A27_VACCW
ID A27_VACCW Reviewed; 110 AA.
AC P11258; Q76ZP6;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Protein A27;
GN OrderedLocusNames=VACWR150; ORFNames=A27L;
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 [GENOMIC DNA].
RX PubMed=1856205; DOI=10.1016/s0021-9258(18)92757-2;
RA Amegadzie B.Y., Ahn B.-Y., Moss B.;
RT "Identification, sequence, and expression of the gene encoding a Mr 35,000
RT subunit of the vaccinia virus DNA-dependent RNA polymerase.";
RL J. Biol. Chem. 266:13712-13718(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2822962; DOI=10.1128/jvi.61.11.3550-3554.1987;
RA Rodriguez J.F., Esteban M.;
RT "Mapping and nucleotide sequence of the vaccinia virus gene that encodes a
RT 14-kilodalton fusion protein.";
RL J. Virol. 61:3550-3554(1987).
RN [3]
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 [4]
RP FUNCTION.
RX PubMed=3806791; DOI=10.1128/jvi.61.2.395-404.1987;
RA Rodriguez J.F., Paez E., Esteban M.;
RT "A 14,000-Mr envelope protein of vaccinia virus is involved in cell fusion
RT and forms covalently linked trimers.";
RL J. Virol. 61:395-404(1987).
RN [5]
RP FUNCTION.
RX PubMed=10640541; DOI=10.1099/0022-1317-81-1-47;
RA Sanderson C.M., Hollinshead M., Smith G.L.;
RT "The vaccinia virus A27L protein is needed for the microtubule-dependent
RT transport of intracellular mature virus particles.";
RL J. Gen. Virol. 81:47-58(2000).
RN [6]
RP SUBUNIT, AND MUTAGENESIS OF LEU-51 AND LEU-54.
RX PubMed=15913650; DOI=10.1016/j.jmb.2005.04.024;
RA Ho Y., Hsiao J.C., Yang M.H., Chung C.S., Peng Y.C., Lin T.H., Chang W.,
RA Tzou D.L.;
RT "The oligomeric structure of vaccinia viral envelope protein A27L is
RT essential for binding to heparin and heparan sulfates on cell surfaces: a
RT structural and functional approach using site-specific mutagenesis.";
RL J. Mol. Biol. 349:1060-1071(2005).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16509968; DOI=10.1186/1743-422x-3-10;
RA Yoder J.D., Chen T.S., Gagnier C.R., Vemulapalli S., Maier C.S.,
RA Hruby D.E.;
RT "Pox proteomics: mass spectrometry analysis and identification of Vaccinia
RT virion proteins.";
RL Virol. J. 3:10-10(2006).
RN [8]
RP INTERACTION WITH A17 AND A26.
RX PubMed=18842719; DOI=10.1128/jvi.01524-08;
RA Howard A.R., Senkevich T.G., Moss B.;
RT "Vaccinia virus A26 and A27 proteins form a stable complex tethered to
RT mature virions by association with the A17 transmembrane protein.";
RL J. Virol. 82:12384-12391(2008).
RN [9]
RP DISULFIDE BONDS.
RX PubMed=19369327; DOI=10.1128/jvi.02295-08;
RA Ching Y.C., Chung C.S., Huang C.Y., Hsia Y., Tang Y.L., Chang W.;
RT "Disulfide bond formation at the C termini of vaccinia virus A26 and A27
RT proteins does not require viral redox enzymes and suppresses
RT glycosaminoglycan-mediated cell fusion.";
RL J. Virol. 83:6464-6476(2009).
CC -!- FUNCTION: Structural protein involved in the envelopment of mature
CC virion (MV) to form the wrapped virion (WV). The wrapping consists of
CC the addition of Golgi membranes to the mature virion. Participates in
CC mature virion (MV) movement within the infected cell. May play an
CC indirect role in MV-cell fusion. {ECO:0000269|PubMed:10640541,
CC ECO:0000269|PubMed:3806791}.
CC -!- SUBUNIT: Homohexamers, covalently linked. Interacts with A17 and A26.
CC {ECO:0000269|PubMed:15913650, ECO:0000269|PubMed:18842719}.
CC -!- SUBCELLULAR LOCATION: Virion. Note=Located to the mature virion
CC membrane via interaction with protein A17.
CC -!- SIMILARITY: Belongs to the chordopoxvirinae A27 protein family.
CC {ECO:0000305}.
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DR EMBL; M61187; AAA48324.1; -; Genomic_DNA.
DR EMBL; M18173; AAA48248.1; -; Genomic_DNA.
DR EMBL; X57318; CAA40577.1; -; Genomic_DNA.
DR EMBL; AY243312; AAO89429.1; -; Genomic_DNA.
DR PIR; A27173; WMVZ14.
DR RefSeq; YP_233032.1; NC_006998.1.
DR PDB; 3VOP; X-ray; 2.20 A; A/B/C=21-84.
DR PDB; 5EOQ; X-ray; 1.95 A; A=31-40.
DR PDB; 5EOR; X-ray; 2.27 A; A=101-110.
DR PDBsum; 3VOP; -.
DR PDBsum; 5EOQ; -.
DR PDBsum; 5EOR; -.
DR BMRB; P11258; -.
DR SMR; P11258; -.
DR ABCD; P11258; 5 sequenced antibodies.
DR DNASU; 3707680; -.
DR GeneID; 3707680; -.
DR KEGG; vg:3707680; -.
DR Proteomes; UP000000344; Genome.
DR GO; GO:0019031; C:viral envelope; IEA:InterPro.
DR GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; IEA:InterPro.
DR InterPro; IPR003436; Chordopox_Fusion/A27.
DR Pfam; PF02346; Vac_Fusion; 1.
DR PRINTS; PR01847; VIRALFUSION.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Disulfide bond; Host-virus interaction;
KW Reference proteome; Virion.
FT CHAIN 1..110
FT /note="Protein A27"
FT /id="PRO_0000099212"
FT COILED 36..101
FT /evidence="ECO:0000255"
FT DISULFID 71
FT /note="Interchain (with C-441 in A26)"
FT /evidence="ECO:0000269|PubMed:19369327"
FT DISULFID 72
FT /note="Interchain (with C-442 in A26)"
FT /evidence="ECO:0000269|PubMed:19369327"
FT MUTAGEN 51
FT /note="L->A: Forms only tetramers, no hexamer."
FT /evidence="ECO:0000269|PubMed:15913650"
FT MUTAGEN 54
FT /note="L->A: Forms more tetramers than hexamers."
FT /evidence="ECO:0000269|PubMed:15913650"
FT CONFLICT 29..30
FT /note="EA -> DR (in Ref. 1; AAA48324 and 3; CAA40577)"
FT /evidence="ECO:0000305"
FT CONFLICT 34
FT /note="A -> Q (in Ref. 1; AAA48324 and 3; CAA40577)"
FT /evidence="ECO:0000305"
FT HELIX 47..83
FT /evidence="ECO:0007829|PDB:3VOP"
SQ SEQUENCE 110 AA; 12572 MW; BAA21A79740CF538 CRC64;
MDGTLFPGDD DLAIPATEFF STKAAKKPEA KREAIVKADE DDNEETLKQR LTNLEKKITN
VTTKFEQIEK CCKRNDEVLF RLENHAETLR AAMISLAKKI DVQTGRRPYE
