B5_VACCW
ID B5_VACCW Reviewed; 317 AA.
AC Q01227; Q76ZL8;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 02-JUN-2021, entry version 98.
DE RecName: Full=Protein B5;
DE AltName: Full=Plaque-size/host range protein;
DE Flags: Precursor;
GN Name=PS/HR; OrderedLocusNames=VACWR187; ORFNames=B5R;
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 [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 [3]
RP SUBCELLULAR LOCATION.
RX PubMed=1585649; DOI=10.1016/0042-6822(92)90535-w;
RA Engelstad M., Howard S.T., Smith G.L.;
RT "A constitutively expressed vaccinia gene encodes a 42-kDa glycoprotein
RT related to complement control factors that forms part of the extracellular
RT virus envelope.";
RL Virology 188:801-810(1992).
RN [4]
RP INTERACTION WITH PROTEIN A33.
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 [5]
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 [6]
RP FUNCTION.
RX PubMed=19264647; DOI=10.1099/vir.0.009092-0;
RA Roberts K.L., Breiman A., Carter G.C., Ewles H.A., Hollinshead M., Law M.,
RA Smith G.L.;
RT "Acidic residues in the membrane-proximal stalk region of vaccinia virus
RT protein B5 are required for glycosaminoglycan-mediated disruption of the
RT extracellular enveloped virus outer membrane.";
RL J. Gen. Virol. 90:1582-1591(2009).
RN [7]
RP FUNCTION.
RX PubMed=20200189; DOI=10.1099/vir.0.020677-0;
RA Breiman A., Smith G.L.;
RT "Vaccinia virus B5 protein affects the glycosylation, localization and
RT stability of the A34 protein.";
RL J. Gen. Virol. 91:1823-1827(2010).
RN [8]
RP PALMITOYLATION AT CYS-301 AND CYS-303, SUBCELLULAR LOCATION, INTERACTION
RP WITH A33; A34 AND ENVELOPE PHOSPHOLIPASE F13, AND MUTAGENESIS OF
RP 301-CYS--CYS-303.
RX PubMed=22238237; DOI=10.1099/vir.0.039016-0;
RA Lorenzo M.M., Sanchez-Puig J.M., Blasco R.;
RT "Mutagenesis of the palmitoylation site in vaccinia virus envelope
RT glycoprotein B5.";
RL J. Gen. Virol. 93:733-743(2012).
CC -!- FUNCTION: Plays a role in the dissolution of the outermost membrane of
CC extracellular enveloped virions (EV) to allow virion entry into host
CC cells. Participates also in wrapping mature virions (MV) to form
CC enveloped virions (EV). {ECO:0000269|PubMed:19264647,
CC ECO:0000269|PubMed:20200189}.
CC -!- SUBUNIT: Interacts with A33; this interaction is required for efficient
CC targeting of A33 and B5 into enveloped virions. Interacts with A34;
CC this interaction is required for the correct glycosylation, trafficking
CC and stability of A34 and B5 incorporation into extracellular enveloped
CC virions. Interacts with envelope phospholipase F13.
CC {ECO:0000269|PubMed:16912323, ECO:0000269|PubMed:22238237}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000269|PubMed:1585649,
CC ECO:0000269|PubMed:22238237}; Single-pass type I membrane protein
CC {ECO:0000305}. Host Golgi apparatus, host trans-Golgi network
CC {ECO:0000269|PubMed:22238237}. Note=B5 is found on enveloped virion
CC (EV) membranes.
CC -!- SIMILARITY: Belongs to the receptors of complement activation (RCA)
CC family. {ECO:0000305}.
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DR EMBL; D11079; BAA01835.1; -; Genomic_DNA.
DR EMBL; AY243312; AAO89466.1; -; Genomic_DNA.
DR PIR; JQ1799; JQ1799.
DR RefSeq; YP_233069.1; NC_006998.1.
DR SMR; Q01227; -.
DR IntAct; Q01227; 3.
DR MINT; Q01227; -.
DR ABCD; Q01227; 5 sequenced antibodies.
DR DNASU; 3707658; -.
DR GeneID; 3707658; -.
DR KEGG; vg:3707658; -.
DR Proteomes; UP000000344; Genome.
DR GO; GO:0044177; C:host cell Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0001848; F:complement binding; IEA:InterPro.
DR GO; GO:0045916; P:negative regulation of complement activation; IEA:InterPro.
DR CDD; cd00033; CCP; 3.
DR InterPro; IPR011176; CCP_VACV_C3/B5.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR Pfam; PF00084; Sushi; 3.
DR PIRSF; PIRSF002486; CIP_VAC_C3L; 1.
DR SMART; SM00032; CCP; 4.
DR SUPFAM; SSF57535; SSF57535; 3.
DR PROSITE; PS50923; SUSHI; 3.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Host Golgi apparatus; Lipoprotein; Membrane;
KW Palmitate; Reference proteome; Repeat; Signal; Sushi; Transmembrane;
KW Transmembrane helix; Virion.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..317
FT /note="Protein B5"
FT /id="PRO_0000006020"
FT TOPO_DOM 18..279
FT /note="Virion surface"
FT /evidence="ECO:0000255"
FT TRANSMEM 280..300
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 301..317
FT /note="Intravirion"
FT /evidence="ECO:0000255"
FT DOMAIN 19..74
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 75..126
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 127..184
FT /note="Sushi 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 185..239
FT /note="Sushi 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT LIPID 301
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000269|PubMed:22238237"
FT LIPID 303
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000269|PubMed:22238237"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 21..61
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 48..72
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 76..110
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 101..125
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 130..171
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 157..182
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 186..225
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 211..237
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT MUTAGEN 301..303
FT /note="CSC->SSS: Complete loss of palmytoylation."
FT /evidence="ECO:0000269|PubMed:22238237"
SQ SEQUENCE 317 AA; 35130 MW; 0816C384779E76B1 CRC64;
MKTISVVTLL CVLPAVVYST CTVPTMNNAK LTSTETSFND KQKVTFTCDQ GYHSSDPNAV
CETDKWKYEN PCKKMCTVSD YISELYNKPL YEVNSTMTLS CNGETKYFRC EEKNGNTSWN
DTVTCPNAEC QPLQLEHGSC QPVKEKYSFG EYMTINCDVG YEVIGASYIS CTANSWNVIP
SCQQKCDMPS LSNGLISGST FSIGGVIHLS CKSGFTLTGS PSSTCIDGKW NPVLPICVRT
NEEFDPVDDG PDDETDLSKL SKDVVQYEQE IESLEATYHI IIVALTIMGV IFLISVIVLV
CSCDKNNDQY KFHKLLP
