A17_VARV
ID A17_VARV Reviewed; 203 AA.
AC P0DOR6; P16711; P68594;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2019, sequence version 1.
DT 29-SEP-2021, entry version 10.
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.
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Garcia-1966;
RA Shchelkunov S.N., Totmenin A.V., Sosnovtsev S.V., Safronov P.F.,
RA Resenchuk S.M., Blinov V.M., Sandakhchiev L.S.;
RT "XhoI-D DNA fragment of Variola minor virus strain Garcia-1966.";
RL Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
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; L22579; AAA60869.1; -; Genomic_DNA.
DR EMBL; X76268; CAA53890.1; -; Genomic_DNA.
DR PIR; G72165; G72165.
DR PIR; T28559; T28559.
DR RefSeq; NP_042165.1; NC_001611.1.
DR GeneID; 1486492; -.
DR KEGG; vg:1486492; -.
DR Proteomes; UP000119805; 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; Transmembrane;
KW Transmembrane helix; Viral envelope protein; Virion.
FT CHAIN 1..203
FT /note="Virion membrane protein A17 precursor"
FT /id="PRO_0000448155"
FT PROPEP 1..16
FT /evidence="ECO:0000250"
FT /id="PRO_0000448156"
FT CHAIN 17..185
FT /note="Mature 21 kDa protein A17"
FT /evidence="ECO:0000250"
FT /id="PRO_0000448157"
FT PROPEP 185..203
FT /evidence="ECO:0000250"
FT /id="PRO_0000448158"
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
