CHIA_HUMAN
ID CHIA_HUMAN Reviewed; 476 AA.
AC Q9BZP6; Q32W79; Q32W80; Q3B866; Q5U5Z5; Q5VUV4; Q86UD8; Q9ULY3; Q9ULY4;
DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Acidic mammalian chitinase;
DE Short=AMCase;
DE EC=3.2.1.14;
DE AltName: Full=Lung-specific protein TSA1902;
DE Flags: Precursor;
GN Name=CHIA;
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 2 AND 3), AND VARIANTS VAL-339 AND
RP GLY-432.
RC TISSUE=Lung;
RX PubMed=10548734; DOI=10.1016/s0378-1119(99)00394-7;
RA Saito A., Ozaki K., Fujiwara T., Nakamura Y., Tanigami A.;
RT "Isolation and mapping of a human lung-specific gene, TSA1902, encoding a
RT novel chitinase family member.";
RL Gene 239:325-331(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=11085997; DOI=10.1074/jbc.m009886200;
RA Boot R.G., Blommaart E.F.C., Swart E., Ghauharali-van der Vlugt K.,
RA Bijl N., Moe C., Place A., Aerts J.M.F.G.;
RT "Identification of a novel acidic mammalian chitinase distinct from
RT chitotriosidase.";
RL J. Biol. Chem. 276:6770-6778(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Kidney;
RA Chen X.H., Cai G.P.;
RT "A novel chitinase family member.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [6]
RP INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=15192232; DOI=10.1126/science.1095336;
RA Zhu Z., Zheng T., Homer R.J., Kim Y.K., Chen N.Y., Cohn L., Hamid Q.,
RA Elias J.A.;
RT "Acidic mammalian chitinase in asthmatic Th2 inflammation and IL-13 pathway
RT activation.";
RL Science 304:1678-1682(2004).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH EGFR, AND SUBCELLULAR
RP LOCATION.
RX PubMed=18824549; DOI=10.1074/jbc.m805574200;
RA Hartl D., He C.H., Koller B., Da Silva C.A., Homer R., Lee C.G.,
RA Elias J.A.;
RT "Acidic mammalian chitinase is secreted via an ADAM17/epidermal growth
RT factor receptor-dependent pathway and stimulates chemokine production by
RT pulmonary epithelial cells.";
RL J. Biol. Chem. 283:33472-33482(2008).
RN [8]
RP FUNCTION, AND MUTAGENESIS OF ASP-138.
RX PubMed=19342690; DOI=10.4049/jimmunol.0803446;
RA Hartl D., He C.H., Koller B., Da Silva C.A., Kobayashi Y., Lee C.G.,
RA Flavell R.A., Elias J.A.;
RT "Acidic mammalian chitinase regulates epithelial cell apoptosis via a
RT chitinolytic-independent mechanism.";
RL J. Immunol. 182:5098-5106(2009).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 22-408 IN COMPLEX WITH
RP METHYLALLOSAMIDIN, CATALYTIC ACTIVITY, AND DISULFIDE BONDS.
RX PubMed=19241384; DOI=10.1002/pro.63;
RA Olland A.M., Strand J., Presman E., Czerwinski R., Joseph-McCarthy D.,
RA Krykbaev R., Schlingmann G., Chopra R., Lin L., Fleming M., Kriz R.,
RA Stahl M., Somers W., Fitz L., Mosyak L.;
RT "Triad of polar residues implicated in pH specificity of acidic mammalian
RT chitinase.";
RL Protein Sci. 18:569-578(2009).
RN [10]
RP VARIANTS ASP-45; ASN-47; MET-61; ARG-102; ARG-125; VAL-339; SER-354 AND
RP GLY-432, CATALYTIC ACTIVITY, FUNCTION, AND CHARACTERIZATION OF VARIANTS
RP ASP-45; ASN-47 AND MET-61.
RX PubMed=19435888; DOI=10.1074/jbc.m109.012443;
RA Seibold M.A., Reese T.A., Choudhry S., Salam M.T., Beckman K., Eng C.,
RA Atakilit A., Meade K., Lenoir M., Watson H.G., Thyne S., Kumar R.,
RA Weiss K.B., Grammer L.C., Avila P., Schleimer R.P., Fahy J.V.,
RA Rodriguez-Santana J., Rodriguez-Cintron W., Boot R.G., Sheppard D.,
RA Gilliland F.D., Locksley R.M., Burchard E.G.;
RT "Differential enzymatic activity of common haplotypic versions of the human
RT acidic mammalian chitinase protein.";
RL J. Biol. Chem. 284:19650-19658(2009).
