CHIL4_MOUSE
ID CHIL4_MOUSE Reviewed; 402 AA.
AC Q91Z98; Q3V2C9; Q8VH43; Q8VHG1;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Chitinase-like protein 4;
DE AltName: Full=Chitinase-3-like protein 4;
DE AltName: Full=Secreted protein Ym2;
DE Flags: Precursor;
GN Name=Chil4; Synonyms=Chi3l4, Ym2;
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], PROTEIN SEQUENCE OF 22-33, FUNCTION,
RP SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=BALB/cJ;
RX PubMed=11553626; DOI=10.1074/jbc.m106223200;
RA Webb D.C., McKenzie A.N.J., Foster P.S.;
RT "Expression of the Ym2 lectin-binding protein is dependent on interleukin
RT (IL)-4 and IL-13 signal transduction: identification of a novel allergy-
RT associated protein.";
RL J. Biol. Chem. 276:41969-41976(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=129/Ola, and BALB/cJ; TISSUE=Stomach;
RA Su W.B., Chang N.-C.A.;
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=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 [4]
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).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 203-392, AND TISSUE SPECIFICITY.
RC STRAIN=129/SvJ;
RX PubMed=9828134; DOI=10.1006/geno.1998.5593;
RA Jin H.M., Copeland N.G., Gilbert D.J., Jenkins N.A., Kirkpatrick R.B.,
RA Rosenberg M.;
RT "Genetic characterization of the murine Ym1 gene and identification of a
RT cluster of highly homologous genes.";
RL Genomics 54:316-322(1998).
RN [6]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15148607; DOI=10.1007/s00418-004-0654-4;
RA Nio J., Fujimoto W., Konno A., Kon Y., Owhashi M., Iwanaga T.;
RT "Cellular expression of murine Ym1 and Ym2, chitinase family proteins, as
RT revealed by in situ hybridization and immunohistochemistry.";
RL Histochem. Cell Biol. 121:473-482(2004).
CC -!- FUNCTION: Has low chemotactic activity for eosinophils. May play a role
CC in inflammation and allergy. Has no chitinase activity.
CC {ECO:0000269|PubMed:11553626}.
CC -!- SUBCELLULAR LOCATION: Secreted. Cytoplasm. Note=Detected in the
CC cytoplasm of keratinocytes.
CC -!- TISSUE SPECIFICITY: Detected in stratified squamous epithelium in the
CC junctional region between forestomach and glandular stomach (at protein
CC level). Expression is mainly restricted to stomach.
CC {ECO:0000269|PubMed:15148607, ECO:0000269|PubMed:9828134}.
CC -!- INDUCTION: Up-regulated in response to IL4 and IL13 and during the
CC allergic response. {ECO:0000269|PubMed:11553626}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class II subfamily. {ECO:0000305}.
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DR EMBL; AY049765; AAL03953.2; -; mRNA.
DR EMBL; AF461142; AAL66748.1; -; Genomic_DNA.
DR EMBL; AY065557; AAL57751.1; -; mRNA.
DR EMBL; AK131914; BAE20869.1; -; mRNA.
DR EMBL; BC130015; AAI30016.1; -; mRNA.
DR CCDS; CCDS17719.1; -.
DR RefSeq; NP_660108.2; NM_145126.2.
DR AlphaFoldDB; Q91Z98; -.
DR SMR; Q91Z98; -.
DR BioGRID; 222433; 1.
DR STRING; 10090.ENSMUSP00000080851; -.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR iPTMnet; Q91Z98; -.
DR PhosphoSitePlus; Q91Z98; -.
DR jPOST; Q91Z98; -.
DR MaxQB; Q91Z98; -.
DR PaxDb; Q91Z98; -.
DR PeptideAtlas; Q91Z98; -.
DR PRIDE; Q91Z98; -.
DR ProteomicsDB; 283904; -.
DR DNASU; 104183; -.
DR Ensembl; ENSMUST00000082219; ENSMUSP00000080851; ENSMUSG00000063779.
DR GeneID; 104183; -.
DR KEGG; mmu:104183; -.
DR UCSC; uc008qvx.2; mouse.
DR CTD; 104183; -.
DR MGI; MGI:1341098; Chil4.
DR VEuPathDB; HostDB:ENSMUSG00000063779; -.
DR eggNOG; KOG2806; Eukaryota.
DR GeneTree; ENSGT00940000154557; -.
DR HOGENOM; CLU_002833_3_1_1; -.
DR InParanoid; Q91Z98; -.
DR OMA; INIPEAN; -.
DR OrthoDB; 826687at2759; -.
DR PhylomeDB; Q91Z98; -.
DR TreeFam; TF315610; -.
DR BioGRID-ORCS; 104183; 3 hits in 71 CRISPR screens.
DR PRO; PR:Q91Z98; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q91Z98; protein.
DR Bgee; ENSMUSG00000063779; Expressed in olfactory epithelium and 16 other tissues.
DR Genevisible; Q91Z98; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0008061; F:chitin binding; IBA:GO_Central.
DR GO; GO:0019900; F:kinase binding; ISO:MGI.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006032; P:chitin catabolic process; ISO:MGI.
DR GO; GO:0032722; P:positive regulation of chemokine production; ISO:MGI.
DR GO; GO:0002532; P:production of molecular mediator involved in inflammatory response; ISO:MGI.
DR Gene3D; 3.10.50.10; -; 1.
DR InterPro; IPR011583; Chitinase_II.
DR InterPro; IPR029070; Chitinase_insertion_sf.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF54556; SSF54556; 1.
DR PROSITE; PS51910; GH18_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Disulfide bond;
KW Inflammatory response; Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:11553626"
FT CHAIN 22..402
FT /note="Chitinase-like protein 4"
FT /id="PRO_0000011971"
FT DOMAIN 22..390
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 70..71
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 97..100
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 141
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 210..213
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 360
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT DISULFID 26..51
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT DISULFID 307..372
FT /evidence="ECO:0000250"
FT CONFLICT 286
FT /note="V -> I (in Ref. 5; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 288
FT /note="A -> T (in Ref. 5; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 361
FT /note="P -> R (in Ref. 5; no nucleotide entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 402 AA; 44975 MW; D935389319A59905 CRC64;
MAKLILVTGL AILLNVQLGS SYQLMCYYTS WAKDRPTEGS FKPGNIDPCL CTHLIYAFAG
MKNNEITYLS EQDLRDYEAL NGLKDRNTEL KTLLAIGGWK FGPAPFSSMV STPQNRQTFI
KSVIRFLRQY NFDGLNLDWQ YPGSRGSPPK DKHLFSVLVQ EMRKAFEEES TLNHIPRLLL
TSTGAGFIDV IKSGYKIPEL SQSLDYIQVM TYDLHDPKNG YTGENSPLYK SPYDIGKSAD
LNVDSIITYW KDHGAASEKL IVGFPAYGHT FILSDPSKNG IGDPTVSAGP PGKYTNEQGL
LAYFEICTFL NEGATEIFDA TQEVPYAYLG NEWVGYDNVR SFKLKAQWLK DNNLGGAVVW
PLDMDDFSGS FCHQGRFPLT TTLKRDLNVH SASCKASYRG EL
