CHIA_MOUSE
ID CHIA_MOUSE Reviewed; 473 AA.
AC Q91XA9; A0T468; B8K282; Q3TVE7; Q99PH2; Q9D803; Q9JLN1;
DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 24-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Acidic mammalian chitinase;
DE Short=AMCase;
DE EC=3.2.1.14;
DE AltName: Full=YNL;
DE Flags: Precursor;
GN Name=Chia; Synonyms=Chia1;
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 22-43, TISSUE SPECIFICITY,
RP AND FUNCTION.
RC STRAIN=BALB/cJ; TISSUE=Lung;
RX PubMed=11085997; DOI=10.1074/jbc.m009886200;
RA Boot R.G., Blommaart E.F.C., Swart E., Ghauharali-van der Vlugt K.,
RA Bijl N., Moe C., Place A., Aerts J.M.F.G.;
RT "Identification of a novel acidic mammalian chitinase distinct from
RT chitotriosidase.";
RL J. Biol. Chem. 276:6770-6778(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Lung;
RA Shen C.-R., Liu C.-L., Yang C.-J., Liu Y.-K.;
RT "Down-regulation of AMcase by siRNA in BALB/c mice.";
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Stomach;
RA Ling C., Zhu S.;
RT "Identification of a novel mutant strain of Mus musculus acidic mammalian
RT chitinase.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Stomach;
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 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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Salivary gland;
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-473.
RC TISSUE=Skin;
RA Price P.A., Harris S.C., Williamson M.K.;
RT "YNL, a putative mouse chitinase.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=12133911; DOI=10.1177/002215540205000810;
RA Suzuki M., Fujimoto W., Goto M., Morimatsu M., Syuto B., Iwanaga T.;
RT "Cellular expression of gut chitinase mRNA in the gastrointestinal tract of
RT mice and chickens.";
RL J. Histochem. Cytochem. 50:1081-1089(2002).
RN [9]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12971947; DOI=10.1016/s0003-9969(03)00150-x;
RA Goto M., Fujimoto W., Nio J., Iwanaga T., Kawasaki T.;
RT "Immunohistochemical demonstration of acidic mammalian chitinase in the
RT mouse salivary gland and gastric mucosa.";
RL Arch. Oral Biol. 48:701-707(2003).
RN [10]
RP FUNCTION, INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=15192232; DOI=10.1126/science.1095336;
RA Zhu Z., Zheng T., Homer R.J., Kim Y.K., Chen N.Y., Cohn L., Hamid Q.,
RA Elias J.A.;
RT "Acidic mammalian chitinase in asthmatic Th2 inflammation and IL-13 pathway
RT activation.";
RL Science 304:1678-1682(2004).
RN [11]
RP MUTAGENESIS OF HIS-208, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=18294964; DOI=10.1016/j.febslet.2008.02.032;
RA Bussink A.P., Vreede J., Aerts J.M., Boot R.G.;
RT "A single histidine residue modulates enzymatic activity in acidic
RT mammalian chitinase.";
RL FEBS Lett. 582:931-935(2008).
RN [12]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=18824549; DOI=10.1074/jbc.m805574200;
RA Hartl D., He C.H., Koller B., Da Silva C.A., Homer R., Lee C.G.,
RA Elias J.A.;
RT "Acidic mammalian chitinase is secreted via an ADAM17/epidermal growth
RT factor receptor-dependent pathway and stimulates chemokine production by
RT pulmonary epithelial cells.";
RL J. Biol. Chem. 283:33472-33482(2008).
RN [13]
RP FUNCTION.