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.
CC {ECO:0000269|PubMed:11085997, ECO:0000269|PubMed:18824549,
CC ECO:0000269|PubMed:19342690, ECO:0000269|PubMed:19435888}.
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:18824549, ECO:0000269|PubMed:19241384,
CC ECO:0000269|PubMed:19435888};
CC -!- SUBUNIT: Interacts with EGFR. {ECO:0000269|PubMed:18824549,
CC ECO:0000269|PubMed:19241384}.
CC -!- INTERACTION:
CC Q9BZP6; Q5RI15: COX20; NbExp=3; IntAct=EBI-14357960, EBI-2834035;
CC Q9BZP6; P00533: EGFR; NbExp=2; IntAct=EBI-14357960, EBI-297353;
CC Q9BZP6; Q8NC74: RBBP8NL; NbExp=3; IntAct=EBI-14357960, EBI-11322432;
CC Q9BZP6; Q92609: TBC1D5; NbExp=3; IntAct=EBI-14357960, EBI-742381;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Secreted. Note=Secretion depends on
CC EGFR activity.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9BZP6-1; Sequence=Displayed;
CC Name=2; Synonyms=TSA1902-L;
CC IsoId=Q9BZP6-2; Sequence=VSP_008635;
CC Name=3; Synonyms=TSA1902-S;
CC IsoId=Q9BZP6-3; Sequence=VSP_008634;
CC -!- TISSUE SPECIFICITY: Detected in lung epithelial cells from asthma
CC patients (at protein level). Highly expressed in stomach. Detected at
CC lower levels in lung. {ECO:0000269|PubMed:11085997,
CC ECO:0000269|PubMed:15192232}.
CC -!- INDUCTION: Up-regulated in lung epithelial cells from asthma patients.
CC {ECO:0000269|PubMed:15192232}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class II subfamily. {ECO:0000305}.
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DR EMBL; AB025008; BAA86980.1; -; mRNA.
DR EMBL; AB025009; BAA86981.1; -; mRNA.
DR EMBL; AF290004; AAG60019.1; -; mRNA.
DR EMBL; AY789444; AAX81431.1; -; mRNA.
DR EMBL; AY789445; AAX81432.1; -; mRNA.
DR EMBL; AL513202; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL356387; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC047336; AAH47336.2; -; mRNA.
DR EMBL; BC036339; AAH36339.2; -; mRNA.
DR EMBL; BC106910; AAI06911.1; -; mRNA.
DR CCDS; CCDS41368.1; -. [Q9BZP6-1]
DR CCDS; CCDS58017.1; -. [Q9BZP6-3]
DR CCDS; CCDS832.1; -. [Q9BZP6-2]
DR RefSeq; NP_001035713.1; NM_001040623.2. [Q9BZP6-3]
DR RefSeq; NP_001244930.1; NM_001258001.1. [Q9BZP6-2]
DR RefSeq; NP_001244931.1; NM_001258002.1. [Q9BZP6-3]
DR RefSeq; NP_001244932.1; NM_001258003.1. [Q9BZP6-2]
DR RefSeq; NP_001244933.1; NM_001258004.1. [Q9BZP6-3]
DR RefSeq; NP_001244934.1; NM_001258005.1. [Q9BZP6-3]
DR RefSeq; NP_068569.2; NM_021797.3. [Q9BZP6-2]
DR RefSeq; NP_970615.2; NM_201653.3. [Q9BZP6-1]
DR RefSeq; XP_006710640.1; XM_006710577.3. [Q9BZP6-3]
DR RefSeq; XP_016856536.1; XM_017001047.1. [Q9BZP6-3]
DR RefSeq; XP_016856537.1; XM_017001048.1. [Q9BZP6-2]
DR PDB; 2YBT; X-ray; 2.22 A; A/B/C/D/E/F=21-398.
DR PDB; 2YBU; X-ray; 2.25 A; A/B/C/D/E/F=21-398.
