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Q9BZP6 (CHIA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acidic mammalian chitinase

Short name=AMCase
EC=3.2.1.14
Alternative name(s):
Lung-specific protein TSA1902
Gene names
Name:CHIA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length476 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Degrades chitin and chitotriose. May participate in the defense against nematodes, fungi and other pathogens. Plays a role in T-helper cell type 2 (Th2) immune response. Contributes to the response to IL-13 and inflammation in response to IL-13. Stimulates chemokine production by pulmonary epithelial cells. Protects lung epithelial cells against apoptosis and promotes phosphorylation of AKT1. Its function in the inflammatory response and in protecting cells against apoptosis is inhibited by allosamidin, suggesting that the function of this protein depends on carbohydrate binding. Ref.2 Ref.7 Ref.8 Ref.10

Catalytic activity

Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins. Ref.7 Ref.9 Ref.10

Subunit structure

Interacts with EGFR. Ref.7

Subcellular location

Isoform 1: Secreted. Note: Secretion depends on EGFR activity. Ref.7

Isoform 2: Cytoplasm Ref.7.

Isoform 3: Cytoplasm Ref.7.

Tissue specificity

Detected in lung epithelial cells from asthma patients (at protein level). Highly expressed in stomach. Detected at lower levels in lung. Ref.2 Ref.6

Induction

Up-regulated in lung epithelial cells from asthma patients. Ref.6

Sequence similarities

Belongs to the glycosyl hydrolase 18 family. Chitinase class II subfamily.

Contains 1 chitin-binding type-2 domain.

Ontologies

Keywords
   Biological processApoptosis
Carbohydrate metabolism
Chitin degradation
Immunity
Inflammatory response
Polysaccharide degradation
   Cellular componentCytoplasm
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainSignal
   LigandChitin-binding
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

cell wall chitin metabolic process

Traceable author statement Ref.2. Source: UniProtKB

chitin catabolic process

Inferred from direct assay Ref.10. Source: UniProtKB

chitin metabolic process

Non-traceable author statement Ref.1. Source: UniProtKB

digestion

Non-traceable author statement Ref.2. Source: UniProtKB

immune response

Non-traceable author statement Ref.2. Source: UniProtKB

polysaccharide catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

positive regulation of chemokine secretion

Inferred from direct assay Ref.7. Source: UniProtKB

production of molecular mediator involved in inflammatory response

Inferred from direct assay Ref.7. Source: UniProtKB

response to acid

Traceable author statement Ref.2. Source: UniProtKB

response to fungus

Traceable author statement Ref.2. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular space

Inferred from direct assay Ref.7. Source: UniProtKB

   Molecular_functioncarbohydrate binding

Non-traceable author statement Ref.2. Source: UniProtKB

chitin binding

Traceable author statement Ref.2. Source: UniProtKB

chitinase activity

Inferred from direct assay Ref.2Ref.10. Source: UniProtKB

kinase binding

Inferred from physical interaction Ref.7. Source: UniProtKB

lysozyme activity

Non-traceable author statement Ref.2. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9BZP6-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9BZP6-2)

Also known as: TSA1902-L;

The sequence of this isoform differs from the canonical sequence as follows:
     1-108: Missing.
Isoform 3 (identifier: Q9BZP6-3)

Also known as: TSA1902-S;

The sequence of this isoform differs from the canonical sequence as follows:
     1-161: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 By similarity
Chain22 – 476455Acidic mammalian chitinase
PRO_0000011944

Regions

Domain427 – 47650Chitin-binding type-2
Region70 – 712Chitooligosaccharide binding Probable
Region97 – 1004Chitooligosaccharide binding Probable
Region210 – 2134Chitooligosaccharide binding Probable
Compositional bias415 – 4206Poly-Ser

Sites

Active site1401Proton donor Probable
Binding site1411Chitooligosaccharide By similarity
Binding site3601Chitooligosaccharide By similarity

