ID   A17_VAR67               Reviewed;         203 AA.
AC   P0DOR5; P16711; P68594;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   16-OCT-2019, sequence version 1.
DT   12-AUG-2020, entry version 5.
DE   RecName: Full=Virion membrane protein A17 precursor;
DE   AltName: Full=23 kDa late protein;
DE   Contains:
DE     RecName: Full=Mature 21 kDa protein A17;
GN   ORFNames=A17L, A18L;
OS   Variola virus (isolate Human/India/Ind3/1967) (VARV) (Smallpox virus).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus.
OX   NCBI_TaxID=587200;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=8384129; DOI=10.1016/0014-5793(93)80041-r;
RA   Shchelkunov S.N., Blinov V.M., Sandakhchiev L.S.;
RT   "Genes of variola and vaccinia viruses necessary to overcome the host
RT   protective mechanisms.";
RL   FEBS Lett. 319:80-83(1993).
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: Homodimer; disulfide-linked (Probable). Interacts (via N-
CC       terminus) with D13 scaffold; this interaction helps D13 to associate
CC       with membranes. Interacts with A14. Interacts with A27; this
CC       interaction allows A27 to be anchored in the mature virion (MV)
CC       membrane. Part of a complex composed of A17, A25, A26 and A27 (By
CC       similarity). {ECO:0000250, ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000305}; Multi-pass
CC       membrane protein {ECO:0000305}. Note=The 23 kDa precursor is associated
CC       with immature virions (IV) and the final 21 kDa form is present in
CC       mature virions (MV). {ECO:0000250}.
CC   -!- PTM: The 23 kDa precursor is cleaved into a final 21 kDa form by the I7
CC       protease during 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   -!- PTM: Not glycosylated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the chordopoxvirinae A17 family. {ECO:0000305}.
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DR   EMBL; X69198; CAA49062.1; -; Genomic_DNA.
DR   PIR; I36849; I36849.
DR   RefSeq; NP_042165.1; NC_001611.1.
DR   GeneID; 1486492; -.
DR   KEGG; vg:1486492; -.
DR   Proteomes; UP000002060; 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..203
FT                   /note="Virion membrane protein A17 precursor"
FT                   /id="PRO_0000099259"
FT   PROPEP          1..16
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000413886"
FT   CHAIN           17..185
FT                   /note="Mature 21 kDa protein A17"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000413887"
FT   PROPEP          185..203
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000413888"
FT   TOPO_DOM        1..65
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        66..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        87..138
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        139..159
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        160..203
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000250"
FT   REGION          1..38
FT                   /note="Binding to D13 scaffold protein"
FT                   /evidence="ECO:0000250"
FT   SITE            16..17
FT                   /note="Cleavage; by I7 protease"
FT                   /evidence="ECO:0000250"
FT   SITE            185..186
FT                   /note="Cleavage; by I7 protease"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         203
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250"
FT   DISULFID        101..121
FT                   /evidence="ECO:0000250"
FT   DISULFID        178
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   203 AA;  22999 MW;  24759AF6FC18D431 CRC64;
     MSYLRYYNML DDFSAGAGVL DKDLFTEEQQ QSFMPKDGGM MQNDYGGMND YLGIFKNNDV
     RTLLGLILFV LALYSPPLIS ILMIFISSFL LPLTSLVITY CLVTQMYRGG NGNTVGMSIV
     CIVAAVIIMA INVFTNSQIF NIISYIILFI LFFAYVMNIE RQDYRRSINV TIPEQYTCNK
     PYTAGNKVDV DIPTFNSLNT DDY