CHIT1_HUMAN
ID CHIT1_HUMAN Reviewed; 466 AA.
AC Q13231; B3KNW6; J3KN09; Q0VGG5; Q0VGG6; Q3ZAR1; Q6ISC2; Q9H3V8; Q9UDJ8;
DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=Chitotriosidase-1;
DE EC=3.2.1.14;
DE AltName: Full=Chitinase-1;
DE Flags: Precursor;
GN Name=CHIT1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Macrophage;
RX PubMed=7592832; DOI=10.1074/jbc.270.44.26252;
RA Boot R.G., Renkema G.H., Strijland A., van Zonneveld A.J., Aerts J.M.F.G.;
RT "Cloning of a cDNA encoding chitotriosidase, a human chitinase produced by
RT macrophages.";
RL J. Biol. Chem. 270:26252-26256(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND VARIANT GLY-442.
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS SER-102
RP AND GLY-442.
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 22-43 AND 178-198, FUNCTION, CATALYTIC ACTIVITY, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Spleen;
RX PubMed=7836450; DOI=10.1074/jbc.270.5.2198;
RA Renkema G.H., Boot R.G., Muijsers A.O., Donker-Koopman W.E.,
RA Aerts J.M.F.G.;
RT "Purification and characterization of human chitotriosidase, a novel member
RT of the chitinase family of proteins.";
RL J. Biol. Chem. 270:2198-2202(1995).
RN [6]
RP POLYMORPHISM, AND FUNCTION (ISOFORM 3).
RX PubMed=9748235; DOI=10.1074/jbc.273.40.25680;
RA Boot R.G., Renkema G.H., Verhoek M., Strijland A., Bliek J.,
RA de Meulemeester T.M.A.M.O., Mannens M.M.A.M., Aerts J.M.F.G.;
RT "The human chitotriosidase gene. Nature of inherited enzyme deficiency.";
RL J. Biol. Chem. 273:25680-25685(1998).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 22-386 IN COMPLEX WITH CHITOBIOSE
RP AND ALLOSAMIDIN, SUBCELLULAR LOCATION, AND DISULFIDE BONDS.
RX PubMed=11960986; DOI=10.1074/jbc.m201636200;
RA Fusetti F., von Moeller H., Houston D., Rozeboom H.J., Dijkstra B.W.,
RA Boot R.G., Aerts J.M.F.G., van Aalten D.M.F.;
RT "Structure of human chitotriosidase. Implications for specific inhibitor
RT design and function of mammalian chitinase-like lectins.";
RL J. Biol. Chem. 277:25537-25544(2002).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 22-385 IN COMPLEX WITH
RP ALLOSAMIDIN.
RX PubMed=12639956; DOI=10.1074/jbc.m300362200;
RA Rao F.V., Houston D.R., Boot R.G., Aerts J.M., Sakuda S., van Aalten D.M.;
RT "Crystal structures of allosamidin derivatives in complex with human
RT macrophage chitinase.";
RL J. Biol. Chem. 278:20110-20116(2003).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 22-466 IN COMPLEX WITH THE
RP CYCLOPENTAPEPTIDE INHIBITOR ARGADIN, AND CATALYTIC ACTIVITY.
RX PubMed=15664516; DOI=10.1016/j.chembiol.2004.10.013;
RA Rao F.V., Houston D.R., Boot R.G., Aerts J.M., Hodkinson M., Adams D.J.,
RA Shiomi K., Omura S., van Aalten D.M.;
RT "Specificity and affinity of natural product cyclopentapeptide inhibitors
RT against A. fumigatus, human, and bacterial chitinases.";
RL Chem. Biol. 12:65-76(2005).
RN [10]
RP VARIANTS LYS-74 AND SER-102.
RX PubMed=17464953; DOI=10.1002/humu.20524;
RA Grace M.E., Balwani M., Nazarenko I., Prakash-Cheng A., Desnick R.J.;
RT "Type 1 Gaucher disease: null and hypomorphic novel chitotriosidase
RT mutations-implications for diagnosis and therapeutic monitoring.";
RL Hum. Mutat. 28:866-873(2007).
RN [11]
RP CHARACTERIZATION OF VARIANT SER-102, SUBCELLULAR LOCATION, CATALYTIC
RP ACTIVITY, AND GLYCOSYLATION AT ASN-100.
