SANS_VACCD
ID SANS_VACCD Reviewed; 351 AA.
AC P23998;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 12-AUG-2020, entry version 92.
DE RecName: Full=Surface antigen S;
DE Short=S antigen;
DE Flags: Precursor;
GN ORFNames=B19R;
OS Vaccinia virus (strain Dairen I) (VACV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX NCBI_TaxID=10250;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2196742; DOI=10.1016/0042-6822(90)90524-u;
RA Ueda Y., Morikawa S., Matsuura Y.;
RT "Identification and nucleotide sequence of the gene encoding a surface
RT antigen induced by vaccinia virus.";
RL Virology 177:588-594(1990).
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; D90076; BAA14116.1; -; Genomic_DNA.
DR PIR; A35522; SAVZVV.
DR SMR; P23998; -.
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; 2.
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..19
FT /evidence="ECO:0000255"
FT CHAIN 20..351
FT /note="Surface antigen S"
FT /id="PRO_0000015466"
FT DOMAIN 65..137
FT /note="Ig-like C2-type 1"
FT DOMAIN 155..237
FT /note="Ig-like C2-type 2"
FT DOMAIN 246..345
FT /note="Ig-like V-type"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 73..129
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 172..221
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 272..333
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 351 AA; 40702 MW; 20997CB67D39E7DB CRC64;
MTMKMMVHIY FVSLLLLLFH SYAIDIENEI TEFFNKMRDT LPAKDSKWLN PACMFGGTMN
DIAALGEPFS AKCPPIEDSL LSHRYKDYVV KWERLEKNRR RQVSNKRVKH GDLWIANYTS
KFSNRRYLCT VTTKNGDCVQ GIVRSHIKKP PSCIPKTYEL GTHDKYGIDL YCGILYAKHY
NNITWYKDNK EINIDDIKYS QTGKKLIIHN PELEDSGRYN CYVHYDDVRI KNDIVVSRCK
ILTVIPSQDH RFKLILDPKI NVTIGEPANI TCTAVSTSLL IDDVLIEWEN PSGWLIGFDF
DVYSVLTSRG GITEATLYFE NVTEEYIGNT YKCRGHNYYF EKTLTTTVVL E