DR PDB; 3FXY; X-ray; 2.00 A; A/B/C/D=22-408.
DR PDB; 3FY1; X-ray; 1.70 A; A/B=22-408.
DR PDB; 3RM4; X-ray; 1.90 A; A/B=22-408.
DR PDB; 3RM8; X-ray; 1.80 A; A/B=22-408.
DR PDB; 3RM9; X-ray; 2.10 A; A/B=22-408.
DR PDB; 3RME; X-ray; 1.80 A; A/B=22-408.
DR PDBsum; 2YBT; -.
DR PDBsum; 2YBU; -.
DR PDBsum; 3FXY; -.
DR PDBsum; 3FY1; -.
DR PDBsum; 3RM4; -.
DR PDBsum; 3RM8; -.
DR PDBsum; 3RM9; -.
DR PDBsum; 3RME; -.
DR AlphaFoldDB; Q9BZP6; -.
DR SMR; Q9BZP6; -.
DR BioGRID; 118039; 41.
DR IntAct; Q9BZP6; 17.
DR STRING; 9606.ENSP00000358755; -.
DR BindingDB; Q9BZP6; -.
DR ChEMBL; CHEMBL1293197; -.
DR GuidetoPHARMACOLOGY; 2982; -.
DR CAZy; CBM14; Carbohydrate-Binding Module Family 14.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR iPTMnet; Q9BZP6; -.
DR PhosphoSitePlus; Q9BZP6; -.
DR BioMuta; CHIA; -.
DR DMDM; 37999771; -.
DR MassIVE; Q9BZP6; -.
DR PaxDb; Q9BZP6; -.
DR PeptideAtlas; Q9BZP6; -.
DR PRIDE; Q9BZP6; -.
DR ProteomicsDB; 79883; -. [Q9BZP6-1]
DR ProteomicsDB; 79884; -. [Q9BZP6-2]
DR ProteomicsDB; 79885; -. [Q9BZP6-3]
DR ABCD; Q9BZP6; 4 sequenced antibodies.
DR Antibodypedia; 33803; 253 antibodies from 24 providers.
DR DNASU; 27159; -.
DR Ensembl; ENST00000343320.10; ENSP00000341828.6; ENSG00000134216.19. [Q9BZP6-1]
DR Ensembl; ENST00000353665.10; ENSP00000338970.7; ENSG00000134216.19. [Q9BZP6-3]
DR Ensembl; ENST00000369740.6; ENSP00000358755.1; ENSG00000134216.19. [Q9BZP6-1]
DR Ensembl; ENST00000430615.1; ENSP00000391132.1; ENSG00000134216.19. [Q9BZP6-2]
DR Ensembl; ENST00000451398.6; ENSP00000390476.2; ENSG00000134216.19. [Q9BZP6-3]
DR Ensembl; ENST00000483391.5; ENSP00000436946.1; ENSG00000134216.19. [Q9BZP6-3]
DR GeneID; 27159; -.
DR KEGG; hsa:27159; -.
DR MANE-Select; ENST00000369740.6; ENSP00000358755.1; NM_201653.4; NP_970615.2.
DR UCSC; uc001eas.5; human. [Q9BZP6-1]
DR CTD; 27159; -.
DR DisGeNET; 27159; -.
DR GeneCards; CHIA; -.
DR HGNC; HGNC:17432; CHIA.
DR HPA; ENSG00000134216; Tissue enriched (stomach).
DR MIM; 606080; gene.
DR neXtProt; NX_Q9BZP6; -.
DR OpenTargets; ENSG00000134216; -.
DR PharmGKB; PA142672117; -.
DR VEuPathDB; HostDB:ENSG00000134216; -.
DR eggNOG; KOG2806; Eukaryota.
DR GeneTree; ENSGT00940000154557; -.
DR HOGENOM; CLU_002833_3_1_1; -.
DR InParanoid; Q9BZP6; -.
DR OMA; NPMTYDF; -.
DR PhylomeDB; Q9BZP6; -.
DR TreeFam; TF315610; -.
DR BRENDA; 3.2.1.14; 2681.
DR PathwayCommons; Q9BZP6; -.
DR Reactome; R-HSA-189085; Digestion of dietary carbohydrate.
DR SignaLink; Q9BZP6; -.