RX PubMed=19725875; DOI=10.1111/j.1742-4658.2009.07259.x;
RA Bussink A.P., Verhoek M., Vreede J., Ghauharali-van der Vlugt K.,
RA Donker-Koopman W.E., Sprenger R.R., Hollak C.E., Aerts J.M., Boot R.G.;
RT "Common G102S polymorphism in chitotriosidase differentially affects
RT activity towards 4-methylumbelliferyl substrates.";
RL FEBS J. 276:5678-5688(2009).
CC -!- FUNCTION: Degrades chitin, chitotriose and chitobiose. May participate
CC in the defense against nematodes and other pathogens. Isoform 3 has no
CC enzymatic activity. {ECO:0000269|PubMed:7592832,
CC ECO:0000269|PubMed:7836450}.
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:0000269|PubMed:15664516, ECO:0000269|PubMed:19725875,
CC ECO:0000269|PubMed:7836450};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11960986,
CC ECO:0000269|PubMed:12639956, ECO:0000269|PubMed:15664516}.
CC -!- SUBCELLULAR LOCATION: Secreted. Lysosome. Note=A small proportion is
CC lysosomal.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q13231-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q13231-2; Sequence=VSP_008631, VSP_008632;
CC Name=3;
CC IsoId=Q13231-3; Sequence=VSP_008633;
CC Name=4;
CC IsoId=Q13231-4; Sequence=VSP_044816;
CC -!- TISSUE SPECIFICITY: Detected in spleen. Secreted by cultured
CC macrophages. {ECO:0000269|PubMed:7836450}.
CC -!- POLYMORPHISM: A 24 bp duplication in exon 10 leads to the activation of
CC an alternative splice site and the production of an inactive protein
CC resulting in chitotriosidase deficiency [MIM:614122]. About 6% of the
CC population are deficient for CHIT1 activity, while 35% are carriers and
CC show reduced enzyme levels. People with CHIT1 deficiency appear
CC perfectly healthy. {ECO:0000269|PubMed:9748235}.
CC -!- MISCELLANEOUS: Very high plasma levels of CHIT1 are found in patients
CC with Gaucher disease type 1 (GD I). Can be used as diagnostic aid and
CC to evaluate the success of treatment that brings levels back to normal.
CC -!- MISCELLANEOUS: [Isoform 3]: Duplication of 24 bp in exon 10 leads to
CC the use of a cryptic splice site. The normal splice site is still
CC present but not used. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class II subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAG51478.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={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; U29615; AAC50246.1; -; mRNA.
DR EMBL; U62662; AAG10644.1; -; mRNA.
DR EMBL; AK055165; BAG51478.1; ALT_INIT; mRNA.
DR EMBL; AC105940; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL359090; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC069614; AAH69614.1; -; mRNA.
DR EMBL; BC103695; AAI03696.1; -; mRNA.
DR EMBL; BC105680; AAI05681.1; -; mRNA.
DR EMBL; BC105681; AAI05682.1; -; mRNA.
DR EMBL; BC105682; AAI05683.1; -; mRNA.
DR CCDS; CCDS1436.1; -. [Q13231-1]
DR CCDS; CCDS58057.1; -. [Q13231-4]
DR RefSeq; NP_001243054.2; NM_001256125.1. [Q13231-4]
DR RefSeq; NP_003456.1; NM_003465.2. [Q13231-1]
DR PDB; 1GUV; X-ray; 2.35 A; A=22-387.
DR PDB; 1HKI; X-ray; 2.55 A; A=22-386.
DR PDB; 1HKJ; X-ray; 2.60 A; A=22-386.
DR PDB; 1HKK; X-ray; 1.85 A; A=22-385.
DR PDB; 1HKM; X-ray; 2.55 A; A=22-386.
DR PDB; 1LG1; X-ray; 2.78 A; A=22-386.
DR PDB; 1LG2; X-ray; 2.10 A; A=22-386.
DR PDB; 1LQ0; X-ray; 2.20 A; A=22-386.
DR PDB; 1WAW; X-ray; 1.75 A; A=22-466.
DR PDB; 1WB0; X-ray; 1.65 A; A=22-466.
DR PDB; 4WJX; X-ray; 1.00 A; A=22-387.
DR PDB; 4WK9; X-ray; 1.10 A; A=22-387.
DR PDB; 4WKA; X-ray; 0.95 A; A=22-386.