RX PubMed=19076793; DOI=10.1111/j.1365-2230.2008.03092.x;
RA Chen L., Shen Z., Wu J.;
RT "Expression, purification and in vitro antifungal activity of acidic
RT mammalian chitinase against Candida albicans, Aspergillus fumigatus and
RT Trichophyton rubrum strains.";
RL Clin. Exp. Dermatol. 34:55-60(2009).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Degrades chitin and chitotriose. May participate in the
CC defense against nematodes, fungi and other pathogens. Plays a role in
CC T-helper cell type 2 (Th2) immune response. Contributes to the response
CC to IL-13 and inflammation in response to IL-13. Stimulates chemokine
CC production by pulmonary epithelial cells. Protects lung epithelial
CC cells against apoptosis and promotes phosphorylation of AKT1. Its
CC function in the inflammatory response and in protecting cells against
CC apoptosis is inhibited by allosamidin, suggesting that the function of
CC this protein depends on carbohydrate binding. Presence in saliva and
CC gastric juice suggests a function as a digestive enzyme.
CC {ECO:0000269|PubMed:11085997, ECO:0000269|PubMed:12133911,
CC ECO:0000269|PubMed:15192232, ECO:0000269|PubMed:19076793}.
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 Evidence={ECO:0000269|PubMed:18294964};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is below 2.5. {ECO:0000269|PubMed:18294964};
CC -!- SUBUNIT: Interacts with EGFR. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasmic granule.
CC Note=Detected in secretory granules of parotid acinar cells and gastric
CC chief cells and secreted from them into saliva and gastric juice,
CC respectively.
CC -!- TISSUE SPECIFICITY: Detected in macrophages and lung epithelial cells.
CC Detected in the acinar cells of parotid gland and von Ebner's gland but
CC not in submandibular and sublingual glands. Detected in gastric chief
CC cells. Also present in parotid glandular saliva and gastric juice (at
CC protein level). Highly expressed in submandibular gland
CC (PubMed:11085997) and stomach. Highly expressed in parotid gland but
CC not in submandibular and sublingual glands (PubMed:12133911). In
CC tongue, expressed only in von Ebner's gland. Expressed at lower levels
CC in lung. {ECO:0000269|PubMed:11085997, ECO:0000269|PubMed:12133911,
CC ECO:0000269|PubMed:12971947, ECO:0000269|PubMed:15192232,
CC ECO:0000269|PubMed:18824549}.
CC -!- DEVELOPMENTAL STAGE: In parotid gland, weak expression detected at
CC postnatal day P12, with levels increasing towards P16. In stomach,
CC first detected at P16, with expression reaching adult levels during
CC P20-24. {ECO:0000269|PubMed:12133911}.
CC -!- INDUCTION: Up-regulated upon pulmonary inflammation elicited by
CC sensitization and aerosol challenge with the aeroallergen ovalbumin.
CC Up-regulated during T-helper cell type 2 (Th2) inflammation. Induction
CC is mediated by IL-13. {ECO:0000269|PubMed:15192232}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class II subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH11134.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF290003; AAG60018.1; -; mRNA.
DR EMBL; DQ349202; ABC86699.1; -; mRNA.
DR EMBL; EF094027; ABK78778.1; -; mRNA.
DR EMBL; AK008633; BAB25795.1; -; mRNA.
DR EMBL; AK160173; BAE35672.1; -; mRNA.
DR EMBL; CH466608; EDL07527.1; -; Genomic_DNA.
DR EMBL; BC011134; AAH11134.1; ALT_INIT; mRNA.
DR EMBL; BC034548; AAH34548.1; -; mRNA.
DR EMBL; AF154571; AAF31644.1; -; mRNA.
DR CCDS; CCDS38585.1; -.
DR RefSeq; NP_075675.2; NM_023186.3.
DR AlphaFoldDB; Q91XA9; -.
DR SMR; Q91XA9; -.
DR IntAct; Q91XA9; 1.
DR STRING; 10090.ENSMUSP00000078134; -.
DR BindingDB; Q91XA9; -.
DR ChEMBL; CHEMBL2052027; -.
DR GuidetoPHARMACOLOGY; 2982; -.
DR CAZy; CBM14; Carbohydrate-Binding Module Family 14.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR iPTMnet; Q91XA9; -.
DR PhosphoSitePlus; Q91XA9; -.
DR MaxQB; Q91XA9; -.
DR PaxDb; Q91XA9; -.
DR PRIDE; Q91XA9; -.
DR ProteomicsDB; 281462; -.
DR ABCD; Q91XA9; 4 sequenced antibodies.
DR DNASU; 81600; -.
DR Ensembl; ENSMUST00000079132; ENSMUSP00000078134; ENSMUSG00000062778.
DR GeneID; 81600; -.
DR KEGG; mmu:81600; -.
DR UCSC; uc008qvv.1; mouse.
DR CTD; 81600; -.
DR MGI; MGI:1932052; Chia1.
DR VEuPathDB; HostDB:ENSMUSG00000062778; -.
DR eggNOG; KOG2806; Eukaryota.
DR GeneTree; ENSGT00940000154557; -.
DR HOGENOM; CLU_002833_3_1_1; -.
DR InParanoid; Q91XA9; -.
DR OMA; CLTYPNS; -.
DR OrthoDB; 826687at2759; -.
DR PhylomeDB; Q91XA9; -.
DR TreeFam; TF315610; -.
DR Reactome; R-MMU-189085; Digestion of dietary carbohydrate.
DR BioGRID-ORCS; 81600; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Chia1; mouse.
DR PRO; PR:Q91XA9; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q91XA9; protein.
DR Bgee; ENSMUSG00000062778; Expressed in epithelium of stomach and 62 other tissues.
DR ExpressionAtlas; Q91XA9; baseline and differential.
DR Genevisible; Q91XA9; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0008061; F:chitin binding; IDA:UniProtKB.
DR GO; GO:0004568; F:chitinase activity; IDA:UniProtKB.
DR GO; GO:0019900; F:kinase binding; ISO:MGI.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0006032; P:chitin catabolic process; IDA:UniProtKB.
DR GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0032722; P:positive regulation of chemokine production; ISS:UniProtKB.
DR GO; GO:0002532; P:production of molecular mediator involved in inflammatory response; ISS:UniProtKB.
DR Gene3D; 3.10.50.10; -; 1.
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 Apoptosis; Carbohydrate metabolism; Chitin degradation; Chitin-binding;
KW Cytoplasm; Direct protein sequencing; Disulfide bond; Glycosidase;
KW Hydrolase; Immunity; Inflammatory response; Polysaccharide degradation;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:11085997"
FT CHAIN 22..473
FT /note="Acidic mammalian chitinase"
FT /id="PRO_0000011945"
FT DOMAIN 22..390
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT DOMAIN 424..473
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT REGION 394..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..421
FT /note="Polar 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: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 49..394
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT DISULFID 307..372
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT DISULFID 457..470
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT MUTAGEN 208
FT /note="H->N: Strongly reduced activity at low pH, with
FT minor effect on activity at neutral pH."
FT /evidence="ECO:0000269|PubMed:18294964"
FT CONFLICT 293
FT /note="P -> A (in Ref. 1; AAG60018)"
FT /evidence="ECO:0000305"
FT CONFLICT 405
FT /note="T -> S (in Ref. 3; ABK78778)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 473 AA; 52003 MW; 333C874477476695 CRC64;
MAKLLLVTGL ALLLNAQLGS AYNLICYFTN WAQYRPGLGS FKPDDINPCL CTHLIYAFAG
MQNNEITTIE WNDVTLYKAF NDLKNRNSKL KTLLAIGGWN FGTAPFTTMV STSQNRQTFI
TSVIKFLRQY GFDGLDLDWE YPGSRGSPPQ DKHLFTVLVK EMREAFEQEA IESNRPRLMV
TAAVAGGISN IQAGYEIPEL SKYLDFIHVM TYDLHGSWEG YTGENSPLYK YPTETGSNAY
LNVDYVMNYW KNNGAPAEKL IVGFPEYGHT FILRNPSDNG IGAPTSGDGP AGPYTRQAGF
WAYYEICTFL RSGATEVWDA SQEVPYAYKA NEWLGYDNIK SFSVKAQWLK QNNFGGAMIW
AIDLDDFTGS FCDQGKFPLT STLNKALGIS TEGCTAPDVP SEPVTTPPGS GSGGGSSGGS
SGGSGFCADK ADGLYPVADD RNAFWQCING ITYQQHCQAG LVFDTSCNCC NWP
