IL1BP_VACCW
ID IL1BP_VACCW Reviewed; 326 AA.
AC P25212; Q76ZK8;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Interleukin-1-binding protein;
DE AltName: Full=Protein B15;
DE Flags: Precursor;
GN OrderedLocusNames=VACWR197; ORFNames=B15R;
OS Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain
OS WR)).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX NCBI_TaxID=10254;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2045793; DOI=10.1099/0022-1317-72-6-1349;
RA Smith G.L., Chan Y.S., Howard S.T.;
RT "Nucleotide sequence of 42 kbp of vaccinia virus strain WR from near the
RT right inverted terminal repeat.";
RL J. Gen. Virol. 72:1349-1376(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1826022; DOI=10.1099/0022-1317-72-3-511;
RA Smith G.L., Chan Y.S.;
RT "Two vaccinia virus proteins structurally related to the interleukin-1
RT receptor and the immunoglobulin superfamily.";
RL J. Gen. Virol. 72:511-518(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Esposito J.J., Frace A.M., Sammons S.A., Olsen-Rasmussen M., Osborne J.,
RA Wohlhueter R.;
RT "Sequencing of the coding region of Vaccinia-WR to an average 9-fold
RT redundancy and an error rate of 0.16/10kb.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MOUSE IL1B.
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).
CC -!- FUNCTION: May reduce the host inflammatory response by interacting with
CC inteleukin-1 beta (Il1b) and thus decreasing the association between
CC IL1B and its cellular receptor. {ECO:0000269|PubMed:1339315}.
CC -!- SUBUNIT: Interacts with mouse Il1b. {ECO:0000269|PubMed:1339315}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1339315}.
CC -!- SIMILARITY: Belongs to the interleukin-1 receptor family.
CC {ECO:0000305}.
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DR EMBL; D11079; BAA01845.1; -; Genomic_DNA.
DR EMBL; D01018; BAA00825.1; -; Genomic_DNA.
DR EMBL; AY243312; AAO89476.1; -; Genomic_DNA.
DR PIR; A38472; WMVZ15.
DR RefSeq; YP_233079.1; NC_006998.1.
DR SMR; P25212; -.
DR DNASU; 3707574; -.
DR GeneID; 3707574; -.
DR KEGG; vg:3707574; -.
DR Proteomes; UP000000344; Genome.
DR GO; GO:0005576; C:extracellular region; 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 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Host-virus interaction;
KW Immunoglobulin domain; Reference proteome; Repeat; Secreted; Signal;
KW Viral immunoevasion.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..326
FT /note="Interleukin-1-binding protein"
FT /id="PRO_0000015463"
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; 36594 MW; 7FF03F64600BE390 CRC64;
MSILPVIFLS IFFYSSFVQT FNAPECIDKG QYFASFMELE NEPVILPCPQ INTLSSGYNI
LDILWEKRGA DNDRIIPIDN GSNMLILNPT QSDSGIYICI TTNETYCDMM SLNLTIVSVS
ESNIDLISYP QIVNERSTGE MVCPNINAFI ASNVNADIIW SGHRRLRNKR LKQRTPGIIT
IEDVRKNDAG YYTCVLEYIY GGKTYNVTRI VKLEVRDKII PSTMQLPDGI VTSIGSNLTI
ACRVSLRPPT TDADVFWISN GMYYEEDDGD GNGRISVANK IYMTDKRRVI TSRLNINPVK
EEDATTFTCM AFTIPSISKT VTVSIT