DR PDB; 4WKF; X-ray; 1.10 A; A=22-387.
DR PDB; 4WKH; X-ray; 1.05 A; A=22-387.
DR PDB; 5HBF; X-ray; 1.95 A; A/B=1-466.
DR PDB; 5NR8; X-ray; 1.35 A; A=22-387.
DR PDB; 5NRA; X-ray; 1.27 A; A=22-387.
DR PDB; 5NRF; X-ray; 1.45 A; A=22-387.
DR PDB; 6JJR; X-ray; 1.83 A; A=22-396.
DR PDB; 6JK6; X-ray; 1.57 A; A=22-396.
DR PDB; 6SO0; NMR; -; A=418-466.
DR PDB; 6ZE8; X-ray; 1.50 A; A/B/C/D/E/F=22-386.
DR PDBsum; 1GUV; -.
DR PDBsum; 1HKI; -.
DR PDBsum; 1HKJ; -.
DR PDBsum; 1HKK; -.
DR PDBsum; 1HKM; -.
DR PDBsum; 1LG1; -.
DR PDBsum; 1LG2; -.
DR PDBsum; 1LQ0; -.
DR PDBsum; 1WAW; -.
DR PDBsum; 1WB0; -.
DR PDBsum; 4WJX; -.
DR PDBsum; 4WK9; -.
DR PDBsum; 4WKA; -.
DR PDBsum; 4WKF; -.
DR PDBsum; 4WKH; -.
DR PDBsum; 5HBF; -.
DR PDBsum; 5NR8; -.
DR PDBsum; 5NRA; -.
DR PDBsum; 5NRF; -.
DR PDBsum; 6JJR; -.
DR PDBsum; 6JK6; -.
DR PDBsum; 6SO0; -.
DR PDBsum; 6ZE8; -.
DR AlphaFoldDB; Q13231; -.
DR SMR; Q13231; -.
DR BioGRID; 107542; 13.
DR IntAct; Q13231; 5.
DR STRING; 9606.ENSP00000356198; -.
DR BindingDB; Q13231; -.
DR ChEMBL; CHEMBL3080; -.
DR DrugBank; DB03539; 2-(Acetylamino)-2-Deoxy-6-O-Methyl-Alpha-D-Allopyranose.
DR DrugBank; DB03109; 2-acetylamino-2-deoxy-b-D-allopyranose.
DR DrugBank; DB04404; Allosamizoline.
DR DrugBank; DB04350; Argadin.
DR DrugBank; DB03632; Argifin.
DR GuidetoPHARMACOLOGY; 3187; -.
DR CAZy; CBM14; Carbohydrate-Binding Module Family 14.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR GlyGen; Q13231; 2 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q13231; -.
DR PhosphoSitePlus; Q13231; -.
DR BioMuta; CHIT1; -.
DR DMDM; 37999493; -.
DR MassIVE; Q13231; -.
DR PaxDb; Q13231; -.
DR PeptideAtlas; Q13231; -.
DR PRIDE; Q13231; -.
DR ProteomicsDB; 59236; -. [Q13231-1]
DR ProteomicsDB; 59237; -. [Q13231-2]
DR ProteomicsDB; 59238; -. [Q13231-3]
DR Antibodypedia; 2441; 244 antibodies from 34 providers.
DR DNASU; 1118; -.
DR Ensembl; ENST00000255427.7; ENSP00000255427.3; ENSG00000133063.16. [Q13231-4]
DR Ensembl; ENST00000367229.6; ENSP00000356198.1; ENSG00000133063.16. [Q13231-1]
DR Ensembl; ENST00000491855.5; ENSP00000423778.1; ENSG00000133063.16. [Q13231-2]
DR GeneID; 1118; -.
DR KEGG; hsa:1118; -.
DR MANE-Select; ENST00000367229.6; ENSP00000356198.1; NM_003465.3; NP_003456.1.
DR UCSC; uc001gzn.3; human. [Q13231-1]
DR CTD; 1118; -.
DR DisGeNET; 1118; -.
DR GeneCards; CHIT1; -.
DR HGNC; HGNC:1936; CHIT1.
DR HPA; ENSG00000133063; Tissue enhanced (bone marrow, lung, lymphoid tissue).
DR MalaCards; CHIT1; -.
DR MIM; 600031; gene.
DR MIM; 614122; phenotype.
DR neXtProt; NX_Q13231; -.
