I18BP_MOUSE
ID I18BP_MOUSE Reviewed; 193 AA.
AC Q9Z0M9; Q4FJR8; Q4FK87; Q9CV30; Q9QUH2; Q9Z0N0;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Interleukin-18-binding protein;
DE Short=IL-18BP;
DE AltName: Full=Interferon gamma-inducing factor-binding protein;
DE Flags: Precursor;
GN Name=Il18bp; Synonyms=Igifbp;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 29-33; 53-56; 94-139;
RP 157-160 AND 164-169.
RC STRAIN=CD-1; TISSUE=Serum;
RX PubMed=10094485; DOI=10.1016/s0014-5793(99)00148-9;
RA Aizawa Y., Akita K., Taniai M., Torigoe K., Mori T., Nishida Y., Ushio S.,
RA Nukada Y., Tanimoto T., Ikegami H., Ikeda M., Kurimoto M.;
RT "Cloning and expression of interleukin-18 binding protein.";
RL FEBS Lett. 445:338-342(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10023777; DOI=10.1016/s1074-7613(00)80013-8;
RA Novick D., Kim S.-H., Fantuzzi G., Reznikov L.L., Dinarello C.A.,
RA Rubinstein M.;
RT "Interleukin-18 binding protein: a novel modulator of the Th1 cytokine
RT response.";
RL Immunity 10:127-136(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Skin;
RX PubMed=10329540; DOI=10.1006/viro.1999.9676;
RA Xiang Y., Moss B.;
RT "Identification of human and mouse homologs of the MC51L-53L-54L family of
RT secreted glycoproteins encoded by the Molluscum contagiosum poxvirus.";
RL Virology 257:297-302(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, Small intestine, and Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J.,
RA Wiemann S., Schick M., Korn B.;
RT "Cloning of mouse full open reading frames in Gateway(R) system entry
RT vector (pDONR201).";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Binds to IL-18 and inhibits its activity. Functions as an
CC inhibitor of the early TH1 cytokine response (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD17193.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC Sequence=AAD17194.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB019505; BAA76375.1; -; mRNA.
DR EMBL; AF110802; AAD17193.1; ALT_SEQ; mRNA.
DR EMBL; AF110803; AAD17194.1; ALT_INIT; mRNA.
DR EMBL; AF122907; AAD41052.1; -; mRNA.
DR EMBL; AK009721; BAB26462.1; -; mRNA.
DR EMBL; AK003370; BAB22744.1; -; mRNA.
DR EMBL; AK008452; BAB25677.1; -; mRNA.
DR EMBL; AK009877; BAB26558.1; -; mRNA.
DR EMBL; CT010164; CAJ18372.1; -; mRNA.
DR EMBL; CT010334; CAJ18542.1; -; mRNA.
DR EMBL; CH466531; EDL16557.1; -; Genomic_DNA.
DR EMBL; CH466531; EDL16558.1; -; Genomic_DNA.
DR EMBL; CH466531; EDL16559.1; -; Genomic_DNA.
DR EMBL; BC018332; AAH18332.1; -; mRNA.
DR CCDS; CCDS21522.1; -.
DR RefSeq; NP_034661.1; NM_010531.1.
DR AlphaFoldDB; Q9Z0M9; -.
DR SMR; Q9Z0M9; -.
DR STRING; 10090.ENSMUSP00000091685; -.
DR GlyGen; Q9Z0M9; 4 sites.
DR PhosphoSitePlus; Q9Z0M9; -.
DR CPTAC; non-CPTAC-3552; -.
DR MaxQB; Q9Z0M9; -.
DR PaxDb; Q9Z0M9; -.
DR PeptideAtlas; Q9Z0M9; -.
DR PRIDE; Q9Z0M9; -.
DR ProteomicsDB; 267078; -.
DR Antibodypedia; 30767; 464 antibodies from 34 providers.
DR DNASU; 16068; -.
DR Ensembl; ENSMUST00000094134; ENSMUSP00000091685; ENSMUSG00000070427.
DR Ensembl; ENSMUST00000209844; ENSMUSP00000148080; ENSMUSG00000070427.
DR GeneID; 16068; -.
DR KEGG; mmu:16068; -.
DR UCSC; uc009iqd.1; mouse.
DR CTD; 10068; -.
DR MGI; MGI:1333800; Il18bp.
DR VEuPathDB; HostDB:ENSMUSG00000070427; -.
DR eggNOG; ENOG502SYZY; Eukaryota.
DR GeneTree; ENSGT00390000004026; -.
DR HOGENOM; CLU_131866_0_0_1; -.
DR InParanoid; Q9Z0M9; -.
DR OMA; PTAKQCP; -.
DR PhylomeDB; Q9Z0M9; -.
DR TreeFam; TF337962; -.
DR BioGRID-ORCS; 16068; 4 hits in 71 CRISPR screens.
DR ChiTaRS; Il18bp; mouse.
DR PRO; PR:Q9Z0M9; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9Z0M9; protein.
DR Bgee; ENSMUSG00000070427; Expressed in granulocyte and 131 other tissues.
DR ExpressionAtlas; Q9Z0M9; baseline and differential.
DR Genevisible; Q9Z0M9; MM.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0042007; F:interleukin-18 binding; ISS:UniProtKB.
DR GO; GO:0042088; P:T-helper 1 type immune response; ISS:UniProtKB.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR039681; IL18BP.
DR PANTHER; PTHR14292; PTHR14292; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Reference proteome; Secreted; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000269|PubMed:10094485"
FT CHAIN 29..193
FT /note="Interleukin-18-binding protein"
FT /id="PRO_0000014779"
FT DOMAIN 60..161
FT /note="Ig-like C2-type"
FT REGION 172..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 81..145
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 172
FT /note="S -> P (in Ref. 2; AAD17194, 5; CAJ18542 and 7;
FT AAH18332)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 193 AA; 21257 MW; D7AD4B0AB07C8248 CRC64;
MTMRHCWTAG PSSWWVLLLY VHVILARATS APQTTATVLT GSSKDPCSSW SPAVPTKQYP
ALDVIWPEKE VPLNGTLTLS CTACSRFPYF SILYWLGNGS FIEHLPGRLK EGHTSREHRN
TSTWLHRALV LEELSPTLRS TNFSCLFVDP GQVAQYHIIL AQLWDGLKTA PSPSQETLSS
HSPVSRSAGP GVA