DR BioGRID-ORCS; 27159; 7 hits in 1068 CRISPR screens.
DR EvolutionaryTrace; Q9BZP6; -.
DR GenomeRNAi; 27159; -.
DR Pharos; Q9BZP6; Tchem.
DR PRO; PR:Q9BZP6; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9BZP6; protein.
DR Bgee; ENSG00000134216; Expressed in cardia of stomach and 98 other tissues.
DR ExpressionAtlas; Q9BZP6; baseline and differential.
DR Genevisible; Q9BZP6; HS.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0008061; F:chitin binding; IBA:GO_Central.
DR GO; GO:0004568; F:chitinase activity; IDA:UniProtKB.
DR GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0006032; P:chitin catabolic process; IDA:UniProtKB.
DR GO; GO:0006030; P:chitin metabolic process; NAS: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:0044245; P:polysaccharide digestion; TAS:Reactome.
DR GO; GO:0032722; P:positive regulation of chemokine production; IDA:UniProtKB.
DR GO; GO:0002532; P:production of molecular mediator involved in inflammatory response; IDA: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 3D-structure; Alternative splicing; Apoptosis; Carbohydrate metabolism;
KW Chitin degradation; Chitin-binding; Cytoplasm; Disulfide bond; Glycosidase;
KW Hydrolase; Immunity; Inflammatory response; Polysaccharide degradation;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000250"
FT CHAIN 22..476
FT /note="Acidic mammalian chitinase"
FT /id="PRO_0000011944"
FT DOMAIN 22..390
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT DOMAIN 427..476
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
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 ECO:0000269|PubMed:19241384"
FT DISULFID 49..394
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144,
FT ECO:0000269|PubMed:19241384"
FT DISULFID 307..372
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144,
FT ECO:0000269|PubMed:19241384"
FT VAR_SEQ 1..161
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10548734, ECO:0000303|Ref.3"
FT /id="VSP_008634"
FT VAR_SEQ 1..108
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10548734,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.3"
FT /id="VSP_008635"
FT VARIANT 45
FT /note="N -> D (increased chitinase activity; when
FT associated with N-47 and M-61; dbSNP:rs41282492)"
FT /evidence="ECO:0000269|PubMed:19435888"
FT /id="VAR_063030"
FT VARIANT 47
FT /note="D -> N (increased chitinase activity; when
FT associated with D-45 and M-61; dbSNP:rs41282494)"
FT /evidence="ECO:0000269|PubMed:19435888"
FT /id="VAR_063031"
FT VARIANT 61
FT /note="R -> M (increased chitinase activity; when
FT associated with D-45 and N-47; dbSNP:rs41282496)"
FT /evidence="ECO:0000269|PubMed:19435888"
FT /id="VAR_063032"
FT VARIANT 102
FT /note="G -> R (in dbSNP:rs3818822)"
FT /evidence="ECO:0000269|PubMed:19435888"
FT /id="VAR_049192"
FT VARIANT 125
FT /note="K -> R (in dbSNP:rs61756687)"
FT /evidence="ECO:0000269|PubMed:19435888"
FT /id="VAR_063033"
FT VARIANT 324
FT /note="V -> G (in dbSNP:rs2256721)"
FT /id="VAR_033730"
FT VARIANT 339
FT /note="I -> V (in dbSNP:rs2275253)"
FT /evidence="ECO:0000269|PubMed:10548734,
FT ECO:0000269|PubMed:19435888"
FT /id="VAR_049193"
FT VARIANT 354
FT /note="F -> S (in dbSNP:rs2275254)"
FT /evidence="ECO:0000269|PubMed:19435888"
FT /id="VAR_049194"
FT VARIANT 377
FT /note="F -> L (in dbSNP:rs36011905)"
FT /id="VAR_049195"
FT VARIANT 432
FT /note="V -> G (in dbSNP:rs2256721)"
FT /evidence="ECO:0000269|PubMed:10548734,
FT ECO:0000269|PubMed:19435888"
FT /id="VAR_049196"
FT MUTAGEN 138
FT /note="D->A: Loss of chitinase activity. No effect on
FT protection against apoptosis or on AKT1 activation."
