ID   IL1BP_VACCA             Reviewed;         326 AA.
AC   O57261;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   23-FEB-2022, entry version 94.
DE   RecName: Full=Interleukin-1-binding protein;
DE   AltName: Full=Protein B16;
DE   Flags: Precursor;
GN   OrderedLocusNames=MVA184R, ACAM3000_MVA_184;
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: Binds interleukin-1 and possibly interleukin-6. Could prevent
CC       these cytokines reaching their natural receptors. In consequence the
CC       inflammatory response would be diminished and virus replication
CC       enhanced.
CC   -!- SUBCELLULAR LOCATION: Virion. Host cell surface. Note=Or secretory
CC       glycoprotein.
CC   -!- SIMILARITY: Belongs to the interleukin-1 receptor family.
CC       {ECO:0000305}.
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DR   EMBL; U94848; AAB96555.1; -; Genomic_DNA.
DR   EMBL; AY603355; AAT10580.1; -; Genomic_DNA.
DR   PIR; T37450; T37450.
DR   SMR; O57261; -.
DR   Proteomes; UP000159908; Genome.
DR   Proteomes; UP000172909; Genome.
DR   GO; GO:0044228; C:host cell surface; IEA:UniProtKB-SubCell.
DR   GO; GO:0019966; F:interleukin-1 binding; IEA:InterPro.
DR   GO; GO:0004908; F:interleukin-1 receptor activity; IEA:InterPro.
DR   GO; GO:0019048; P:modulation by virus of host process; IEA:InterPro.
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; IPR003598; Ig_sub2.
DR   InterPro; IPR004078; IL-1-bd.
DR   InterPro; IPR015621; IL-1_rcpt_fam.
DR   InterPro; IPR004074; IL-1_rcpt_I/II-typ.
DR   InterPro; IPR013151; Immunoglobulin.
DR   PANTHER; PTHR11890; PTHR11890; 1.
DR   Pfam; PF00047; ig; 1.
DR   PRINTS; PR01540; INTRLEUKN1BP.
DR   PRINTS; PR01536; INTRLKN1R12F.
DR   SMART; SM00409; IG; 3.
DR   SMART; SM00408; IGc2; 3.
DR   SUPFAM; SSF48726; SSF48726; 3.
DR   PROSITE; PS50835; IG_LIKE; 3.
PE   3: Inferred from homology;
KW   Disulfide bond; Glycoprotein; Immunoglobulin domain; Repeat; Signal;
KW   Virion.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..326
FT                   /note="Interleukin-1-binding protein"
FT                   /id="PRO_0000015461"
FT   DOMAIN          24..115
FT                   /note="Ig-like 1"
FT   DOMAIN          122..212
FT                   /note="Ig-like 2"
FT   DOMAIN          221..322
FT                   /note="Ig-like 3"
FT   CARBOHYD        80
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        103
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        113
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        206
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        237
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   DISULFID        48..99
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        143..194
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        242..309
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   326 AA;  36595 MW;  DC44B776EA235F0A CRC64;
     MSILPVIFLS IFFYSSFVQT FNAPECIDKG QYFASFMELE NEPVILPCPQ INTLSSGYNI
     LDILWEKRGA DNDRIIPIDN GSNMLILNPT QSDSGIYICI TTNETYCDMM SLNLTIVSVS
     ESNIDLISYP QIVNERSTGE MVCPNINAFI ASNVNADIIW SGHRRLRNKR LKQRTPGIIT
     IEDVRKNDAG YYTCVLEYIY GGKTYNVTRI VKLEVRDKII PSTMQLPEGV VTSIGSNLTI
     ACRVSLRPPT TDADVFWISN GMYYEEDDGD GDGRISVANK IYMTDKRRVI TSRLNINPVK
     EEDATTFTCM AFTIPSISKT VTVSIT