ID   A16_VAR67               Reviewed;         377 AA.
AC   P33841;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Virion membrane protein A16;
GN   ORFNames=A16L;
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 part of the entry-fusion complex responsible
CC       for the virus membrane fusion with host cell membrane during virus
CC       entry. Also plays a role in cell-cell fusion (syncytium formation) (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Part of a stable entry-fusion complex (EFC) which is at least
CC       composed of proteins A16, A21, A28, G3, G9, H2, J5, and L5. Formation
CC       of the viral membrane is necessary for the assembly of the complex.
CC       Interacts with G9 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000305}; Single-pass type
CC       II membrane protein {ECO:0000305}. Note=Component of the mature virion
CC       (MV) membrane. The mature virion is located in the cytoplasm of
CC       infected cells and is probably released by cell lysis. {ECO:0000250}.
CC   -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC   -!- PTM: Most cysteines are linked by disulfide bonds. They are created by
CC       the viral disulfide bond formation pathway, a poxvirus-specific redox
CC       pathway that operates on the cytoplasmic side of the MV membranes (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the poxviridae A16/G9/J5 family. {ECO:0000305}.
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DR   EMBL; X69198; CAA49061.1; -; Genomic_DNA.
DR   PIR; H36849; H36849.
DR   RefSeq; NP_042164.1; NC_001611.1.
DR   GeneID; 1486491; -.
DR   KEGG; vg:1486491; -.
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   GO; GO:0039663; P:membrane fusion involved in viral entry into host cell; IEA:UniProtKB-KW.
DR   GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR   InterPro; IPR004251; Pox_virus_G9/A16.
DR   Pfam; PF03003; Pox_G9-A16; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Fusion of virus membrane with host membrane; Late protein;
KW   Lipoprotein; Membrane; Myristate; Reference proteome; Signal-anchor;
KW   Transmembrane; Transmembrane helix; Viral envelope protein;
KW   Viral penetration into host cytoplasm; Virion; Virus entry into host cell.
FT   INIT_MET        1
FT                   /note="Removed; by host"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..377
FT                   /note="Virion membrane protein A16"
FT                   /id="PRO_0000099254"
FT   TOPO_DOM        2..341
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        342..362
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        363..377
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255"
FT   LIPID           2
FT                   /note="N-myristoyl glycine; by host"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   377 AA;  43546 MW;  98002E9E45602894 CRC64;
     MGAAVTLNRI NIASGIADIR DKYMELGFNY PKYNRTVKFA EESYMYYYET SPGEIKPKFC
     LIDGMSIDHC SSFIVPEFAK QYVLIHGEPC SSFKFRPGTL IYYQNEVTPE YIKDLKHATD
     YIASGQRCHF IKKDYLLGDS DSVAKCCSKT NTKHCPKIFN NNYKTEHCDD FMTGFCRNDP
     GNPNCLEWLR VKRKPAMSTY SDICSKHMDA RYCSEFIRII RPDYFTFGDT ALYVFCNDHK
     GNRNCWCANY PKSNSGDKYL GPRVCWLHEC TDESRDRKWL YYNQDVQRTR CKYVGCTINV
     NSLALKNSQA ELTSNCTRTT STVGDIHPGE PVVKDKIKLP TWLGAAITLV VISVIFYFIS
     IYSRPKIKTN DINVRRR