Amino acid modifications

Disulfide bond26 ↔ 51 Ref.9
Disulfide bond49 ↔ 394 Ref.9
Disulfide bond307 ↔ 372 Ref.9

Natural variations

Alternative sequence1 – 161161Missing in isoform 3.
VSP_008634
Alternative sequence1 – 108108Missing in isoform 2.
VSP_008635
Natural variant451N → D Increased chitinase activity; when associated with N-47 and M-61. Ref.10
Corresponds to variant rs41282492 [ dbSNP | Ensembl ].
VAR_063030
Natural variant471D → N Increased chitinase activity; when associated with N-47 and M-61. Ref.10
Corresponds to variant rs41282494 [ dbSNP | Ensembl ].
VAR_063031
Natural variant611R → M Increased chitinase activity; when associated with N-47 and M-61. Ref.10
Corresponds to variant rs41282496 [ dbSNP | Ensembl ].
VAR_063032
Natural variant1021G → R. Ref.10
Corresponds to variant rs3818822 [ dbSNP | Ensembl ].
VAR_049192
Natural variant1251K → R. Ref.10
Corresponds to variant rs61756687 [ dbSNP | Ensembl ].
VAR_063033
Natural variant3241V → G.
Corresponds to variant rs2256721 [ dbSNP | Ensembl ].
VAR_033730
Natural variant3391I → V. Ref.1 Ref.10
Corresponds to variant rs2275253 [ dbSNP | Ensembl ].
VAR_049193
Natural variant3541F → S. Ref.10
Corresponds to variant rs2275254 [ dbSNP | Ensembl ].
VAR_049194
Natural variant3771F → L.
Corresponds to variant rs36011905 [ dbSNP | Ensembl ].
VAR_049195
Natural variant4321V → G. Ref.1 Ref.10
Corresponds to variant rs2256721 [ dbSNP | Ensembl ].
VAR_049196

Experimental info

Mutagenesis1381D → A: Loss of chitinase activity. No effect on protection against apoptosis or on AKT1 activation. Ref.8
Sequence conflict2031Y → C in AAX81431. Ref.3

Secondary structure

......................................................................... 476
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 92B27BAD2F7EB4CC

FASTA47652,271
        10         20         30         40         50         60 
MTKLILLTGL VLILNLQLGS AYQLTCYFTN WAQYRPGLGR FMPDNIDPCL CTHLIYAFAG 

        70         80         90        100        110        120 
RQNNEITTIE WNDVTLYQAF NGLKNKNSQL KTLLAIGGWN FGTAPFTAMV STPENRQTFI 

       130        140        150        160        170        180 
TSVIKFLRQY EFDGLDFDWE YPGSRGSPPQ DKHLFTVLVQ EMREAFEQEA KQINKPRLMV 

       190        200        210        220        230        240 
TAAVAAGISN IQSGYEIPQL SQYLDYIHVM TYDLHGSWEG YTGENSPLYK YPTDTGSNAY 

       250        260        270        280        290        300 
LNVDYVMNYW KDNGAPAEKL IVGFPTYGHN FILSNPSNTG IGAPTSGAGP AGPYAKESGI 

       310        320        330        340        350        360 
WAYYEICTFL KNGATQGWDA PQEVPYAYQG NVWVGYDNIK SFDIKAQWLK HNKFGGAMVW 

       370        380        390        400        410        420 
AIDLDDFTGT FCNQGKFPLI STLKKALGLQ SASCTAPAQP IEPITAAPSG SGNGSGSSSS 

       430        440        450        460        470 
GGSSGGSGFC AVRANGLYPV ANNRNAFWHC VNGVTYQQNC QAGLVFDTSC DCCNWA 

« Hide

Isoform 2 (TSA1902-L) [UniParc].

Checksum: FC2558C4CEA48609
Show »

FASTA36840,139
Isoform 3 (TSA1902-S) [UniParc].

