ID   F17_VACCC               Reviewed;         101 AA.
AC   P68454; P07397;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1988, sequence version 1.
DT   03-AUG-2022, entry version 48.
DE   RecName: Full=Phosphoprotein F17;
GN   ORFNames=F17R;
OS   Vaccinia virus (strain Copenhagen) (VACV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX   NCBI_TaxID=10249;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=2219722; DOI=10.1016/0042-6822(90)90294-2;
RA   Goebel S.J., Johnson G.P., Perkus M.E., Davis S.W., Winslow J.P.,
RA   Paoletti E.;
RT   "The complete DNA sequence of vaccinia virus.";
RL   Virology 179:247-266(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Goebel S.J., Johnson G.P., Perkus M.E., Davis S.W., Winslow J.P.,
RA   Paoletti E.;
RT   "Appendix to 'The complete DNA sequence of vaccinia virus'.";
RL   Virology 179:517-563(1990).
CC   -!- FUNCTION: Plays an essential role in virion assembly and morphogenesis.
CC       Also plays a role in the inhibition of host immune response by
CC       dysregulating mTOR. Sequesters host RICTOR and RPTOR, thereby
CC       disrupting mTORC1 and mTORC2 crosstalk. In turn, blocks the host
CC       antiviral response in part through mTOR-dependent degradation of cGAS,
CC       the primary poxvirus sensor. {ECO:0000250|UniProtKB:P07396}.
CC   -!- SUBUNIT: Self-associates to form high molecular-weight forms. Interacts
CC       with protein A30. Interacts with host RICTOR and RPTOR; these
CC       interactions disrupt the mTORC1 and mTORC2 crosstalk.
CC       {ECO:0000250|UniProtKB:P07396}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:P07396}. Note=Major
CC       component of the virion comprising about 10% of the virion mass.
CC       {ECO:0000250|UniProtKB:P07396}.
CC   -!- PTM: Phosphorylated on two serines. While these phosphorylations do not
CC       play a role in virion assembly; they are essential for the interaction
CC       with host RICTOR and RPTOR. {ECO:0000250|UniProtKB:P07396}.
CC   -!- MISCELLANEOUS: Originally annotated as the product of the F18R open
CC       reading frame (protein F18), it is now referred as protein F17 since
CC       there are only 17 open reading frames in the HindIII fragment.
CC       {ECO:0000250|UniProtKB:P07396}.
CC   -!- SIMILARITY: Belongs to the poxviridae F17 protein family.
CC       {ECO:0000305}.
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DR   EMBL; M35027; AAA48036.1; -; Genomic_DNA.
DR   PIR; A25726; WMVZ12.
DR   Proteomes; UP000008269; Genome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0019082; P:viral protein processing; IEA:InterPro.
DR   InterPro; IPR006854; Phosphoprotein_F17.
DR   Pfam; PF04767; Pox_F17; 1.
DR   PIRSF; PIRSF003688; VAC_PP; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Late protein; Phosphoprotein; Reference proteome; Virion.
FT   CHAIN           1..101
FT                   /note="Phosphoprotein F17"
FT                   /id="PRO_0000099518"
FT   REGION          51..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         53
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P07396"
FT   MOD_RES         62
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P07396"
SQ   SEQUENCE   101 AA;  11336 MW;  D9917F95A62EE6E0 CRC64;
     MNSHFASAHT PFYINTKEGR YLVLKAVKVC DVRTVECEGS KASCVLKVDK PSSPACERRP
     SSPSRCERMN NPGKQVPFMR TDMLQNMFAA NRDNVASRLL N