ID A16_VACCC Reviewed; 378 AA. AC P20993; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 23-FEB-2022, entry version 77. DE RecName: Full=Virion membrane protein A16; GN ORFNames=A16L; OS Vaccinia virus (strain Copenhagen) (VACV). OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes; OC Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus. OX NCBI_TaxID=10249; OH NCBI_TaxID=9606; Homo sapiens (Human). RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=2219722; DOI=10.1016/0042-6822(90)90294-2; RA Goebel S.J., Johnson G.P., Perkus M.E., Davis S.W., Winslow J.P., RA Paoletti E.; RT "The complete DNA sequence of vaccinia virus."; RL Virology 179:247-266(1990). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Goebel S.J., Johnson G.P., Perkus M.E., Davis S.W., Winslow J.P., RA Paoletti E.; RT "Appendix to 'The complete DNA sequence of vaccinia virus'."; RL Virology 179:517-563(1990). RN [3] RP MYRISTOYLATION AT GLY-2, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLY-2. RX PubMed=9188589; DOI=10.1128/jvi.71.7.5218-5226.1997; RA Martin K.H., Grosenbach D.W., Franke C.A., Hruby D.E.; RT "Identification and analysis of three myristylated vaccinia virus late RT proteins."; RL J. Virol. 71:5218-5226(1997). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M35027; AAA48138.1; -; Genomic_DNA. DR PIR; I42518; I42518. DR SMR; P20993; -. DR iPTMnet; P20993; -. DR Proteomes; UP000008269; 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 InterPro; IPR004251; Pox_virus_G9/A16. DR Pfam; PF03003; Pox_G9-A16; 1. PE 1: Evidence at protein 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 CHAIN 2..378 FT /note="Virion membrane protein A16" FT /id="PRO_0000099251" FT TOPO_DOM 2..342 FT /note="Virion surface" FT /evidence="ECO:0000255" FT TRANSMEM 343..363 FT /note="Helical; Signal-anchor for type II membrane protein" FT /evidence="ECO:0000255" FT TOPO_DOM 364..378 FT /note="Intravirion" FT /evidence="ECO:0000255" FT LIPID 2 FT /note="N-myristoyl glycine; by host" FT /evidence="ECO:0000269|PubMed:9188589" FT MUTAGEN 2 FT /note="G->A: Complete loss of myristoylation." FT /evidence="ECO:0000269|PubMed:9188589" SQ SEQUENCE 378 AA; 43562 MW; 05ED614AA1D11A19 CRC64; MGAAVTLNRI KIAPGIADIR DKYMELGFNY PEYNRAVKFA EESYTYYYET SPGEIKPKFC LIDGMSIDHC SSFIVPEFAK QYVLIHGEPC SSFKFRPGSL IYYQNEVTPE YIKDLKHATD YIASGQRCHF IKKDYLLGDS DSVAKCCSKT NTKHCPKIFN NNYKTEHCDD FMTGFCRNDP GNPNCLEWLR AKRKPAMSTY SDICSKHMDA RYCSEFIRII RPDYFTFGDT ALYVFCNDHK GNRNCWCANY PKSNSGDKYL GPRVCWLHEC TDESRDRKWL YYNQDVQRTR CKYVGCTINV NSLALKNSQA ELTSNCTRTT SAVGDVHHPG EPVVKDKIKL PTWLGAAITL VVISVIFYFI SIYSRPKIKT NDINVRRR //