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Database: UniProt
Entry: Q9BZP6
LinkDB: Q9BZP6
Original site: Q9BZP6 
ID   CHIA_HUMAN              Reviewed;         476 AA.
AC   Q9BZP6; Q32W79; Q32W80; Q3B866; Q5U5Z5; Q5VUV4; Q86UD8; Q9ULY3;
AC   Q9ULY4;
DT   24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   01-OCT-2014, entry version 132.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), AND VARIANTS VAL-339
RP   AND 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,
RT   encoding a novel chitinase family member.";
RL   Gene 239:325-331(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE
RP   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.,
RA   Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA   Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA   McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA   Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA   Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA   Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA   Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA   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.,
RA   Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA   Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA   Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA   Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA   Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA   Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA   Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA   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.,
RA   Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA   Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA   Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA   Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA   Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA   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
RT   project: 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
RT   pathway 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
RT   by 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
RT   mammalian 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
RP   AND GLY-432, CATALYTIC ACTIVITY, FUNCTION, AND CHARACTERIZATION OF
RP   VARIANTS 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
RT   human 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
CC       in T-helper cell type 2 (Th2) immune response. Contributes to the
CC       response to IL-13 and inflammation in response to IL-13.
CC       Stimulates chemokine production by pulmonary epithelial cells.
CC       Protects lung epithelial cells against apoptosis and promotes
CC       phosphorylation of AKT1. Its function in the inflammatory response
CC       and in protecting cells against apoptosis is inhibited by
CC       allosamidin, suggesting that the function of this protein depends
CC       on carbohydrate binding. {ECO:0000269|PubMed:11085997,
CC       ECO:0000269|PubMed:18824549, ECO:0000269|PubMed:19342690,
CC       ECO:0000269|PubMed:19435888}.
CC   -!- CATALYTIC ACTIVITY: Random hydrolysis of N-acetyl-beta-D-
CC       glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.
CC       {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   -!- SUBCELLULAR LOCATION: Isoform 1: Secreted. Note=Secretion depends
CC       on 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
CC       at lower levels in lung. {ECO:0000269|PubMed:11085997,
CC       ECO:0000269|PubMed:15192232}.
CC   -!- INDUCTION: Up-regulated in lung epithelial cells from asthma
CC       patients. {ECO:0000269|PubMed:15192232}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC       class II subfamily. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 chitin-binding type-2 domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00144}.
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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; CAH70803.1; -; Genomic_DNA.
DR   EMBL; AL356387; CAH70803.1; JOINED; Genomic_DNA.
DR   EMBL; AL356387; CAI19265.1; -; Genomic_DNA.
DR   EMBL; AL513202; CAI19265.1; JOINED; 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_006710577.1. [Q9BZP6-3]
DR   UniGene; Hs.128814; -.
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   ProteinModelPortal; Q9BZP6; -.
DR   SMR; Q9BZP6; 21-397.
DR   BindingDB; Q9BZP6; -.
DR   ChEMBL; CHEMBL1293197; -.
DR   CAZy; CBM14; Carbohydrate-Binding Module Family 14.
DR   CAZy; GH18; Glycoside Hydrolase Family 18.
DR   PhosphoSite; Q9BZP6; -.
DR   DMDM; 37999771; -.
DR   MaxQB; Q9BZP6; -.
DR   PaxDb; Q9BZP6; -.
DR   PRIDE; Q9BZP6; -.
DR   Ensembl; ENST00000343320; ENSP00000341828; ENSG00000134216. [Q9BZP6-1]
DR   Ensembl; ENST00000353665; ENSP00000338970; ENSG00000134216. [Q9BZP6-3]
DR   Ensembl; ENST00000369740; ENSP00000358755; ENSG00000134216. [Q9BZP6-1]
DR   Ensembl; ENST00000430615; ENSP00000391132; ENSG00000134216. [Q9BZP6-2]
DR   Ensembl; ENST00000451398; ENSP00000390476; ENSG00000134216. [Q9BZP6-3]
DR   Ensembl; ENST00000483391; ENSP00000436946; ENSG00000134216. [Q9BZP6-3]
DR   GeneID; 27159; -.
DR   KEGG; hsa:27159; -.
DR   UCSC; uc001eaq.4; human. [Q9BZP6-1]
DR   CTD; 27159; -.
