A34_VACCW
ID A34_VACCW Reviewed; 168 AA.
AC P24761; Q76ZP2;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Protein A34;
GN OrderedLocusNames=VACWR157; ORFNames=A34R, SALL4R;
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=2045793; DOI=10.1099/0022-1317-72-6-1349;
RA Smith G.L., Chan Y.S., Howard S.T.;
RT "Nucleotide sequence of 42 kbp of vaccinia virus strain WR from near the
RT right inverted terminal repeat.";
RL J. Gen. Virol. 72:1349-1376(1991).
RN [2]
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 [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 SUBCELLULAR LOCATION.
RX PubMed=1738204; DOI=10.1128/jvi.66.3.1610-1621.1992;
RA Duncan S.A., Smith G.L.;
RT "Identification and characterization of an extracellular envelope
RT glycoprotein affecting vaccinia virus egress.";
RL J. Virol. 66:1610-1621(1992).
RN [5]
RP INTERACTION WITH PROTEINS A36 AND B5.
RX PubMed=10074134; DOI=10.1128/jvi.73.4.2863-2875.1999;
RA Rottger S., Frischknecht F., Reckmann I., Smith G.L., Way M.;
RT "Interactions between vaccinia virus IEV membrane proteins and their roles
RT in IEV assembly and actin tail formation.";
RL J. Virol. 73:2863-2875(1999).
RN [6]
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 [7]
RP FUNCTION.
RX PubMed=18094186; DOI=10.1128/jvi.01969-07;
RA Perdiguero B., Lorenzo M.M., Blasco R.;
RT "Vaccinia virus A34 glycoprotein determines the protein composition of the
RT extracellular virus envelope.";
RL J. Virol. 82:2150-2160(2008).
CC -!- FUNCTION: Required for the envelopment of intracellular viral particles
CC and egress of enveloped virions from the infected cell.
CC {ECO:0000269|PubMed:18094186}.
CC -!- SUBUNIT: Interacts with proteins A36 AND B5.
CC {ECO:0000269|PubMed:10074134}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000305}; Single-pass type
CC II membrane protein {ECO:0000305}. Note=Present in the enveloped virion
CC (EV) membrane. {ECO:0000269|PubMed:1738204}.
CC -!- SIMILARITY: Belongs to the chordopoxvirinae A34 protein family.
CC {ECO:0000305}.
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DR EMBL; D11079; BAA01806.1; -; Genomic_DNA.
DR EMBL; M61187; AAA48331.1; -; Genomic_DNA.
DR EMBL; AY243312; AAO89436.1; -; Genomic_DNA.
DR PIR; JQ1770; JQ1770.
DR RefSeq; YP_233039.1; NC_006998.1.
DR SMR; P24761; -.
DR IntAct; P24761; 4.
DR MINT; P24761; -.
DR DNASU; 3707687; -.
DR GeneID; 3707687; -.
DR KEGG; vg:3707687; -.
DR Proteomes; UP000000344; Genome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR Gene3D; 3.10.100.10; -; 1.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR016187; CTDL_fold.
DR Pfam; PF00059; Lectin_C; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Membrane; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix; Virion.
FT CHAIN 1..168
FT /note="Protein A34"
FT /id="PRO_0000099320"
FT TOPO_DOM 1..14
FT /note="Intravirion"
FT /evidence="ECO:0000255"
FT TRANSMEM 15..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 38..168
FT /note="Virion surface"
FT /evidence="ECO:0000255"
FT DOMAIN 54..163
FT /note="C-type lectin"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 75..162
FT /evidence="ECO:0000250"
FT DISULFID 141..154
FT /evidence="ECO:0000250"
SQ SEQUENCE 168 AA; 19555 MW; 69F72EA9D971F19F CRC64;
MKSLNRQTVS RFKKLSVPAA IMMILSTIIS GIGTFLHYKE ELMPSACANG WIQYDKHCYL
DTNIKMSTDN AVYQCRKLRA RLPRPDTRHL RVLFSIFYKD YWVSLKKTND KWLDINNDKD
IDISKLTNFK QLNSTTDAEA CYIYKSGKLV KTVCKSTQSV LCVKKFYK