DR OpenTargets; ENSG00000133063; -.
DR PharmGKB; PA26467; -.
DR VEuPathDB; HostDB:ENSG00000133063; -.
DR eggNOG; KOG2806; Eukaryota.
DR GeneTree; ENSGT00940000161149; -.
DR HOGENOM; CLU_002833_3_1_1; -.
DR InParanoid; Q13231; -.
DR OMA; QRFTDMV; -.
DR OrthoDB; 1289629at2759; -.
DR PhylomeDB; Q13231; -.
DR TreeFam; TF315610; -.
DR PathwayCommons; Q13231; -.
DR Reactome; R-HSA-189085; Digestion of dietary carbohydrate.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; Q13231; -.
DR BioGRID-ORCS; 1118; 7 hits in 1069 CRISPR screens.
DR ChiTaRS; CHIT1; human.
DR EvolutionaryTrace; Q13231; -.
DR GenomeRNAi; 1118; -.
DR Pharos; Q13231; Tchem.
DR PRO; PR:Q13231; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q13231; protein.
DR Bgee; ENSG00000133063; Expressed in bone marrow and 108 other tissues.
DR ExpressionAtlas; Q13231; baseline and differential.
DR Genevisible; Q13231; HS.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0035580; C:specific granule lumen; TAS:Reactome.
DR GO; GO:1904724; C:tertiary granule lumen; TAS:Reactome.
DR GO; GO:0008061; F:chitin binding; IBA:GO_Central.
DR GO; GO:0004568; F:chitinase activity; IDA:UniProtKB.
DR GO; GO:0008843; F:endochitinase activity; IDA:UniProtKB.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; TAS:Reactome.
DR GO; GO:0006032; P:chitin catabolic process; IDA:UniProtKB.
DR GO; GO:0006955; P:immune response; NAS:UniProtKB.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0044245; P:polysaccharide digestion; TAS:Reactome.
DR GO; GO:0009617; P:response to bacterium; TAS:ProtInc.
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 3D-structure; Alternative splicing; Carbohydrate metabolism;
KW Chitin degradation; Chitin-binding; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Lysosome;
KW Polysaccharide degradation; Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:7836450"
FT CHAIN 22..466
FT /note="Chitotriosidase-1"
FT /id="PRO_0000011941"
FT DOMAIN 22..388
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT DOMAIN 417..466
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT REGION 392..424
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 358
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine; in variant S-102"
FT /evidence="ECO:0000269|PubMed:19725875"
FT DISULFID 26..51
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258,
FT ECO:0000269|PubMed:11960986"
FT DISULFID 307..370
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144,
FT ECO:0000269|PubMed:11960986"
FT DISULFID 450..463
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT VAR_SEQ 87..105
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044816"
FT VAR_SEQ 344..372
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_008633"
FT VAR_SEQ 386..387
FT /note="SL -> NG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7592832"
FT /id="VSP_008631"
FT VAR_SEQ 388..466
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7592832"
FT /id="VSP_008632"
FT VARIANT 40
FT /note="R -> H (in dbSNP:rs35920428)"
FT /id="VAR_049190"
FT VARIANT 74
FT /note="E -> K (rare variant detected in patients with
FT Gaucher disease type 1; dbSNP:rs137852607)"
FT /evidence="ECO:0000269|PubMed:17464953"
FT /id="VAR_065914"
FT VARIANT 102
FT /note="G -> S (common variant detected in patients with
FT Gaucher disease type 1 as well as healthy individuals;
FT slightly reduced activity towards 4-methylumbelliferyl-
