ID   A16_FOWPN               Reviewed;         369 AA.
AC   Q9J552;
DT   29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 48.
DE   RecName: Full=Virion membrane protein A16 homolog;
GN   OrderedLocusNames=FPV181;
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 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; AF198100; AAF44525.1; -; Genomic_DNA.
DR   RefSeq; NP_039144.1; NC_002188.1.
DR   GeneID; 1486753; -.
DR   KEGG; vg:1486753; -.
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   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
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   Lipid-binding; Lipoprotein; Membrane; Myristate; Reference proteome;
KW   Signal-anchor; 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..369
FT                   /note="Virion membrane protein A16 homolog"
FT                   /id="PRO_0000099256"
FT   TOPO_DOM        2..330
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        331..351
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        352..369
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255"
FT   LIPID           2
FT                   /note="N-myristoyl glycine; by host"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   369 AA;  42082 MW;  380A71032C18BB99 CRC64;
     MGQHVSNITV IATPQAPETK YLRVEYTGGY DDEYIRFFEA ENIHSGDIGS EISPPFCLTR
     DTTVKQCASF LSPEAKKKFV IVPGEPCKSL SFRPGSILDL QKIPYGTESY VLDGTRCRFI
     NIDYLYTDPD IKRCCNKESD KDCPEIFSNN YETDHCDTIM SSICLQTPGS LPCREWLEKK
     REVAFDTYMK VCSDHLDANY CSDFVDYTRP DNFGYSDAAI LSYCSKHRNN PNCWCVTTPK
     NDKLFSLELA LGPKVCWLHE CTDKSKDRKY LLFDQDVQRT NCKYIGCNIN VDTLRLRNSV
     AELIAKCGGS IAEDTVLGDD SYNKEAKLPS FFSIIPVCIV LLCLFVLFYF LRIYDAKVIN
     SNTINVYRK