A33_VACCW
ID A33_VACCW Reviewed; 185 AA.
AC P68617; P21056; Q76ZP3;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 58.
DE RecName: Full=Protein A33;
GN OrderedLocusNames=VACWR156; ORFNames=A33R;
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=8648710; DOI=10.1128/jvi.70.6.3753-3762.1996;
RA Roper R.L., Payne L.G., Moss B.;
RT "Extracellular vaccinia virus envelope glycoprotein encoded by the A33R
RT gene.";
RL J. Virol. 70:3753-3762(1996).
RN [5]
RP FUNCTION.
RX PubMed=9557708; DOI=10.1128/jvi.72.5.4192-4204.1998;
RA Roper R.L., Wolffe E.J., Weisberg A., Moss B.;
RT "The envelope protein encoded by the A33R gene is required for formation of
RT actin-containing microvilli and efficient cell-to-cell spread of vaccinia
RT virus.";
RL J. Virol. 72:4192-4204(1998).
RN [6]
RP INTERACTION WITH PROTEIN A36.
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 [7]
RP FUNCTION.
RX PubMed=11119600; DOI=10.1128/jvi.75.1.303-310.2001;
RA Wolffe E.J., Weisberg A.S., Moss B.;
RT "The vaccinia virus A33R protein provides a chaperone function for viral
RT membrane localization and tyrosine phosphorylation of the A36R protein.";
RL J. Virol. 75:303-310(2001).
RN [8]
RP FUNCTION.
RX PubMed=14581563; DOI=10.1128/jvi.77.22.12266-12275.2003;
RA Katz E., Ward B.M., Weisberg A.S., Moss B.;
RT "Mutations in the vaccinia virus A33R and B5R envelope proteins that
RT enhance release of extracellular virions and eliminate formation of actin-
RT containing microvilli without preventing tyrosine phosphorylation of the
RT A36R protein.";
RL J. Virol. 77:12266-12275(2003).
RN [9]
RP INTERACTION WITH B5.
RX PubMed=16912323; DOI=10.1128/jvi.00598-06;
RA Perdiguero B., Blasco R.;
RT "Interaction between vaccinia virus extracellular virus envelope A33 and B5
RT glycoproteins.";
RL J. Virol. 80:8763-8777(2006).
RN [10]
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 [11]
RP SUBUNIT.
RX PubMed=20947114; DOI=10.1016/j.virol.2010.09.021;
RA Chan W.M., Kalkanoglu A.E., Ward B.M.;
RT "The inability of vaccinia virus A33R protein to form intermolecular
RT disulfide-bonded homodimers does not affect the production of infectious
RT extracellular virus.";
RL Virology 408:109-118(2010).
RN [12]
RP DOMAIN.
RX PubMed=20302896; DOI=10.1016/j.virusres.2010.03.004;
RA Krupovic M., Cvirkaite-Krupovic V., Bamford D.H.;
RT "Protein A33 responsible for antibody-resistant spread of Vaccinia virus is
RT homologous to C-type lectin-like proteins.";
RL Virus Res. 151:97-101(2010).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 90-185.
RX PubMed=20032175; DOI=10.1128/jvi.02247-09;
RA Su H.P., Singh K., Gittis A.G., Garboczi D.N.;
RT "The structure of the poxvirus A33 protein reveals a dimer of unique C-type
RT lectin-like domains.";
RL J. Virol. 84:2502-2510(2010).
CC -!- FUNCTION: Coordinates the incorporation of A36 into wrapped enveloped
CC virion (EV) membranes and, subsequently, the production of actin tails.
CC Therefore plays an essential role in efficient cell-to-cell spread of
CC viral particles. {ECO:0000269|PubMed:11119600,
CC ECO:0000269|PubMed:14581563, ECO:0000269|PubMed:9557708}.
CC -!- SUBUNIT: Homodimer, disulfide-linked. Interacts with protein B5.
CC Interacts (via C-terminus) with protein A36.
CC {ECO:0000269|PubMed:10074134, ECO:0000269|PubMed:16912323,
CC ECO:0000269|PubMed:20947114}.
CC -!- INTERACTION:
CC P68617; P04021: VACWR052; NbExp=2; IntAct=EBI-7133633, EBI-7736497;
CC P68617; P68619: VACWR159; NbExp=7; IntAct=EBI-7133633, EBI-7133540;
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000305}; Single-pass type
CC II membrane protein {ECO:0000305}. Host membrane {ECO:0000305}; Single-
CC pass type II membrane protein {ECO:0000305}. Note=Component of the
CC enveloped virion (EV) membrane. {ECO:0000269|PubMed:8648710}.
CC -!- SIMILARITY: Belongs to the chordopoxvirinae A33 protein family.
CC {ECO:0000305}.
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DR EMBL; D11079; BAA01805.1; -; Genomic_DNA.
DR EMBL; M61187; AAA48330.1; -; Genomic_DNA.
DR EMBL; X57318; CAA40583.1; -; Genomic_DNA.
DR EMBL; AY243312; AAO89435.1; -; Genomic_DNA.
DR PIR; H42520; H42520.
DR RefSeq; YP_233038.1; NC_006998.1.
DR PDB; 3K7B; X-ray; 2.10 A; A/B=90-185.
DR PDBsum; 3K7B; -.
DR SMR; P68617; -.
DR IntAct; P68617; 4.
DR MINT; P68617; -.
DR ABCD; P68617; 9 sequenced antibodies.
DR DNASU; 3707686; -.
DR GeneID; 3707686; -.
DR KEGG; vg:3707686; -.
DR EvolutionaryTrace; P68617; -.
DR Proteomes; UP000000344; Genome.
DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
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 Gene3D; 3.10.100.10; -; 1.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR009238; Chordopox_A33R.
DR Pfam; PF05966; Chordopox_A33R; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Glycoprotein; Host membrane; Membrane;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix;
KW Viral envelope protein; Virion.
FT CHAIN 1..185
FT /note="Protein A33"
FT /id="PRO_0000099317"
FT TOPO_DOM 1..33
FT /note="Intravirion"
FT /evidence="ECO:0000250"
FT TRANSMEM 34..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 57..185
FT /note="Virion surface"
FT /evidence="ECO:0000250"
FT REGION 98..185
FT /note="C-type lectin-like domain"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 62
FT /note="Interchain"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:3K7B"
FT STRAND 108..117
FT /evidence="ECO:0007829|PDB:3K7B"
FT HELIX 119..128
FT /evidence="ECO:0007829|PDB:3K7B"
FT HELIX 136..139
FT /evidence="ECO:0007829|PDB:3K7B"
FT HELIX 145..148
FT /evidence="ECO:0007829|PDB:3K7B"
FT STRAND 156..159
FT /evidence="ECO:0007829|PDB:3K7B"
FT STRAND 176..183
FT /evidence="ECO:0007829|PDB:3K7B"
SQ SEQUENCE 185 AA; 20506 MW; 201CF65C2D2076A4 CRC64;
MMTPENDEEQ TSVFSATVYG DKIQGKNKRK RVIGLCIRIS MVISLLSMIT MSAFLIVRLN
QCMSANEAAI TDAAVAVAAA SSTHRKVASS TTQYDHKESC NGLYYQGSCY ILHSDYQLFS
DAKANCTAES STLPNKSDVL ITWLIDYVED TWGSDGNPIT KTTSDYQDSD VSQEVRKYFC
VKTMN