F17_VARV
ID F17_VARV Reviewed; 101 AA.
AC P0DON6; P33875;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2019, sequence version 1.
DT 03-AUG-2022, entry version 12.
DE RecName: Full=Phosphoprotein F17;
GN ORFNames=C21R, F17R;
OS Variola virus.
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus.
OX NCBI_TaxID=10255;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Bangladesh-1975;
RX PubMed=8264798; DOI=10.1038/366748a0;
RA Massung R.F., Esposito J.J., Liu L.I., Qi J., Utterback T.R., Knight J.C.,
RA Aubin L., Yuran T.E., Parsons J.M., Loparev V.N., Selivanov N.A.,
RA Cavallaro K.F., Kerlavage A.R., Mahy B.W.J., Venter J.C.;
RT "Potential virulence determinants in terminal regions of variola smallpox
RT virus genome.";
RL Nature 366:748-751(1993).
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 -!- SIMILARITY: Belongs to the poxviridae F17 protein family.
CC {ECO:0000305}.
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DR EMBL; L22579; AAA60789.1; -; Genomic_DNA.
DR PIR; T28479; T28479.
DR RefSeq; NP_042085.1; NC_001611.1.
DR GeneID; 1486578; -.
DR KEGG; vg:1486578; -.
DR Proteomes; UP000119805; 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; Phosphoprotein; Virion.
FT CHAIN 1..101
FT /note="Phosphoprotein F17"
FT /id="PRO_0000448190"
FT REGION 48..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..69
FT /note="Polar residues"
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; 11337 MW; B8160F92D14BF2B1 CRC64;
MNSHFASAHT PFYINTKEGR YLVLKAVKVC DVRTVEFEGS KASCVLKVDK PSSPASERRP
SSPSRCERMN NPGKQVPFMR TDMLQNMFAA NRDNVASRLL S