A14_VACCW
ID A14_VACCW Reviewed; 90 AA.
AC Q76ZQ3;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 02-JUN-2021, entry version 52.
DE RecName: Full=Virion membrane protein A14;
GN Name=VACWR133;
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 PROTEIN SEQUENCE OF 1-9.
RX PubMed=17678539; DOI=10.1186/1743-422x-4-78;
RA Yang S.J.;
RT "Characterization of vaccinia virus A12L protein proteolysis and its
RT participation in virus assembly.";
RL Virol. J. 4:78-78(2007).
RN [3]
RP FUNCTION.
RX PubMed=9445029; DOI=10.1128/jvi.72.2.1287-1296.1998;
RA Rodriguez J.R., Risco C., Carrascosa J.L., Esteban M., Rodriguez D.;
RT "Vaccinia virus 15-kilodalton (A14L) protein is essential for assembly and
RT attachment of viral crescents to virosomes.";
RL J. Virol. 72:1287-1296(1998).
RN [4]
RP PHOSPHORYLATION, AND INTERACTION WITH A17.
RX PubMed=10196242; DOI=10.1128/jvi.73.5.3534-3543.1999;
RA Betakova T., Wolffe E.J., Moss B.;
RT "Regulation of vaccinia virus morphogenesis: phosphorylation of the A14L
RT and A17L membrane proteins and C-terminal truncation of the A17L protein
RT are dependent on the F10L kinase.";
RL J. Virol. 73:3534-3543(1999).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10729144; DOI=10.1128/jvi.74.8.3682-3695.2000;
RA Traktman P., Liu K., DeMasi J., Rollins R., Jesty S., Unger B.;
RT "Elucidating the essential role of the A14 phosphoprotein in vaccinia virus
RT morphogenesis: construction and characterization of a tetracycline-
RT inducible recombinant.";
RL J. Virol. 74:3682-3695(2000).
RN [6]
RP DISULFIDE BONDS, PHOSPHORYLATION AT SER-85, TOPOLOGY, AND MUTAGENESIS OF
RP SER-12; SER-25; SER-34; SER-36; SER-38; SER-47; SER-65; CYS-71; SER-77;
RP SER-85 AND SER-88.
RX PubMed=12885904; DOI=10.1128/jvi.77.16.8857-8871.2003;
RA Mercer J., Traktman P.;
RT "Investigation of structural and functional motifs within the vaccinia
RT virus A14 phosphoprotein, an essential component of the virion membrane.";
RL J. Virol. 77:8857-8871(2003).
CC -!- FUNCTION: Envelope protein which is a major component of the mature
CC virion (MV) membrane. Essential for membrane biogenesis. Is required,
CC together with A17, to form bona fide crescents, which can progress to
CC form the immature virion (IV) membrane. A14 and A17 form a lattice that
CC is stabilized by disulfide bonds and serves as an anchor within the
CC viral membrane to which several other proteins important in virion
CC structure and morphogenesis attach. {ECO:0000269|PubMed:10729144,
CC ECO:0000269|PubMed:9445029}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Interacts with A17.
CC {ECO:0000269|PubMed:10196242, ECO:0000269|PubMed:12885904}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}. Note=Component of the mature virion
CC (MV) membrane. {ECO:0000269|PubMed:10729144}.
CC -!- PTM: Phosphorylated by viral F10 kinase, phosphorylation state is
CC regulated by H1 phosphatase. {ECO:0000305|PubMed:10196242,
CC ECO:0000305|PubMed:12885904}.
CC -!- SIMILARITY: Belongs to the chordopoxvirinae A14 family. {ECO:0000305}.
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DR EMBL; AY243312; AAO89412.1; -; Genomic_DNA.
DR RefSeq; YP_233015.1; NC_006998.1.
DR PDB; 4N8V; X-ray; 2.50 A; C/F=61-69.
DR PDBsum; 4N8V; -.
DR SMR; Q76ZQ3; -.
DR iPTMnet; Q76ZQ3; -.
DR DNASU; 3707531; -.
DR GeneID; 3707531; -.
DR KEGG; vg:3707531; -.
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 InterPro; IPR008785; Poxvirus_A14.
DR Pfam; PF05767; Pox_A14; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Membrane;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW Viral envelope protein; Virion.
FT CHAIN 1..90
FT /note="Virion membrane protein A14"
FT /id="PRO_0000414115"
FT TOPO_DOM 1..10
FT /note="Intravirion"
FT /evidence="ECO:0000255"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..44
FT /note="Virion surface"
FT /evidence="ECO:0000255"
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 66..90
FT /note="Intravirion"
FT /evidence="ECO:0000255"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:12885904"
FT DISULFID 71
FT /note="Interchain"
FT /evidence="ECO:0000269|PubMed:12885904"
FT MUTAGEN 12
FT /note="S->A: Loss of functionality. No effect on
FT phosphorylation."
FT /evidence="ECO:0000269|PubMed:12885904"
FT MUTAGEN 25
FT /note="S->A: No effect on phosphorylation."
FT /evidence="ECO:0000269|PubMed:12885904"
FT MUTAGEN 34
FT /note="S->A: No effect on phosphorylation."
FT /evidence="ECO:0000269|PubMed:12885904"
FT MUTAGEN 36
FT /note="S->A: No effect on phosphorylation."
FT /evidence="ECO:0000269|PubMed:12885904"
FT MUTAGEN 38
FT /note="S->A: No effect on phosphorylation."
FT /evidence="ECO:0000269|PubMed:12885904"
FT MUTAGEN 47
FT /note="S->A: No effect on phosphorylation."
FT /evidence="ECO:0000269|PubMed:12885904"
FT MUTAGEN 65
FT /note="S->A: No effect on phosphorylation."
FT /evidence="ECO:0000269|PubMed:12885904"
FT MUTAGEN 71
FT /note="C->S: Loss of dimerization; loss of viral yield."
FT /evidence="ECO:0000269|PubMed:12885904"
FT MUTAGEN 77
FT /note="S->A: No effect on phosphorylation."
FT /evidence="ECO:0000269|PubMed:12885904"
FT MUTAGEN 85
FT /note="S->A: Loss of phosphorylation."
FT /evidence="ECO:0000269|PubMed:12885904"
FT MUTAGEN 88
FT /note="S->A: No effect on phosphorylation."
FT /evidence="ECO:0000269|PubMed:12885904"
SQ SEQUENCE 90 AA; 9994 MW; 98C751EF61678168 CRC64;
MDMMLMIGNY FSGVLIAGII LLILSCIFAF IDFSKSTSPT RTWKVLSIMA FILGIIITVG
MLIYSMWGKH CAPHRVSGVI HTNHSDISMN