DR   GeneCards; GC01P111833; -.
DR   HGNC; HGNC:17432; CHIA.
DR   HPA; HPA059193; -.
DR   MIM; 606080; gene.
DR   neXtProt; NX_Q9BZP6; -.
DR   PharmGKB; PA142672117; -.
DR   eggNOG; COG3325; -.
DR   HOVERGEN; HBG011684; -.
DR   InParanoid; Q9BZP6; -.
DR   KO; K01183; -.
DR   OMA; RNAFWHC; -.
DR   PhylomeDB; Q9BZP6; -.
DR   TreeFam; TF315610; -.
DR   BRENDA; 3.2.1.14; 2681.
DR   EvolutionaryTrace; Q9BZP6; -.
DR   GenomeRNAi; 27159; -.
DR   NextBio; 49937; -.
DR   PRO; PR:Q9BZP6; -.
DR   ArrayExpress; Q9BZP6; -.
DR   Bgee; Q9BZP6; -.
DR   Genevestigator; Q9BZP6; -.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR   GO; GO:0030246; F:carbohydrate binding; NAS:UniProtKB.
DR   GO; GO:0008061; F:chitin binding; TAS:UniProtKB.
DR   GO; GO:0004568; F:chitinase activity; IDA:UniProtKB.
DR   GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
DR   GO; GO:0003796; F:lysozyme activity; NAS:UniProtKB.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0006037; P:cell wall chitin metabolic process; TAS:UniProtKB.
DR   GO; GO:0006032; P:chitin catabolic process; IDA:UniProtKB.
DR   GO; GO:0006030; P:chitin metabolic process; NAS:UniProtKB.
DR   GO; GO:0007586; P:digestion; NAS:UniProtKB.
DR   GO; GO:0006955; P:immune response; NAS:UniProtKB.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0090197; P:positive regulation of chemokine secretion; IDA:UniProtKB.
DR   GO; GO:0002532; P:production of molecular mediator involved in inflammatory response; IDA:UniProtKB.
DR   GO; GO:0001101; P:response to acid; TAS:UniProtKB.
DR   GO; GO:0009620; P:response to fungus; TAS:UniProtKB.
DR   Gene3D; 2.170.140.10; -; 1.
DR   Gene3D; 3.10.50.10; -; 1.
DR   Gene3D; 3.20.20.80; -; 2.
DR   InterPro; IPR002557; Chitin-bd_dom.
DR   InterPro; IPR011583; Chitinase_II.
DR   InterPro; IPR029070; Chitinase_insertion.
DR   InterPro; IPR001223; Glyco_hydro18cat.
DR   InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR   InterPro; IPR013781; Glyco_hydro_catalytic_dom.
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; 2.
DR   SUPFAM; SSF54556; SSF54556; 1.
DR   SUPFAM; SSF57625; SSF57625; 1.
DR   PROSITE; PS50940; CHIT_BIND_II; 1.
DR   PROSITE; PS01095; CHITINASE_18; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Apoptosis;
KW   Carbohydrate metabolism; Chitin degradation; Chitin-binding;
KW   Complete proteome; Cytoplasm; Disulfide bond; Glycosidase; Hydrolase;
KW   Immunity; Inflammatory response; Polymorphism;
KW   Polysaccharide degradation; Reference proteome; Secreted; Signal.
FT   SIGNAL        1     21       {ECO:0000250}.
FT   CHAIN        22    476       Acidic mammalian chitinase.
FT                                /FTId=PRO_0000011944.
FT   DOMAIN      427    476       Chitin-binding type-2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00144}.
FT   REGION       70     71       Chitooligosaccharide binding.
FT                                {ECO:0000305}.
FT   REGION       97    100       Chitooligosaccharide binding.
FT                                {ECO:0000305}.
FT   REGION      210    213       Chitooligosaccharide binding.
FT                                {ECO:0000305}.
FT   COMPBIAS    415    420       Poly-Ser.
FT   ACT_SITE    140    140       Proton donor. {ECO:0000305}.
FT   BINDING     141    141       Chitooligosaccharide. {ECO:0000250}.
FT   BINDING     360    360       Chitooligosaccharide. {ECO:0000250}.
FT   DISULFID     26     51       {ECO:0000255|PROSITE-ProRule:PRU00144,
FT                                ECO:0000269|PubMed:19241384}.
FT   DISULFID     49    394       {ECO:0000255|PROSITE-ProRule:PRU00144,
FT                                ECO:0000269|PubMed:19241384}.
FT   DISULFID    307    372       {ECO:0000255|PROSITE-ProRule:PRU00144,
FT                                ECO:0000269|PubMed:19241384}.
FT   VAR_SEQ       1    161       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:10548734,
FT                                ECO:0000303|Ref.3}.
FT                                /FTId=VSP_008634.
FT   VAR_SEQ       1    108       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:10548734,
FT                                ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|Ref.3}.
FT                                /FTId=VSP_008635.
FT   VARIANT      45     45       N -> D (increased chitinase activity;
FT                                when associated with N-47 and M-61;
FT                                dbSNP:rs41282492).
FT                                {ECO:0000269|PubMed:19435888}.
FT                                /FTId=VAR_063030.
FT   VARIANT      47     47       D -> N (increased chitinase activity;
FT                                when associated with N-47 and M-61;
FT                                dbSNP:rs41282494).
FT                                {ECO:0000269|PubMed:19435888}.
FT                                /FTId=VAR_063031.
FT   VARIANT      61     61       R -> M (increased chitinase activity;
FT                                when associated with N-47 and M-61;
FT                                dbSNP:rs41282496).
FT                                {ECO:0000269|PubMed:19435888}.
FT                                /FTId=VAR_063032.
FT   VARIANT     102    102       G -> R (in dbSNP:rs3818822).
FT                                {ECO:0000269|PubMed:19435888}.
FT                                /FTId=VAR_049192.
FT   VARIANT     125    125       K -> R (in dbSNP:rs61756687).
FT                                {ECO:0000269|PubMed:19435888}.
FT                                /FTId=VAR_063033.
FT   VARIANT     324    324       V -> G (in dbSNP:rs2256721).
FT                                /FTId=VAR_033730.
FT   VARIANT     339    339       I -> V (in dbSNP:rs2275253).
FT                                {ECO:0000269|PubMed:10548734,
FT                                ECO:0000269|PubMed:19435888}.
FT                                /FTId=VAR_049193.
FT   VARIANT     354    354       F -> S (in dbSNP:rs2275254).
FT                                {ECO:0000269|PubMed:19435888}.
FT                                /FTId=VAR_049194.
FT   VARIANT     377    377       F -> L (in dbSNP:rs36011905).
FT                                /FTId=VAR_049195.
FT   VARIANT     432    432       V -> G (in dbSNP:rs2256721).
FT                                {ECO:0000269|PubMed:10548734,
FT                                ECO:0000269|PubMed:19435888}.
FT                                /FTId=VAR_049196.
FT   MUTAGEN     138    138       D->A: Loss of chitinase activity. No
FT                                effect on protection against apoptosis or
FT                                on AKT1 activation.
FT                                {ECO:0000269|PubMed:19342690}.
FT   CONFLICT    203    203       Y -> C (in Ref. 3; AAX81431).
FT                                {ECO:0000305}.
FT   STRAND       23     29
FT   HELIX        32     34
FT   HELIX        37     39
FT   HELIX        43     45
FT   TURN         48     50
FT   STRAND       52     62
FT   STRAND       65     67
FT   HELIX        73     82
FT   HELIX        83     85
FT   STRAND       91     97
FT   HELIX        99    101
FT   HELIX       104    110
FT   HELIX       113    130
FT   STRAND      133    138
FT   HELIX       151    173
FT   STRAND      179    184
FT   HELIX       188    194
FT   HELIX       197    203
FT   STRAND      205    209
FT   HELIX       217    219
FT   HELIX       236    240
FT   HELIX       243    252
FT   HELIX       257    259
FT   STRAND      260    275
FT   STRAND      284    288
FT   TURN        293    295
FT   STRAND      300    302
FT   HELIX       303    311
FT   STRAND      315    319
FT   TURN        320    323
FT   STRAND      324    329
FT   STRAND      332    335
FT   HELIX       339    351
FT   STRAND      355    360
FT   HELIX       362    364
FT   STRAND      367    369
FT   TURN        370    372
FT   HELIX       378    386
FT   HELIX       392    394
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
//
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