ID   A17_FOWPN               Reviewed;         198 AA.
AC   Q9J551;
DT   29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   02-DEC-2020, entry version 60.
DE   RecName: Full=Virion membrane protein A17 precursor homolog;
GN   OrderedLocusNames=FPV182;
OS   Fowlpox virus (strain NVSL) (FPV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Avipoxvirus.
OX   NCBI_TaxID=928301;
OH   NCBI_TaxID=7742; Vertebrata.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10729156; DOI=10.1128/jvi.74.8.3815-3831.2000;
RA   Afonso C.L., Tulman E.R., Lu Z., Zsak L., Kutish G.F., Rock D.L.;
RT   "The genome of fowlpox virus.";
RL   J. Virol. 74:3815-3831(2000).
CC   -!- FUNCTION: Envelope protein which participates in virus morphogenesis.
CC       Needed for an early step in viral crescent membrane formation by
CC       interacting with D13 scaffold protein. Its interaction with D13
CC       scaffold protein leads to the formation of rigid, crescent-shaped
CC       membranes that assemble around the cytoplasmic virus factory. Membrane
CC       anchor for the protein A27. A17-A27 virus envelope protein might be
CC       involved in fusion or attachment, and can further associate to A26 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts (via N-terminus) with D13 scaffold; this interaction
CC       helps D13 to associate with membranes. Interacts with A14. Interacts
CC       with A27; this interaction allows A27 to be anchored in the mature
CC       virion (MV) membrane. Part of a complex composed of A17, A25, A26 and
CC       A27 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000305}; Multi-pass
CC       membrane protein {ECO:0000305}.
CC   -!- PTM: The 22 kDa precursor is probably cleaved by the I7 protease during
CC       virus maturation. {ECO:0000250}.
CC   -!- PTM: Phosphorylated on tyrosine and threonine. Its phosphorylation
CC       state is regulated by the F10 kinase and the H1 phosphatase (By
CC       similarity). Phosphorylation by F10 kinase seems to be required to form
CC       the membranes associated with IV (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the chordopoxvirinae A17 family. {ECO:0000305}.
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DR   EMBL; AF198100; AAF44526.1; -; Genomic_DNA.
DR   RefSeq; NP_039145.1; NC_002188.1.
DR   GeneID; 1486754; -.
DR   KEGG; vg:1486754; -.
DR   Proteomes; UP000008597; Genome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR   GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR007977; Poxvirus_P21.
DR   Pfam; PF05313; Pox_P21; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Membrane; Phosphoprotein; Reference proteome;
KW   Transmembrane; Transmembrane helix; Viral envelope protein; Virion.
FT   CHAIN           1..198
FT                   /note="Virion membrane protein A17 precursor homolog"
FT                   /id="PRO_0000099260"
FT   TOPO_DOM        1..55
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        56..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        77..145
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        146..166
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        167..198
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000250"
FT   SITE            18..19
FT                   /note="Cleavage; by I7 protease"
FT                   /evidence="ECO:0000250"
FT   SITE            182..183
FT                   /note="Cleavage; by I7 protease"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         198
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250"
FT   DISULFID        177
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   198 AA;  21966 MW;  C75FDCED33A57F2E CRC64;
     MDNNYLNYYN VFEEFDAGAG IKEKELFTEE QQLSFLPKKG LGNGGFDGVE RLYSNIINNN
     DIKSLLALIM LVFAINTNSL VALIFIILSA IFVPVPALII AYCIALHLKN GSDATHVGIS
     ILLMLASAVT IYLTSTSKIS KGFKRAIDVV LLVILGFYIV KIYGIDRQIS IPSRRYCRQM
     SGPSSLENLN AFQTHSNY