Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q13231 (CHIT1_HUMAN)

Last modified November 3, 2009. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Chitotriosidase-1
    EC=3.2.1.14
Alternative name(s):
    Chitinase-1
Gene names
Name: CHIT1
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length466 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 and other pathogens. Isoform 3 has no enzymatic activity. Ref.1 Ref.3 Ref.4

Catalytic activity

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

Subunit structure

Monomer.

Subcellular location

Secreted. Lysosome. Note: A small proportion is lysosomal. Ref.1

Tissue specificity

Detected in spleen. Secreted by cultured macrophages. Ref.3

Polymorphism

A 24 bp duplication in exon 10 leads to the activation of an alternative splice site and the production of an inactive protein. About 6% of the population are deficient for CHIT1 activity, while 35% are carriers and show reduced enzyme levels. People with CHIT1 deficiency appear perfectly healthy.

Involvement in disease

Very high plasma levels of CHIT1 are found in patients with Gaucher disease type 1 (GD I). This can be used as diagnostic aid and to evaluate the success of treatment. Successful therapy brings the CHIT1 activity levels back to normal.

Sequence similarities

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

Contains 1 chitin-binding type-2 domain.

Ontologies

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q13231-1)

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: Q13231-2)

The sequence of this isoform differs from the canonical sequence as follows:
     386-387: SL → NG
     388-466: Missing.
Isoform 3 (identifier: Q13231-3)

The sequence of this isoform differs from the canonical sequence as follows:
     344-372: Missing.
Note: Duplication of 24 bp in exon 10 leads to the use of a cryptic splice site. The normal splice site is still present but not used.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Ref.3
Chain22 – 466445Chitotriosidase-1
PRO_0000011941

Regions

Domain417 – 46650Chitin-binding type-2

Sites

Active site1401Proton donor By similarity

Amino acid modifications

Disulfide bond26 ↔ 51
Disulfide bond307 ↔ 370
Disulfide bond450 ↔ 463 By similarity

Natural variations

Alternative sequence344 – 37229Missing in isoform 3.
VSP_008633
Alternative sequence386 – 3872SL → NG in isoform 2.
VSP_008631
Alternative sequence388 – 46679Missing in isoform 2.
VSP_008632
Natural variant401R → H: dbSNP rs35920428.
VAR_049190
Natural variant1021G → S: dbSNP rs2297950. Ref.2
VAR_022138
Natural variant1711Q → H: dbSNP rs12562058.
VAR_049191
Natural variant4421A → G: dbSNP rs1065761. Ref.2
VAR_024458

Secondary structure

........................................................................ 466
Helix Strand Turn

Details...

Sequences

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

Last modified November 1, 1996. Version 1.
Checksum: B4312D1E885E386D

FASTA46651,681
        10         20         30         40         50         60 
MVRSVAWAGF MVLLMIPWGS AAKLVCYFTN WAQYRQGEAR FLPKDLDPSL CTHLIYAFAG 

        70         80         90        100        110        120 
MTNHQLSTTE WNDETLYQEF NGLKKMNPKL KTLLAIGGWN FGTQKFTDMV ATANNRQTFV 

       130        140        150        160        170        180 
NSAIRFLRKY SFDGLDLDWE YPGSQGSPAV DKERFTTLVQ DLANAFQQEA QTSGKERLLL 

       190        200        210        220        230        240 
SAAVPAGQTY VDAGYEVDKI AQNLDFVNLM AYDFHGSWEK VTGHNSPLYK RQEESGAAAS 

       250        260        270        280        290        300 
LNVDAAVQQW LQKGTPASKL ILGMPTYGRS FTLASSSDTR VGAPATGSGT PGPFTKEGGM 

       310        320        330        340        350        360 
LAYYEVCSWK GATKQRIQDQ KVPYIFRDNQ WVGFDDVESF KTKVSYLKQK GLGGAMVWAL 

       370        380        390        400        410        420 
DLDDFAGFSC NQGRYPLIQT LRQELSLPYL PSGTPELEVP KPGQPSEPEH GPSPGQDTFC 

       430        440        450        460 
QGKADGLYPN PRERSSFYSC AAGRLFQQSC PTGLVFSNSC KCCTWN 

« Hide

Isoform 2.

Checksum: 03A272B8BC5E0D71
Show »

FASTA38743,133
Isoform 3.

