ID   CHIT1_MOUSE             Reviewed;         464 AA.
AC   Q9D7Q1; Q6QJD2;
DT   24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 2.
DT   27-MAR-2024, entry version 179.
DE   RecName: Full=Chitotriosidase-1;
DE            EC=3.2.1.14;
DE   AltName: Full=Chitinase-1;
DE   Flags: Precursor;
GN   Name=Chit1;
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] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP   TISSUE SPECIFICITY, AND MUTAGENESIS OF ASP-136 AND GLU-140.
RC   STRAIN=C57BL/6J; TISSUE=Tongue;
RX   PubMed=16005164; DOI=10.1016/j.gene.2005.05.006;
RA   Zheng T., Rabach M., Chen N.Y., Rabach L., Hu X., Elias J.A., Zhu Z.;
RT   "Molecular cloning and functional characterization of mouse
RT   chitotriosidase.";
RL   Gene 357:37-46(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6J; TISSUE=Tongue;
RX   PubMed=15923370; DOI=10.1369/jhc.4a6547.2005;
RA   Boot R.G., Bussink A.P., Verhoek M., de Boer P.A.J., Moorman A.F.,
RA   Aerts J.M.F.G.;
RT   "Marked differences in tissue-specific expression of chitinases in mouse
RT   and man.";
RL   J. Histochem. Cytochem. 53:1283-1292(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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).
CC   -!- FUNCTION: Degrades chitin, chitotriose and chitobiose. May participate
CC       in the defense against nematodes and other pathogens (By similarity).
CC       {ECO:0000250, ECO:0000269|PubMed:16005164}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide
CC         (1->4)-beta-linkages in chitin and chitodextrins.; EC=3.2.1.14;
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16005164}. Lysosome
CC       {ECO:0000250}. Note=A small proportion is lysosomal. {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9D7Q1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9D7Q1-2; Sequence=VSP_020143, VSP_020144;
CC   -!- TISSUE SPECIFICITY: Highly expressed in tongue, stomach, kidney, brain,
CC       skin, testis, and bone marrow. Low level of expression was found in
CC       lung, heart, spleen, small intestine, and liver. Not detectable in
CC       pancreas, salivary gland, large intestine, uterus, or peripheral blood
CC       mononuclear cells (PBMC). {ECO:0000269|PubMed:15923370,
CC       ECO:0000269|PubMed:16005164}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC       class II subfamily. {ECO:0000305}.
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DR   EMBL; AY458654; AAR14312.1; -; mRNA.
DR   EMBL; AY536287; AAS47832.1; -; mRNA.
DR   EMBL; AK009012; BAB26025.1; -; mRNA.
DR   CCDS; CCDS15304.1; -. [Q9D7Q1-1]
DR   CCDS; CCDS69943.1; -. [Q9D7Q1-2]
DR   RefSeq; NP_001271453.1; NM_001284524.1. [Q9D7Q1-2]
DR   RefSeq; NP_001271454.1; NM_001284525.1. [Q9D7Q1-1]
DR   RefSeq; NP_082255.1; NM_027979.2. [Q9D7Q1-1]
DR   RefSeq; XP_006529942.1; XM_006529879.2. [Q9D7Q1-1]
DR   RefSeq; XP_006529943.1; XM_006529880.1. [Q9D7Q1-1]
DR   RefSeq; XP_006529944.1; XM_006529881.2. [Q9D7Q1-2]
DR   AlphaFoldDB; Q9D7Q1; -.
DR   SMR; Q9D7Q1; -.
DR   STRING; 10090.ENSMUSP00000123979; -.
DR   BindingDB; Q9D7Q1; -.
DR   ChEMBL; CHEMBL4105845; -.
DR   GuidetoPHARMACOLOGY; 3187; -.
DR   CAZy; CBM14; Carbohydrate-Binding Module Family 14.
DR   CAZy; GH18; Glycoside Hydrolase Family 18.
DR   PhosphoSitePlus; Q9D7Q1; -.
DR   CPTAC; non-CPTAC-3569; -.
DR   MaxQB; Q9D7Q1; -.
DR   PaxDb; 10090-ENSMUSP00000123979; -.
DR   PeptideAtlas; Q9D7Q1; -.
DR   ProteomicsDB; 283906; -. [Q9D7Q1-1]
DR   ProteomicsDB; 283907; -. [Q9D7Q1-2]
DR   Antibodypedia; 2441; 277 antibodies from 34 providers.
DR   DNASU; 71884; -.
DR   Ensembl; ENSMUST00000086475.3; ENSMUSP00000083666.3; ENSMUSG00000026450.15. [Q9D7Q1-1]
DR   Ensembl; ENSMUST00000159963.8; ENSMUSP00000123979.2; ENSMUSG00000026450.15. [Q9D7Q1-1]
DR   Ensembl; ENSMUST00000160060.8; ENSMUSP00000124331.2; ENSMUSG00000026450.15. [Q9D7Q1-2]
DR   GeneID; 71884; -.
DR   KEGG; mmu:71884; -.
DR   UCSC; uc007crf.2; mouse. [Q9D7Q1-1]
DR   UCSC; uc033flh.1; mouse. [Q9D7Q1-2]
DR   AGR; MGI:1919134; -.
DR   CTD; 1118; -.
DR   MGI; MGI:1919134; Chit1.
DR   VEuPathDB; HostDB:ENSMUSG00000026450; -.
DR   eggNOG; KOG2806; Eukaryota.
DR   GeneTree; ENSGT00940000161149; -.
DR   HOGENOM; CLU_002833_3_1_1; -.
DR   InParanoid; Q9D7Q1; -.
DR   OMA; NWDIYAR; -.
DR   OrthoDB; 1752999at2759; -.
DR   PhylomeDB; Q9D7Q1; -.
DR   TreeFam; TF315610; -.
DR   Reactome; R-MMU-189085; Digestion of dietary carbohydrate.
DR   Reactome; R-MMU-6798695; Neutrophil degranulation.
DR   BioGRID-ORCS; 71884; 1 hit in 79 CRISPR screens.
DR   ChiTaRS; Chit1; mouse.
DR   PRO; PR:Q9D7Q1; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; Q9D7Q1; Protein.
DR   Bgee; ENSMUSG00000026450; Expressed in lip and 31 other cell types or tissues.
DR   ExpressionAtlas; Q9D7Q1; baseline and differential.
DR   GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; ISO:MGI.
DR   GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0008061; F:chitin binding; IBA:GO_Central.
DR   GO; GO:0004568; F:chitinase activity; ISO:MGI.
DR   GO; GO:0008843; F:endochitinase activity; ISO:MGI.
DR   GO; GO:0006032; P:chitin catabolic process; ISS:UniProtKB.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd02872; GH18_chitolectin_chitotriosidase; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 2.
DR   InterPro; IPR002557; Chitin-bd_dom.
DR   InterPro; IPR036508; Chitin-bd_dom_sf.
DR   InterPro; IPR011583; Chitinase_II.
DR   InterPro; IPR029070; Chitinase_insertion_sf.
DR   InterPro; IPR001223; Glyco_hydro18_cat.
DR   InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR11177; CHITINASE; 1.
DR   PANTHER; PTHR11177:SF248; CHITOTRIOSIDASE-1; 1.
DR   Pfam; PF01607; CBM_14; 1.
DR   Pfam; PF00704; Glyco_hydro_18; 1.
DR   SMART; SM00494; ChtBD2; 1.
DR   SMART; SM00636; Glyco_18; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF54556; Chitinase insertion domain; 1.
DR   SUPFAM; SSF57625; Invertebrate chitin-binding proteins; 1.
DR   PROSITE; PS50940; CHIT_BIND_II; 1.
DR   PROSITE; PS01095; GH18_1; 1.
DR   PROSITE; PS51910; GH18_2; 1.
DR   Genevisible; Q9D7Q1; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; Carbohydrate metabolism; Chitin degradation;
KW   Chitin-binding; Disulfide bond; Glycosidase; Hydrolase; Lysosome;
KW   Polysaccharide degradation; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000250"
FT   CHAIN           22..464
FT                   /note="Chitotriosidase-1"
FT                   /id="PRO_0000011942"
FT   DOMAIN          22..386
FT                   /note="GH18"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   DOMAIN          415..464
FT                   /note="Chitin-binding type-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT   REGION          385..416
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        393..407
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        140
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   BINDING         70..71
FT                   /ligand="chitin"
FT                   /ligand_id="ChEBI:CHEBI:17029"
FT                   /evidence="ECO:0000250"
FT   BINDING         97..100
FT                   /ligand="chitin"
FT                   /ligand_id="ChEBI:CHEBI:17029"
FT                   /evidence="ECO:0000250"
FT   BINDING         210..213
FT                   /ligand="chitin"
FT                   /ligand_id="ChEBI:CHEBI:17029"
FT                   /evidence="ECO:0000250"
FT   DISULFID        26..51
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   DISULFID        307..368
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT   DISULFID        448..461
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT   VAR_SEQ         343..396
FT                   /note="AYLKQKGLGGAMVWVLDLDDFKGSFCNQGPYPLIRTLRQELNLPSETPRSPE
FT                   QI -> KLMGSTPTLETSPLTTTVEEGGCSSRAVLQAWCLEPLANVVPGAKFLEPHPTP
FT                   V (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_020143"
FT   VAR_SEQ         397..464
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_020144"
FT   MUTAGEN         136
FT                   /note="D->N: Loss of activity; when associated with Q-140."
FT                   /evidence="ECO:0000269|PubMed:16005164"
FT   MUTAGEN         140
FT                   /note="E->Q: Loss of activity; when associated with N-136."
FT                   /evidence="ECO:0000269|PubMed:16005164"
SQ   SEQUENCE   464 AA;  51112 MW;  6276B6A414B4E96A CRC64;
     MVQSLAWAGV MTLLMVQWGS AAKLVCYLTN WSQYRTEAVR FFPRDVDPNL CTHVIFAFAG
     MDNHQLSTVE HNDELLYQEL NSLKTKNPKL KTLLAVGGWT FGTQKFTDMV ATASNRQTFV
     KSALSFLRTQ GFDGLDLDWE FPGGRGSPTV DKERFTALIQ DLAKAFQEEA QSSGKERLLL
     TAAVPSDRGL VDAGYEVDKI AQSLDFINLM AYDFHSSLEK TTGHNSPLYK RQGESGAAAE
     QNVDAAVTLW LQKGTPASKL ILGMPTYGRS FTLASSSDNG VGAPATGPGA PGPYTKDKGV
     LAYYEACSWK ERHRIEDQKV PYAFQDNQWV SFDDVESFKA KAAYLKQKGL GGAMVWVLDL
     DDFKGSFCNQ GPYPLIRTLR QELNLPSETP RSPEQIIPEP RPSSMPEQGP SPGLDNFCQG
     KADGVYPNPG DESTYYNCGG GRLFQQSCPP GLVFRASCKC CTWS
//