CHIA_RAT
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 03-AUG-2022, entry version 121.
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}.
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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 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; 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 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