FT /evidence="ECO:0000269|PubMed:19342690"
FT CONFLICT 203
FT /note="Y -> C (in Ref. 3; AAX81431)"
FT /evidence="ECO:0000305"
FT STRAND 23..29
FT /evidence="ECO:0007829|PDB:3FY1"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:3FY1"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:3FY1"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:3FY1"
FT TURN 48..50
FT /evidence="ECO:0007829|PDB:3RM8"
FT STRAND 52..62
FT /evidence="ECO:0007829|PDB:3FY1"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:3FY1"
FT HELIX 73..82
FT /evidence="ECO:0007829|PDB:3FY1"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:3FY1"
FT STRAND 91..97
FT /evidence="ECO:0007829|PDB:3FY1"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:3FY1"
FT HELIX 104..110
FT /evidence="ECO:0007829|PDB:3FY1"
FT HELIX 113..130
FT /evidence="ECO:0007829|PDB:3FY1"
FT STRAND 133..138
FT /evidence="ECO:0007829|PDB:3FY1"
FT HELIX 151..173
FT /evidence="ECO:0007829|PDB:3FY1"
FT STRAND 179..184
FT /evidence="ECO:0007829|PDB:3FY1"
FT HELIX 188..194
FT /evidence="ECO:0007829|PDB:3FY1"
FT HELIX 197..203
FT /evidence="ECO:0007829|PDB:3FY1"
FT STRAND 205..209
FT /evidence="ECO:0007829|PDB:3FY1"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:3FY1"
FT HELIX 236..240
FT /evidence="ECO:0007829|PDB:3FY1"
FT HELIX 243..252
FT /evidence="ECO:0007829|PDB:3FY1"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:3FY1"
FT STRAND 260..275
FT /evidence="ECO:0007829|PDB:3FY1"
FT STRAND 284..288
FT /evidence="ECO:0007829|PDB:3FY1"
FT TURN 293..295
FT /evidence="ECO:0007829|PDB:3FY1"
FT STRAND 300..302
FT /evidence="ECO:0007829|PDB:3FY1"
FT HELIX 303..311
FT /evidence="ECO:0007829|PDB:3FY1"
FT STRAND 315..319
FT /evidence="ECO:0007829|PDB:3FY1"
FT TURN 320..323
FT /evidence="ECO:0007829|PDB:3FY1"
FT STRAND 324..329
FT /evidence="ECO:0007829|PDB:3FY1"
FT STRAND 332..335
FT /evidence="ECO:0007829|PDB:3FY1"
FT HELIX 339..351
FT /evidence="ECO:0007829|PDB:3FY1"
FT STRAND 355..360
FT /evidence="ECO:0007829|PDB:3FY1"
FT HELIX 362..364
FT /evidence="ECO:0007829|PDB:3FY1"
FT STRAND 367..369
FT /evidence="ECO:0007829|PDB:3FY1"
FT TURN 370..372
FT /evidence="ECO:0007829|PDB:3FY1"
FT HELIX 378..386
FT /evidence="ECO:0007829|PDB:3FY1"
FT HELIX 392..394
FT /evidence="ECO:0007829|PDB:3FXY"
SQ SEQUENCE 476 AA; 52271 MW; 92B27BAD2F7EB4CC CRC64;
MTKLILLTGL VLILNLQLGS AYQLTCYFTN WAQYRPGLGR FMPDNIDPCL CTHLIYAFAG
RQNNEITTIE WNDVTLYQAF NGLKNKNSQL KTLLAIGGWN FGTAPFTAMV STPENRQTFI
TSVIKFLRQY EFDGLDFDWE YPGSRGSPPQ DKHLFTVLVQ EMREAFEQEA KQINKPRLMV
TAAVAAGISN IQSGYEIPQL SQYLDYIHVM TYDLHGSWEG YTGENSPLYK YPTDTGSNAY
LNVDYVMNYW KDNGAPAEKL IVGFPTYGHN FILSNPSNTG IGAPTSGAGP AGPYAKESGI
WAYYEICTFL KNGATQGWDA PQEVPYAYQG NVWVGYDNIK SFDIKAQWLK HNKFGGAMVW
AIDLDDFTGT FCNQGKFPLI STLKKALGLQ SASCTAPAQP IEPITAAPSG SGNGSGSSSS
GGSSGGSGFC AVRANGLYPV ANNRNAFWHC VNGVTYQQNC QAGLVFDTSC DCCNWA