Checksum: 61D614709B577CAD
Show »

FASTA31533,906

References

« Hide 'large scale' references
[1]"Isolation and mapping of a human lung-specific gene, TSA1902, encoding a novel chitinase family member."
Saito A., Ozaki K., Fujiwara T., Nakamura Y., Tanigami A.
Gene 239:325-331(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), VARIANTS VAL-339 AND GLY-432.
Tissue: Lung.
[2]"Identification of a novel acidic mammalian chitinase distinct from chitotriosidase."
Boot R.G., Blommaart E.F.C., Swart E., Ghauharali-van der Vlugt K., Bijl N., Moe C., Place A., Aerts J.M.F.G.
J. Biol. Chem. 276:6770-6778(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
[3]"A novel chitinase family member."
Chen X.H., Cai G.P.
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
Tissue: Kidney.
[4]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[6]"Acidic mammalian chitinase in asthmatic Th2 inflammation and IL-13 pathway activation."
Zhu Z., Zheng T., Homer R.J., Kim Y.K., Chen N.Y., Cohn L., Hamid Q., Elias J.A.
Science 304:1678-1682(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION, TISSUE SPECIFICITY.
[7]"Acidic mammalian chitinase is secreted via an ADAM17/epidermal growth factor receptor-dependent pathway and stimulates chemokine production by pulmonary epithelial cells."
Hartl D., He C.H., Koller B., Da Silva C.A., Homer R., Lee C.G., Elias J.A.
J. Biol. Chem. 283:33472-33482(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH EGFR, SUBCELLULAR LOCATION.
[8]"Acidic mammalian chitinase regulates epithelial cell apoptosis via a chitinolytic-independent mechanism."
Hartl D., He C.H., Koller B., Da Silva C.A., Kobayashi Y., Lee C.G., Flavell R.A., Elias J.A.
J. Immunol. 182:5098-5106(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF ASP-138.
[9]"Triad of polar residues implicated in pH specificity of acidic mammalian chitinase."
Olland A.M., Strand J., Presman E., Czerwinski R., Joseph-McCarthy D., Krykbaev R., Schlingmann G., Chopra R., Lin L., Fleming M., Kriz R., Stahl M., Somers W., Fitz L., Mosyak L.
Protein Sci. 18:569-578(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 22-408 IN COMPLEX WITH METHYLALLOSAMIDIN, CATALYTIC ACTIVITY, DISULFIDE BONDS.
[10]"Differential enzymatic activity of common haplotypic versions of the human acidic mammalian chitinase protein."
Seibold M.A., Reese T.A., Choudhry S., Salam M.T., Beckman K., Eng C., Atakilit A., Meade K., Lenoir M., Watson H.G., Thyne S., Kumar R., Weiss K.B., Grammer L.C., Avila P., Schleimer R.P., Fahy J.V., Rodriguez-Santana J. expand/collapse author list , Rodriguez-Cintron W., Boot R.G., Sheppard D., Gilliland F.D., Locksley R.M., Burchard E.G.
J. Biol. Chem. 284:19650-19658(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ASP-45; ASN-47; MET-61; ARG-102; ARG-125; VAL-339; SER-354 AND GLY-432, CATALYTIC ACTIVITY, FUNCTION, CHARACTERIZATION OF VARIANTS ASP-45; ASN-47 AND MET-61.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB025008 mRNA. Translation: BAA86980.1.
AB025009 mRNA. Translation: BAA86981.1.
AF290004 mRNA. Translation: AAG60019.1.
AY789444 mRNA. Translation: AAX81431.1.
AY789445 mRNA. Translation: AAX81432.1.
AL513202, AL356387 Genomic DNA. Translation: CAH70803.1.
AL356387, AL513202 Genomic DNA. Translation: CAI19265.1.
BC047336 mRNA. Translation: AAH47336.2.
BC036339 mRNA. Translation: AAH36339.2.
BC106910 mRNA. Translation: AAI06911.1.
RefSeqNP_001035713.1. NM_001040623.2.
NP_001244930.1. NM_001258001.1.
NP_001244931.1. NM_001258002.1.
NP_001244932.1. NM_001258003.1.
NP_001244933.1. NM_001258004.1.
NP_001244934.1. NM_001258005.1.
NP_068569.2. NM_021797.3.
NP_970615.2. NM_201653.3.
UniGeneHs.128814.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2YBTX-ray2.22A/B/C/D/E/F21-398[»]
2YBUX-ray2.25A/B/C/D/E/F21-398[»]
3FXYX-ray2.00A/B/C/D22-408[»]
3FY1X-ray1.70A/B22-408[»]
3RM4X-ray1.90A/B22-408[»]
3RM8X-ray1.80A/B22-408[»]
3RM9X-ray2.10A/B22-408[»]
3RMEX-ray1.80A/B22-408[»]
ProteinModelPortalQ9BZP6.
SMRQ9BZP6. Positions 21-397.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBQ9BZP6.
ChEMBLCHEMBL1293197.

Protein family/group databases

CAZyCBM14. Carbohydrate-Binding Module Family 14.
GH18. Glycoside Hydrolase Family 18.

PTM databases

PhosphoSiteQ9BZP6.

Polymorphism databases

DMDM37999771.

Proteomic databases

PaxDbQ9BZP6.
PRIDEQ9BZP6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000343320; ENSP00000341828; ENSG00000134216. [Q9BZP6-1]
ENST00000353665; ENSP00000338970; ENSG00000134216. [Q9BZP6-3]
ENST00000369740; ENSP00000358755; ENSG00000134216. [Q9BZP6-1]
ENST00000430615; ENSP00000391132; ENSG00000134216. [Q9BZP6-2]
ENST00000451398; ENSP00000390476; ENSG00000134216. [Q9BZP6-3]
ENST00000483391; ENSP00000436946; ENSG00000134216. [Q9BZP6-3]
GeneID27159.
KEGGhsa:27159.
UCSCuc001eaq.4. human. [Q9BZP6-1]

Organism-specific databases

CTD27159.
GeneCardsGC01P111833.
HGNCHGNC:17432. CHIA.
HPAHPA059193.
MIM606080. gene.
neXtProtNX_Q9BZP6.
PharmGKBPA142672117.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG3325.
HOVERGENHBG011684.
InParanoidQ9BZP6.
KOK01183.
OMAFDIKAQW.
PhylomeDBQ9BZP6.
TreeFamTF315610.

Enzyme and pathway databases

BRENDA3.2.1.14. 2681.

Gene expression databases

ArrayExpressQ9BZP6.
BgeeQ9BZP6.
GenevestigatorQ9BZP6.

Family and domain databases

Gene3D2.170.140.10. 1 hit.
3.20.20.80. 2 hits.
InterProIPR002557. Chitin-bd_dom.
IPR011583. Chitinase_II.
IPR001223. Glyco_hydro18cat.
IPR001579. Glyco_hydro_18_chit_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF01607. CBM_14. 1 hit.
PF00704. Glyco_hydro_18. 1 hit.
[Graphical view]
SMARTSM00494. ChtBD2. 1 hit.
SM00636. Glyco_18. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 2 hits.
SSF57625. SSF57625. 1 hit.
PROSITEPS50940. CHIT_BIND_II. 1 hit.
PS01095. CHITINASE_18. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9BZP6.
GenomeRNAi27159.
NextBio49937.
PROQ9BZP6.
SOURCESearch...

Entry information

Entry nameCHIA_HUMAN
AccessionPrimary (citable) accession number: Q9BZP6
Secondary accession number(s): Q32W79 expand/collapse secondary AC list , Q32W80, Q3B866, Q5U5Z5, Q5VUV4, Q86UD8, Q9ULY3, Q9ULY4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 24, 2003
Last sequence update: June 1, 2001
Last modified: April 16, 2014
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries