CHIT1_MOUSE
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 03-AUG-2022, entry version 170.
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; Q9D7Q1; -.
DR PeptideAtlas; Q9D7Q1; -.
DR PRIDE; Q9D7Q1; -.
DR ProteomicsDB; 283906; -. [Q9D7Q1-1]
DR ProteomicsDB; 283907; -. [Q9D7Q1-2]
DR Antibodypedia; 2441; 244 antibodies from 34 providers.
DR DNASU; 71884; -.
DR Ensembl; ENSMUST00000086475; ENSMUSP00000083666; ENSMUSG00000026450. [Q9D7Q1-1]
DR Ensembl; ENSMUST00000159963; ENSMUSP00000123979; ENSMUSG00000026450. [Q9D7Q1-1]
DR Ensembl; ENSMUST00000160060; ENSMUSP00000124331; ENSMUSG00000026450. [Q9D7Q1-2]
DR GeneID; 71884; -.
DR KEGG; mmu:71884; -.
DR UCSC; uc007crf.2; mouse. [Q9D7Q1-1]
DR UCSC; uc033flh.1; mouse. [Q9D7Q1-2]
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; QRFTDMV; -.
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 74 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 29 other tissues.
DR ExpressionAtlas; Q9D7Q1; baseline and differential.
DR Genevisible; Q9D7Q1; MM.
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 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 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; SSF51445; 1.
DR SUPFAM; SSF54556; SSF54556; 1.
DR SUPFAM; SSF57625; SSF57625; 1.
DR PROSITE; PS50940; CHIT_BIND_II; 1.
DR PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 1.
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
