ID   B5_VACCA                Reviewed;         317 AA.
AC   O57254;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   07-APR-2021, entry version 81.
DE   RecName: Full=Protein B5;
DE   AltName: Full=Plaque-size/host range protein;
DE   Flags: Precursor;
GN   Name=PS/HR; OrderedLocusNames=MVA173R, ACAM3000_MVA_173;
OS   Vaccinia virus (strain Ankara) (VACV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX   NCBI_TaxID=126794;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=9601507; DOI=10.1006/viro.1998.9123;
RA   Antoine G., Scheiflinger F., Dorner F., Falkner F.G.;
RT   "The complete genomic sequence of the modified vaccinia Ankara strain:
RT   comparison with other orthopoxviruses.";
RL   Virology 244:365-396(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate Acambis 3000;
RA   Esposito J.J., Frace M., Sammons S.A., Olsen-Rasmussen M.S., Osborne J.,
RA   Khristova M., Wohlhueter R.M.;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Regulation of plaque size and host range.
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:0000250|UniProtKB:Q01227}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000250|UniProtKB:Q01227};
CC       Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q01227}.
CC       Host Golgi apparatus, host trans-Golgi network
CC       {ECO:0000250|UniProtKB:Q01227}. Note=B5 is found on enveloped virion
CC       (EV) membranes. {ECO:0000250|UniProtKB:Q01227}.
CC   -!- SIMILARITY: Belongs to the receptors of complement activation (RCA)
CC       family. {ECO:0000305}.
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DR   EMBL; U94848; AAB96547.1; -; Genomic_DNA.
DR   EMBL; AY603355; AAT10569.1; -; Genomic_DNA.
DR   PIR; T37442; T37442.
DR   SMR; O57254; -.
DR   Proteomes; UP000159908; Genome.
DR   Proteomes; UP000172909; 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   3: Inferred from homology;
KW   Disulfide bond; Host Golgi apparatus; Lipoprotein; Membrane; Palmitate;
KW   Repeat; Signal; Sushi; Transmembrane; Transmembrane helix; Virion.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..317
FT                   /note="Protein B5"
FT                   /id="PRO_0000006016"
FT   TRANSMEM        280..300
FT                   /note="Helical"
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:0000250|UniProtKB:Q01227"
FT   LIPID           303
FT                   /note="S-palmitoyl cysteine; by host"
FT                   /evidence="ECO:0000250|UniProtKB:Q01227"
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"
SQ   SEQUENCE   317 AA;  35078 MW;  A834466D7D3F6304 CRC64;
     MKTISVVTLL CVLPAVVYST CTVPTMNNAK LTSTETSFNN NQKVTFTCDQ GYHSSDPNAV
     CETDKWKYEN PCKKMCTVSD YISELYNKPL YEVNSTMTLS CNGETKYFRC EEKNGNTSWN
     DTVTCPNAEC QPLQLEHGSC QPVKEKYSFG EYITINCDVG YEVIGASYIS CTANSWNVIP
     SCQQKCDIPS LSNGLISGST FSIGGVIHLS CKSGFILTGS PSSTCIDGKW NPILPTCVRS
     NEKFDPVDDG PDDETDLSKL SKDVVQYEQE IESLEATYHI IIVALTIMGV IFLISVIVLV
     CSCDKNNDQY KFHKLLP