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 21-SEP-2011, entry version 68. 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; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; 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 CC in T helper cell type 2 (Th2) immune response. Contributes to the CC response to IL-13 and inflammation in response to IL-13. CC Stimulates chemokine production by pulmonary epithelial cells. CC Protects lung epithelial cells against apoptosis and promotes CC phosphorylation of AKT1. Its function in the inflammatory response CC and in protecting cells against apoptosis is inhibited by CC allosamidin, suggesting that the function of this protein depends CC on carbohydrate binding (By similarity). CC -!- CATALYTIC ACTIVITY: Random hydrolysis of N-acetyl-beta-D- CC glucosaminide (1->4)-beta-linkages in chitin and chitodextrins. CC -!- SUBUNIT: Interacts with EGFR (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Secreted (By CC similarity). CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase CC class II subfamily. CC -!- SIMILARITY: Contains 1 chitin-binding type-2 domain. 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 IPI; IPI00421295; -. DR RefSeq; NP_997469.1; NM_207586.1. DR UniGene; Rn.43692; -. DR ProteinModelPortal; Q6RY07; -. DR SMR; Q6RY07; 22-394. DR STRING; Q6RY07; -. DR CAZy; CBM14; Carbohydrate-Binding Module Family 14. DR CAZy; GH18; Glycoside Hydrolase Family 18. DR PRIDE; Q6RY07; -. DR GeneID; 113901; -. DR KEGG; rno:113901; -. DR CTD; 27159; -. DR RGD; 1303058; Chia. DR eggNOG; roNOG10317; -. DR GeneTree; ENSGT00550000074323; -. DR HOVERGEN; HBG011684; -. DR OrthoDB; EOG476K16; -. DR PhylomeDB; Q6RY07; -. DR NextBio; 617982; -. DR ArrayExpress; Q6RY07; -. DR Genevestigator; Q6RY07; -. DR GermOnline; ENSRNOG00000033162; Rattus norvegicus. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB. DR GO; GO:0043169; F:cation binding; IEA:InterPro. DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW. DR GO; GO:0004568; F:chitinase activity; ISS:UniProtKB. DR GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW. DR GO; GO:0006032; P:chitin catabolic process; ISS:UniProtKB. DR GO; GO:0090197; P:positive regulation of chemokine secretion; ISS:UniProtKB. DR GO; GO:0002532; P:production of molecular mediator involved in inflammatory response; ISS:UniProtKB. DR InterPro; IPR002557; Chitin-bd_dom. DR InterPro; IPR011583; Chitinase_II. DR InterPro; IPR001223; Glyco_hydro18cat. DR InterPro; IPR001579; Glyco_hydro_18_chit_AS. DR InterPro; IPR013781; Glyco_hydro_subgr_catalytic. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR Gene3D; G3DSA:2.170.140.10; Chitin-bd_dom; 1. DR Gene3D; G3DSA:3.20.20.80; Glyco_hydro_cat; 2. 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; SSF57625; Chitin_bind_PerA; 1. DR SUPFAM; SSF51445; Glyco_hydro_cat; 1. DR PROSITE; PS50940; CHIT_BIND_II; 1. DR PROSITE; PS01095; CHITINASE_18; 1. PE 2: Evidence at transcript level; KW Apoptosis; Carbohydrate metabolism; Chitin degradation; KW Chitin-binding; Complete proteome; Cytoplasm; Disulfide bond; KW Glycosidase; Hydrolase; Immunity; Inflammatory response; KW Polysaccharide degradation; Reference proteome; Secreted; Signal. FT SIGNAL 1 21 By similarity. FT CHAIN 22 473 Acidic mammalian chitinase. FT /FTId=PRO_0000011946. FT DOMAIN 424 473 Chitin-binding type-2. FT REGION 70 71 Chitooligosaccharide binding (By FT similarity). FT REGION 97 100 Chitooligosaccharide binding (By FT similarity). FT REGION 210 213 Chitooligosaccharide binding (By FT similarity). FT COMPBIAS 409 425 Gly/Ser-rich. FT ACT_SITE 140 140 Proton donor (By similarity). FT BINDING 141 141 Chitooligosaccharide (By similarity). FT BINDING 360 360 Chitooligosaccharide (By similarity). FT DISULFID 26 51 By similarity. FT DISULFID 49 394 By similarity. FT DISULFID 307 372 By similarity. FT DISULFID 457 470 By similarity. 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 //