ID Q8AV87_CHICK Unreviewed; 482 AA. AC Q8AV87; DT 01-MAR-2003, integrated into UniProtKB/TrEMBL. DT 01-MAR-2003, sequence version 1. DT 02-SEP-2026, entry version 130. DE RecName: Full=Chitinase {ECO:0000256|PROSITE-ProRule:PRU10053}; DE EC=3.2.1.14 {ECO:0000256|PROSITE-ProRule:PRU10053}; GN Name=cbpch04 {ECO:0000313|EMBL:BAC53757.1}; OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae; OC Phasianinae; Gallus. OX NCBI_TaxID=9031 {ECO:0000313|EMBL:BAC53757.1}; RN [1] {ECO:0000313|EMBL:BAC53757.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Leghorn {ECO:0000313|EMBL:BAC53757.1}; RC TISSUE=Grandular stomach {ECO:0000313|EMBL:BAC53757.1}; RX PubMed=12133911; 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). 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:0000256|ARBA:ARBA00000822, ECO:0000256|PROSITE- CC ProRule:PRU10053}; CC -!- SUBUNIT: Interacts with EGFR. {ECO:0000256|ARBA:ARBA00062006}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. CC Secreted {ECO:0000256|ARBA:ARBA00004613}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase CC class II subfamily. {ECO:0000256|ARBA:ARBA00009121}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01258}. 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; AB071038; BAC53757.1; -; mRNA. DR RefSeq; NP_989760.2; NM_204429.2. DR AlphaFoldDB; Q8AV87; -. DR SMR; Q8AV87; -. DR GeneID; 395072; -. DR KEGG; gga:395072; -. DR CTD; 27159; -. DR VEuPathDB; HostDB:geneid_395072; -. DR OrthoDB; 76388at2759; -. DR PhylomeDB; Q8AV87; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0008061; F:chitin binding; IEA:InterPro. DR GO; GO:0008843; F:endochitinase activity; IEA:UniProtKB-EC. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-ARBA. DR CDD; cd02872; GH18_chitolectin_chitotriosidase; 1. DR FunFam; 2.170.140.10:FF:000001; Acidic mammalian chitinase; 1. DR FunFam; 3.20.20.80:FF:000007; Acidic mammalian chitinase; 1. DR FunFam; 3.20.20.80:FF:000081; Chitinase 1; 1. DR FunFam; 3.10.50.10:FF:000001; Chitinase 3-like 1; 1. DR Gene3D; 3.10.50.10; -; 1. DR Gene3D; 2.170.140.10; Chitin binding domain; 1. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR InterPro; IPR002557; Chitin-bd_dom. DR InterPro; IPR036508; Chitin-bd_dom_sf. DR InterPro; IPR011583; Chitinase_II/V-like_cat. DR InterPro; IPR029070; Chitinase_insertion_sf. DR InterPro; IPR017853; GH_hydrolase_sf. DR InterPro; IPR001223; Glyco_hydro18_cat. DR InterPro; IPR001579; Glyco_hydro_18_chit_AS. DR InterPro; IPR050314; Glycosyl_Hydrlase_18. DR PANTHER; PTHR11177:SF188; ACIDIC MAMMALIAN CHITINASE; 1. DR PANTHER; PTHR11177; CHITINASE; 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. PE 2: Evidence at transcript level; KW Apoptosis {ECO:0000256|ARBA:ARBA00022703}; KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277}; KW Chitin degradation {ECO:0000256|ARBA:ARBA00023024}; KW Chitin-binding {ECO:0000256|ARBA:ARBA00022669, ECO:0000256|PROSITE- KW ProRule:PRU00144}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE- KW ProRule:PRU00144}; KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PROSITE- KW ProRule:PRU01258}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE- KW ProRule:PRU01258}; Immunity {ECO:0000256|ARBA:ARBA00022859}; KW Inflammatory response {ECO:0000256|ARBA:ARBA00023198}; KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326}; KW Secreted {ECO:0000256|ARBA:ARBA00022525}; KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}. FT SIGNAL 1..21 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 22..482 FT /note="Chitinase" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5004305590" FT DOMAIN 22..390 FT /note="GH18" FT /evidence="ECO:0000259|PROSITE:PS51910" FT DOMAIN 433..482 FT /note="Chitin-binding type-2" FT /evidence="ECO:0000259|PROSITE:PS50940" FT REGION 391..426 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 412..422 FT /note="Gly residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 140 FT /note="Proton donor" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10053" FT BINDING 70..71 FT /ligand="chitin" FT /ligand_id="ChEBI:CHEBI:17029" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01258" FT BINDING 97..100 FT /ligand="chitin" FT /ligand_id="ChEBI:CHEBI:17029" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01258" FT BINDING 141 FT /ligand="chitin" FT /ligand_id="ChEBI:CHEBI:17029" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01258" FT BINDING 210..213 FT /ligand="chitin" FT /ligand_id="ChEBI:CHEBI:17029" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01258" FT BINDING 360 FT /ligand="chitin" FT /ligand_id="ChEBI:CHEBI:17029" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01258" FT DISULFID 466..479 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00144" SQ SEQUENCE 482 AA; 52239 MW; 68DB483D47907FD1 CRC64; MAKLILITGL ALLLNAQIGS TYVLSCYFTN WAQYRPGLGK YMPDNIDPCL CDHLIYAFAG MSNNEITTYE WNDETLYKSF NGLKNQNGNL KTLLAIGGWN FGTAKFSTMV STPENRQTFI NSVIKFLRQY QFDGLDIDWE YPGSKGSPSQ DKGLFTVLVQ EMLAAFEQEA KQVNKPRLMI TAAVAAGLSN IQAGYQIAEL GKYLDYFHVM TYDFHGSWDG QTGENSPLYK GPADTGDLIY FNVDYAMNYW KSNGAPAEKL LVGFPTYGHS YILKNPSDTA VGAPTSGPGP AGPYTRQSGF LAYYEICTFL DSGATQAWDA PQDVPYAYKS SEWVGYGNIK SFNIKIDWLK KNNYGGAMVW SLDMDDFTGT FCKQGKYPLI TTLKNALGQQ SSSCVPPAQP NPPITAAPST GSGSGSGSGS GSSGSNTGSS GGSGFCAGKA NGIYADPTNK SKFYNCNNGE TFVQSCQAGL VFDSSCSCCN WA //