ID   IL1BP_CWPXB             Reviewed;         326 AA.
AC   Q04523; Q77DR6;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Interleukin-1-binding protein;
DE   AltName: Full=Protein B15;
DE   Flags: Precursor;
GN   OrderedLocusNames=CPXV209; ORFNames=B15R;
OS   Cowpox virus (strain Brighton Red) (CPV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus.
OX   NCBI_TaxID=265872;
OH   NCBI_TaxID=9913; Bos taurus (Bovine).
OH   NCBI_TaxID=9685; Felis catus (Cat) (Felis silvestris catus).
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=9785; Loxodonta africana (African elephant).
OH   NCBI_TaxID=29092; Microtus agrestis (Short-tailed field vole).
OH   NCBI_TaxID=10090; Mus musculus (Mouse).
OH   NCBI_TaxID=447135; Myodes glareolus (Bank vole) (Clethrionomys glareolus).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1339315; DOI=10.1016/0092-8674(92)90273-f;
RA   Spriggs M.K., Hruby D.E., Maliszewski C.R., Pickup D.J., Sims J.E.,
RA   Buller R.M.L., Vanslyke J.;
RT   "Vaccinia and cowpox viruses encode a novel secreted interleukin-1-binding
RT   protein.";
RL   Cell 71:145-152(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Dietrich F.S., Ray C.A., Sharma D.A., Allen A., Pickup D.J.;
RL   Submitted (MAY-2003) 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; M95202; AAA85776.1; -; Genomic_DNA.
DR   EMBL; AF482758; AAM13648.1; -; Genomic_DNA.
DR   RefSeq; NP_619990.1; NC_003663.2.
DR   SMR; Q04523; -.
DR   PRIDE; Q04523; -.
DR   GeneID; 1486088; -.
DR   KEGG; vg:1486088; -.
DR   Proteomes; UP000152733; 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; Early protein; Glycoprotein; Immunoglobulin domain; Repeat;
KW   Signal; Virion.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..326
FT                   /note="Interleukin-1-binding protein"
FT                   /id="PRO_0000015464"
FT   DOMAIN          24..115
FT                   /note="Ig-like C2-type 1"
FT   DOMAIN          122..208
FT                   /note="Ig-like C2-type 2"
FT   DOMAIN          221..322
FT                   /note="Ig-like C2-type 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        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;  36790 MW;  7AE206F4A7FD4F54 CRC64;
     MSIPPVIFLP IFFYSSFVQA FNAPECIDKG QYFASFMELE NEPVILPCPQ INTISSGYNI
     LDILWEKRGA DNDRIIPIDN GSNMLILNPT QSDSGIYICI TKNETYCDMM SLNLTIVSVS
     ESNIDLISYT QIVNERTTGE MVCPNINAFI ASNVNADIIW SGHRRLRNKR LRQRTPGIIT
     IEDVRKNDAG YYTCVLKYTY GDKTYDVTRI VKLEVRDRMI PPTMQLPDGV VTSIGSNLTI
     ACRVSLRPPT TDADVFWISN GMYYEEDDED GDGRISVANK IYTTDKRRVI TSRLKINPVK
     EEDATTFTCM AFTIPSISKT VTISIT