ID   SANS_VARV               Reviewed;         354 AA.
AC   P0DST2; P33795;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   16-OCT-2019, sequence version 1.
DT   29-SEP-2021, entry version 10.
DE   RecName: Full=Surface antigen S;
DE            Short=S antigen;
DE   Flags: Precursor;
GN   ORFNames=B19R, B20R;
OS   Variola virus.
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus.
OX   NCBI_TaxID=10255;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Bangladesh-1975;
RX   PubMed=8264798; DOI=10.1038/366748a0;
RA   Massung R.F., Esposito J.J., Liu L.I., Qi J., Utterback T.R., Knight J.C.,
RA   Aubin L., Yuran T.E., Parsons J.M., Loparev V.N., Selivanov N.A.,
RA   Cavallaro K.F., Kerlavage A.R., Mahy B.W.J., Venter J.C.;
RT   "Potential virulence determinants in terminal regions of variola smallpox
RT   virus genome.";
RL   Nature 366:748-751(1993).
CC   -!- FUNCTION: May bind interleukin-1 and/or interleukin-6 and prevent these
CC       cytokines reaching their natural receptors. In consequence the
CC       inflammatory response would be diminished and virus replication
CC       enhanced.
CC   -!- SUBCELLULAR LOCATION: Host cell surface. Note=Induced on the surface of
CC       vaccinia virus-infected cells.
CC   -!- SIMILARITY: Belongs to the interleukin-1 receptor family.
CC       {ECO:0000305}.
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DR   EMBL; L22579; AAA60926.1; -; Genomic_DNA.
DR   PIR; T28616; T28616.
DR   RefSeq; NP_042232.1; NC_001611.1.
DR   SMR; P0DST2; -.
DR   GeneID; 1486551; -.
DR   KEGG; vg:1486551; -.
DR   Proteomes; UP000119805; Genome.
DR   GO; GO:0044228; C:host cell surface; IEA:UniProtKB-SubCell.
DR   Gene3D; 2.60.40.10; -; 3.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR015621; IL-1_rcpt_fam.
DR   InterPro; IPR013151; Immunoglobulin.
DR   PANTHER; PTHR11890; PTHR11890; 1.
DR   Pfam; PF00047; ig; 1.
DR   Pfam; PF13895; Ig_2; 1.
DR   SMART; SM00409; IG; 3.
DR   SUPFAM; SSF48726; SSF48726; 2.
DR   PROSITE; PS50835; IG_LIKE; 2.
PE   3: Inferred from homology;
KW   Disulfide bond; Early protein; Glycoprotein; Immunoglobulin domain; Repeat;
KW   Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..354
FT                   /note="Surface antigen S"
FT                   /id="PRO_0000448109"
FT   DOMAIN          68..150
FT                   /note="Ig-like C2-type 1"
FT   DOMAIN          158..240
FT                   /note="Ig-like C2-type 2"
FT   DOMAIN          249..348
FT                   /note="Ig-like V-type"
FT   CARBOHYD        120
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        124
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        185
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        272
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        324
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   DISULFID        76..132
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        175..224
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        275..336
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   354 AA;  40868 MW;  F9CB76356732E722 CRC64;
     MMKMTMKMMV HIYFVSLLLL LFHSYAIDIE NEITDFFNKM KDTLPAKDSK WLNPTCIFGG
     TMNNMAAIGE PFSAKCPPIE DSLLSRRYIN KDNVVNWEKI GKTRRPLNRR VKNGDLWIAN
     YTSNDSHRMY LCTVITKNGD CIQGIVRSHV RKPSSCIPEI YELGTHDKYG IDLYCGIIYA
     KHYNNITWYK DNKEINIDDI KYSQTGKELI IHNPALEDSG RYDCYVHYDD VRIKNDIVVS
     RCKILTVIPS QDHRFKLILD SKINVIIGEP ANITCTAVST SLLFDDVLIE WENPSGWLIG
     FDFDVYSVLT SRGGITEATL YFKNVTEEYI GNTYKCRGHN YYFEKTLTTT VVLE