B5_VACCC
ID B5_VACCC Reviewed; 317 AA.
AC P21115;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 23-FEB-2022, entry version 98.
DE RecName: Full=Protein B5;
DE AltName: Full=Plaque-size/host range protein;
DE Flags: Precursor;
GN Name=PS/HR; ORFNames=B5R;
OS Vaccinia virus (strain Copenhagen) (VACV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX NCBI_TaxID=10249;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=2219722; DOI=10.1016/0042-6822(90)90294-2;
RA Goebel S.J., Johnson G.P., Perkus M.E., Davis S.W., Winslow J.P.,
RA Paoletti E.;
RT "The complete DNA sequence of vaccinia virus.";
RL Virology 179:247-266(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Goebel S.J., Johnson G.P., Perkus M.E., Davis S.W., Winslow J.P.,
RA Paoletti E.;
RT "Appendix to 'The complete DNA sequence of vaccinia virus'.";
RL Virology 179:517-563(1990).
CC -!- FUNCTION: Plays a role in the dissolution of the outermost membrane of
CC extracellular enveloped virions (EEV) to allow virion entry into host
CC cells. Participates also in wrapping intracellular mature virions (IMV)
CC to form intracellular enveloped virions (IEV) (By similarity).
CC {ECO:0000250}.
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; M35027; AAA48201.1; -; Genomic_DNA.
DR PIR; D42526; D42526.
DR SMR; P21115; -.
DR Proteomes; UP000008269; 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 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_0000006017"
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: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; 35109 MW; B66E3E29EF3C2BA7 CRC64;
MKTISVVTLL CVLPAVVYST CTVPTMNNAK LTSTETSFNN NQKVTFTCDQ GYHSSDPNAV
CETDKWKYEN PCKKMCTVSD YISELYNKPL YEVNSTMTLS CNGETKYFRC EEKNGNTSWN
DTVTCPNAEC QPLQLEHGSC QPVKEKYSFG EYMTINCDVG YEVIGASYIS CTANSWNVIP
SCQQKCDIPS LSNGLISGST FSIGGVIHLS CKSGFILTGS PSSTCIDGKW NPVLPICVRT
NEEFDPVDDG PDDETDLSKL SKDVVQYEQE IESLEATYHI IIVALTIMGV IFLISVIVLV
CSCDKNNDQY KFHKLLP