Checksum: 1A073A5F90A43717
Show »

FASTA43748,565

References

« Hide 'large scale' references
[1]"Cloning of a cDNA encoding chitotriosidase, a human chitinase produced by macrophages."
Boot R.G., Renkema G.H., Strijland A., van Zonneveld A.J., Aerts J.M.F.G.
J. Biol. Chem. 270:26252-26256(1995) [PubMed: 7592832] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR LOCATION.
Tissue: Macrophage.
[2]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS SER-102 AND GLY-442.
[3]"Purification and characterization of human chitotriosidase, a novel member of the chitinase family of proteins."
Renkema G.H., Boot R.G., Muijsers A.O., Donker-Koopman W.E., Aerts J.M.F.G.
J. Biol. Chem. 270:2198-2202(1995) [PubMed: 7836450] [Abstract]
Cited for: PROTEIN SEQUENCE OF 22-42 AND 178-198, FUNCTION, TISSUE SPECIFICITY.
[4]"The human chitotriosidase gene. Nature of inherited enzyme deficiency."
Boot R.G., Renkema G.H., Verhoek M., Strijland A., Bliek J., de Meulemeester T.M.A.M.O., Mannens M.M.A.M., Aerts J.M.F.G.
J. Biol. Chem. 273:25680-25685(1998) [PubMed: 9748235] [Abstract]
Cited for: POLYMORPHISM, FUNCTION (ISOFORM 3).
[5]"Structure of human chitotriosidase. Implications for specific inhibitor design and function of mammalian chitinase-like lectins."
Fusetti F., von Moeller H., Houston D., Rozeboom H.J., Dijkstra B.W., Boot R.G., Aerts J.M.F.G., van Aalten D.M.F.
J. Biol. Chem. 277:25537-25544(2002) [PubMed: 11960986] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 22-386 IN COMPLEX WITH CHITOBIOSE AND ALLOSAMIDIN.
+Additional computationally mapped references.

Cross-references

Sequence databases

U29615 mRNA. Translation: AAC50246.1.
U62662 mRNA. Translation: AAG10644.1.
BC069614 mRNA. Translation: AAH69614.1.
BC103695 mRNA. Translation: AAI03696.1.
BC105680 mRNA. Translation: AAI05681.1.
BC105681 mRNA. Translation: AAI05682.1.
BC105682 mRNA. Translation: AAI05683.1.
IPIIPI00375364.
IPI00478217.
IPI00852865.
RefSeqNP_003456.1.
UniGeneHs.201688

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1GUVX-ray2.35A22-387[»]
1HKIX-ray2.55A22-386[»]
1HKJX-ray2.60A22-386[»]
1HKKX-ray1.85A22-385[»]
1HKMX-ray2.55A22-386[»]
1LG1X-ray2.78A22-386[»]
1LG2X-ray2.10A22-386[»]
1LQ0X-ray2.20A22-386[»]
1WAWX-ray1.75A22-466[»]
1WB0X-ray1.65A22-466[»]
ModBaseSearch...

Protein-protein interaction databases

STRINGQ13231.

Protein family/group databases

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

Proteomic databases

PRIDEQ13231.

Genome annotation databases

EnsemblENST00000255427; ENSP00000255427; ENSG00000133063; Homo sapiens. [Genome view]
ENST00000362046; ENSP00000355262; ENSG00000133063; Homo sapiens. [Genome view]
ENST00000367229; ENSP00000356198; ENSG00000133063; Homo sapiens. [Genome view]
GeneID1118.
KEGGhsa:1118.
UCSCuc001gzn.2. human.

Organism-specific databases

CTD1118.
GeneCardsGC01M201451.
H-InvDBHIX0001488.
HGNCHGNC:1936. CHIT1.
HPAHPA010575.
MIM600031. gene.
PharmGKBPA26467.
GenAtlasSearch...

Phylogenomic databases

HOGENOMQ13231.
HOVERGENQ13231.

Enzyme and pathway databases

BRENDA3.2.1.14. 247.

Gene expression databases

ArrayExpressQ13231.
BgeeQ13231.
CleanExHS_CHIT1.
GenevestigatorQ13231.
GermOnlineENSG00000133063. Homo sapiens.

Family and domain databases

InterProIPR002557. Chitin-bd_peritrophin-A.
IPR011583. Chitinase_II.
IPR001223. Glyco_hydro18cat.
IPR001579. Glyco_hydro_18_chit_AS.
IPR013781. Glyco_hydro_sg_catalytic.
[Graphical view]
Gene3DG3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
PfamPF01607. CBM_14. 1 hit.
PF00704. Glyco_hydro_18. 1 hit.
[Graphical view]
ProDomPD000471. Chitinase_II. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00494. ChtBD2. 1 hit.
SM00636. Glyco_18. 1 hit.
[Graphical view]
PROSITEPS50940. CHIT_BIND_II. 1 hit.
PS01095. CHITINASE_18. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio4638.
SOURCESearch...

Entry information

Entry nameCHIT1_HUMAN
AccessionPrimary (citable) accession number: Q13231
Secondary accession number(s): Q0VGG5 expand/collapse secondary AC list , Q0VGG6, Q3ZAR1, Q6ISC2, Q9H3V8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 24, 2003
Last sequence update: November 1, 1996
Last modified: November 3, 2009
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

Human chromosome 1

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents