ID CHIA_RAT Reviewed; 473 AA. AC Q6RY07; DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 14-DEC-2022, entry version 122. DE RecName: Full=Acidic mammalian chitinase; DE Short=AMCase; DE EC=3.2.1.14; DE Flags: Precursor; GN Name=Chia; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Sprague-Dawley; TISSUE=Stomach; RA Chen X.-H., Cai G.-P.; RT "Rattus norvegicus similar to acidic mammalian chitinase precursor."; RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases. 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 (By similarity). CC {ECO:0000250}. 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: Interacts with EGFR. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Secreted {ECO:0000250}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase CC class II subfamily. {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; AY486074; AAR28968.1; -; mRNA. DR RefSeq; NP_997469.1; NM_207586.2. DR AlphaFoldDB; Q6RY07; -. DR SMR; Q6RY07; -. DR STRING; 10116.ENSRNOP00000044947; -. DR CAZy; CBM14; Carbohydrate-Binding Module Family 14. DR CAZy; GH18; Glycoside Hydrolase Family 18. DR PaxDb; Q6RY07; -. DR GeneID; 113901; -. DR KEGG; rno:113901; -. DR UCSC; RGD:1303058; rat. DR AGR; RGD:1303058; -. DR CTD; 27159; -. DR RGD; 1303058; Chia. DR eggNOG; KOG2806; Eukaryota. DR InParanoid; Q6RY07; -. DR OrthoDB; 826687at2759; -. DR PhylomeDB; Q6RY07; -. DR Reactome; R-RNO-189085; Digestion of dietary carbohydrate. DR PRO; PR:Q6RY07; -. DR Proteomes; UP000002494; Unplaced. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005576; C:extracellular region; IDA:RGD. DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB. DR GO; GO:0008061; F:chitin binding; ISO:RGD. DR GO; GO:0004568; F:chitinase activity; IDA:RGD. DR GO; GO:0019900; F:kinase binding; ISO:RGD. DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW. DR GO; GO:0006032; P:chitin catabolic process; IDA:RGD. 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; (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. PE 2: Evidence at transcript level; KW Apoptosis; Carbohydrate metabolism; Chitin degradation; Chitin-binding; KW Cytoplasm; Disulfide bond; Glycosidase; Hydrolase; Immunity; KW Inflammatory response; Polysaccharide degradation; Reference proteome; KW Secreted; Signal. FT SIGNAL 1..21 FT /evidence="ECO:0000250" FT CHAIN 22..473 FT /note="Acidic mammalian chitinase" FT /id="PRO_0000011946" 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 395..421 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 405..419 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" SQ SEQUENCE 473 AA; 51951 MW; FBB0DB91A42C1EFD CRC64; MAKLILVTGL VLLLNVQLGS AYNLVCYFTN WAQYRPGLGS FKPDDINPCL CTHLIYAFAG MQNNQITTIE WNDVTLYKAF NDLKNRNSKL KTLLAIGGWN FGTAPFTTMV STSQNRQTFI TSVIKFLRQY GFDGLDLDWE YPGSRGSPPQ DKHLFTVLVK ELREAFEQEA IESNRPRLMV TAAVAAGISN IQAGYEIPEL SQYLDFIHVM TYDLHGSWDG YTGENSPLYK LPTETGSNAY LNVDYVMNYW KDNGAPAEKL IVGFPEYGHT YILSNPSDTG IGAPTSGNGP AGPYTRQAGF WAYYEICTFL RNGATQDWDA PQEVPYAYKG NEWVGYDNIK SFSVKAQWLK QNNFGGAMIW AIDLDDFTGS FCDQGKFPLT STLNKALDIP TAGCTAPDLP SEPVTTPPGS GSGGGSSGGG SEGSGFCAGK ADGLYPVADD RNAFWHCING ITYQQHCQAG LVFDTSCNCC NWP //