; Zinc-finger.
FT   CHAIN           1..164
FT                   /note="Transforming protein STP"
FT                   /id="PRO_0000116191"
FT   TRANSMEM        136..161
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ZN_FING         122..135
FT   REGION          1..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..32
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   164 AA;  17061 MW;  BAB6AB8D650ADE62 CRC64;
     MARGLGEGDP QENDESNGDP PHNTDERSDG DDGPTPYLPV TLLNAGPFGP YNPYCLLGHP
     VQESGCPGRP TALSGAVGLP TPSGSRSSSH LSTPVGLSAV RVSGCGGAGS EEHVYAEVGS
     LHSEHEQEGD KCTDCSVTIL LLLVIIVLLL IIIGLMLVIM FKKM