FT chitotrioside but no effect on activity towards 4-
FT methylumbelliferyl-deoxychitobioside; dbSNP:rs2297950)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:17464953, ECO:0000269|PubMed:19725875"
FT /id="VAR_022138"
FT VARIANT 171
FT /note="Q -> H (in dbSNP:rs12562058)"
FT /id="VAR_049191"
FT VARIANT 442
FT /note="A -> G (in dbSNP:rs1065761)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_024458"
FT STRAND 23..29
FT /evidence="ECO:0007829|PDB:4WKA"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:4WKA"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:4WKA"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:4WKA"
FT TURN 48..50
FT /evidence="ECO:0007829|PDB:4WKH"
FT STRAND 52..62
FT /evidence="ECO:0007829|PDB:4WKA"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:4WKA"
FT HELIX 73..86
FT /evidence="ECO:0007829|PDB:4WKA"
FT STRAND 91..97
FT /evidence="ECO:0007829|PDB:4WKA"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:4WKA"
FT HELIX 104..110
FT /evidence="ECO:0007829|PDB:4WKA"
FT HELIX 113..130
FT /evidence="ECO:0007829|PDB:4WKA"
FT STRAND 133..138
FT /evidence="ECO:0007829|PDB:4WKA"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:1HKI"
FT HELIX 151..173
FT /evidence="ECO:0007829|PDB:4WKA"
FT STRAND 179..185
FT /evidence="ECO:0007829|PDB:4WKA"
FT HELIX 188..194
FT /evidence="ECO:0007829|PDB:4WKA"
FT HELIX 197..201
FT /evidence="ECO:0007829|PDB:4WKA"
FT STRAND 205..210
FT /evidence="ECO:0007829|PDB:4WKA"
FT STRAND 219..221
FT /evidence="ECO:0007829|PDB:4WKA"
FT HELIX 236..240
FT /evidence="ECO:0007829|PDB:4WKA"
FT HELIX 243..252
FT /evidence="ECO:0007829|PDB:4WKA"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:4WKA"
FT STRAND 260..274
FT /evidence="ECO:0007829|PDB:4WKA"
FT STRAND 284..288
FT /evidence="ECO:0007829|PDB:4WKA"
FT TURN 293..295
FT /evidence="ECO:0007829|PDB:4WKA"
FT STRAND 300..302
FT /evidence="ECO:0007829|PDB:4WKA"
FT HELIX 303..306
FT /evidence="ECO:0007829|PDB:4WKA"
FT STRAND 313..317
FT /evidence="ECO:0007829|PDB:4WKA"
FT TURN 318..321
FT /evidence="ECO:0007829|PDB:4WKA"
FT STRAND 322..327
FT /evidence="ECO:0007829|PDB:4WKA"
FT STRAND 330..333
FT /evidence="ECO:0007829|PDB:4WKA"
FT HELIX 337..349
FT /evidence="ECO:0007829|PDB:4WKA"
FT STRAND 353..358
FT /evidence="ECO:0007829|PDB:4WKA"
FT HELIX 360..362
FT /evidence="ECO:0007829|PDB:4WKA"
FT STRAND 367..372
FT /evidence="ECO:0007829|PDB:4WKA"
FT HELIX 376..384
FT /evidence="ECO:0007829|PDB:4WKA"
FT TURN 419..422
FT /evidence="ECO:0007829|PDB:5HBF"
FT STRAND 425..430
FT /evidence="ECO:0007829|PDB:5HBF"
FT STRAND 433..441
FT /evidence="ECO:0007829|PDB:5HBF"
FT STRAND 444..449
FT /evidence="ECO:0007829|PDB:5HBF"
FT STRAND 455..457
FT /evidence="ECO:0007829|PDB:5HBF"
FT TURN 458..461
FT /evidence="ECO:0007829|PDB:5HBF"
FT STRAND 462..464
FT /evidence="ECO:0007829|PDB:5HBF"
SQ SEQUENCE 466 AA; 51681 MW; B4312D1E885E386D CRC64;
MVRSVAWAGF MVLLMIPWGS AAKLVCYFTN WAQYRQGEAR FLPKDLDPSL CTHLIYAFAG
MTNHQLSTTE WNDETLYQEF NGLKKMNPKL KTLLAIGGWN FGTQKFTDMV ATANNRQTFV
NSAIRFLRKY SFDGLDLDWE YPGSQGSPAV DKERFTTLVQ DLANAFQQEA QTSGKERLLL
SAAVPAGQTY VDAGYEVDKI AQNLDFVNLM AYDFHGSWEK VTGHNSPLYK RQEESGAAAS
LNVDAAVQQW LQKGTPASKL ILGMPTYGRS FTLASSSDTR VGAPATGSGT PGPFTKEGGM
LAYYEVCSWK GATKQRIQDQ KVPYIFRDNQ WVGFDDVESF KTKVSYLKQK GLGGAMVWAL
DLDDFAGFSC NQGRYPLIQT LRQELSLPYL PSGTPELEVP KPGQPSEPEH GPSPGQDTFC
QGKADGLYPN PRERSSFYSC AAGRLFQQSC PTGLVFSNSC KCCTWN
