A16_VACCW
ID A16_VACCW Reviewed; 377 AA.
AC P16710; Q80HV5;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Virion membrane protein A16;
GN OrderedLocusNames=VACWR136; ORFNames=A16L;
OS Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain
OS WR)).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX NCBI_TaxID=10254;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Esposito J.J., Frace A.M., Sammons S.A., Olsen-Rasmussen M., Osborne J.,
RA Wohlhueter R.;
RT "Sequencing of the coding region of Vaccinia-WR to an average 9-fold
RT redundancy and an error rate of 0.16/10kb.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-275.
RX PubMed=2370683; DOI=10.1128/jvi.64.8.3853-3863.1990;
RA Pacha R.F., Meis R.J., Condit R.C.;
RT "Structure and expression of the vaccinia virus gene which prevents virus-
RT induced breakdown of RNA.";
RL J. Virol. 64:3853-3863(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).
RN [4]
RP IDENTIFICATION IN A COMPLEX WITH A21; A28; G3; G9; H2; J5 AND L5.
RX PubMed=16339313; DOI=10.1073/pnas.0509239102;
RA Senkevich T.G., Ojeda S., Townsley A., Nelson G.E., Moss B.;
RT "Poxvirus multiprotein entry-fusion complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:18572-18577(2005).
RN [5]
RP FUNCTION, DISULFIDE BONDS, INDUCTION, AND TOPOLOGY.
RX PubMed=16352530; DOI=10.1128/jvi.80.1.51-61.2006;
RA Ojeda S., Senkevich T.G., Moss B.;
RT "Entry of vaccinia virus and cell-cell fusion require a highly conserved
RT cysteine-rich membrane protein encoded by the A16L gene.";
RL J. Virol. 80:51-61(2006).
RN [6]
RP INTERACTION WITH G9.
RX PubMed=18353946; DOI=10.1128/jvi.00162-08;
RA Wagenaar T.R., Ojeda S., Moss B.;
RT "Vaccinia virus A56/K2 fusion regulatory protein interacts with the A16 and
RT G9 subunits of the entry fusion complex.";
RL J. Virol. 82:5153-5160(2008).
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).
CC {ECO:0000269|PubMed:16352530}.
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. {ECO:0000269|PubMed:16339313,
CC ECO:0000269|PubMed:18353946}.
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 (Probable). The mature virion is located in the cytoplasm
CC of infected cells and is probably released by cell lysis.
CC {ECO:0000269|PubMed:9188589, ECO:0000305}.
CC -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC {ECO:0000269|PubMed:16352530}.
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.
CC -!- SIMILARITY: Belongs to the poxviridae A16/G9/J5 family. {ECO:0000305}.
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DR EMBL; AY243312; AAO89415.1; -; Genomic_DNA.
DR EMBL; M32064; AAA48348.2; -; Genomic_DNA.
DR PIR; A36415; A36415.
DR RefSeq; YP_233018.1; NC_006998.1.
DR IntAct; P16710; 1.
DR MINT; P16710; -.
DR iPTMnet; P16710; -.
DR DNASU; 3707666; -.
DR GeneID; 3707666; -.
DR KEGG; vg:3707666; -.
DR Proteomes; UP000000344; 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 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..377
FT /note="Virion membrane protein A16"
FT /id="PRO_0000099253"
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..377
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 377 AA; 43425 MW; EE79C44446B542FA 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 SAVGDVHPGE PVVKDKIKLP TWLGAAITLV VISVIFYFIS
IYSRPKIKTN DINVRRR
