CHIA_BOVIN
ID CHIA_BOVIN Reviewed; 472 AA.
AC Q95M17; Q3SZE1;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, 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 AltName: Full=Chitin-binding protein b04;
DE Short=CBPb04;
DE Flags: Precursor;
GN Name=CHIA;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 22-40; 126-171 AND 312-350,
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=11591385; DOI=10.1016/s0014-5793(01)02893-9;
RA Suzuki M., Morimatsu M., Yamashita T., Iwanaga T., Syuto B.;
RT "A novel serum chitinase that is expressed in bovine liver.";
RL FEBS Lett. 506:127-130(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) 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, ECO:0000269|PubMed:11591385}.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5.6-7.6.;
CC -!- SUBUNIT: Interacts with EGFR. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Secreted
CC {ECO:0000269|PubMed:11591385}.
CC -!- TISSUE SPECIFICITY: Detected in liver and in serum.
CC {ECO:0000269|PubMed:11591385}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class II subfamily. {ECO:0000305}.
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DR EMBL; AB051629; BAB71805.1; -; mRNA.
DR EMBL; BC102931; AAI02932.1; -; mRNA.
DR RefSeq; NP_777124.1; NM_174699.2.
DR AlphaFoldDB; Q95M17; -.
DR SMR; Q95M17; -.
DR STRING; 9913.ENSBTAP00000000324; -.
DR CAZy; CBM14; Carbohydrate-Binding Module Family 14.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR PaxDb; Q95M17; -.
DR PRIDE; Q95M17; -.
DR GeneID; 282645; -.
DR KEGG; bta:282645; -.
DR CTD; 27159; -.
DR eggNOG; KOG2806; Eukaryota.
DR InParanoid; Q95M17; -.
DR OrthoDB; 826687at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR GO; GO:0004568; F:chitinase activity; ISS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0006032; P:chitin catabolic process; ISS: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; Glycoprotein;
KW Glycosidase; Hydrolase; Immunity; Inflammatory response;
KW Polysaccharide degradation; Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:11591385"
FT CHAIN 22..472
FT /note="Acidic mammalian chitinase"
FT /id="PRO_0000011943"
FT DOMAIN 22..390
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT DOMAIN 423..472
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT REGION 397..421
FT /note="Disordered"
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 CARBOHYD 395
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 409
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 415
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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 456..469
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT CONFLICT 144
FT /note="F -> S (in Ref. 2; AAI02932)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 472 AA; 52129 MW; 7A4A600E8DA04B1E CRC64;
MAKLIFLTGL AFLLNAQLGS AYQLVCYFSN WAQYRPGLGS FKPDNIDPCL CTHLIYAFAG
MSNSEITTIE WNDVALYSSF NDLKKKNSQL KILLAIGGWN FGTAPFTAMV ATPENRKTFI
SSVIKFLHQY GFDGLDFDWE YPGFRGSPSQ DKHLFTVLVQ ETREAFEQEA KQTNKPRLLV
TAAVAAGISN IQAGYEIPQL SQYLDFIHVM TYDFHGSWEG YTGENSPLYK YPTDTGSNTY
LNVEYAMNYW KKNGAPAEKL IIGFPAYGHN FILRDASNNG IGAPTSGAGP AGPYTREAGF
WAYYEICAFL KDGATEAWDD SQNVPYAYKG TEWVGYDNVN SFRIKAQWLK ENNFGGAMVW
AIDLDDFTGT FCNQGKFPLI NTLKDALGLK SATCNASTQS SEPNSSPGNE SGSGNKSSSS
EGRGYCAGKA DGLYPVADNR NAFWNCVNGI TYKQNCLTGL VFDTSCHCCN WA
