Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9D7Q1 (CHIT1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Chitotriosidase-1

EC=3.2.1.14
Alternative name(s):
Chitinase-1
Gene names
Name:Chit1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length464 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, chitotriose and chitobiose. May participate in the defense against nematodes and other pathogens By similarity. Ref.1

Catalytic activity

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

Subunit structure

Monomer By similarity.

Subcellular location

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

Tissue specificity

Highly expressed in tongue, stomach, kidney, brain, skin, testis, and bone marrow. Low level of expression was found in lung, heart, spleen, small intestine, and liver. Not detectable in pancreas, salivary gland, large intestine, uterus, or peripheral blood mononuclear cells (PBMC). Ref.1 Ref.2

Sequence similarities

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

Contains 1 chitin-binding type-2 domain.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Chitin degradation
Polysaccharide degradation
   Cellular componentLysosome
Secreted
   Coding sequence diversityAlternative splicing
   DomainSignal
   LigandChitin-binding
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processchitin catabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

polysaccharide catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular space

Inferred from electronic annotation. Source: Ensembl

lysosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionchitin binding

Inferred from electronic annotation. Source: UniProtKB-KW

endochitinase activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9D7Q1-1)

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: Q9D7Q1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     343-396: AYLKQKGLGG...SETPRSPEQI → KLMGSTPTLE...KFLEPHPTPV
     397-464: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 By similarity
Chain22 – 464443Chitotriosidase-1
PRO_0000011942

Regions

Domain415 – 46450Chitin-binding type-2
Region70 – 712Chitooligosaccharide binding By similarity
Region97 – 1004Chitooligosaccharide binding By similarity
Region210 – 2134Chitooligosaccharide binding By similarity

Sites

Active site1401Proton donor By similarity
Binding site2691Chitooligosaccharide By similarity
Binding site3561Chitooligosaccharide By similarity

Amino acid modifications

Disulfide bond26 ↔ 51 By similarity
Disulfide bond307 ↔ 368 By similarity
Disulfide bond448 ↔ 461 By similarity

Natural variations

Alternative sequence343 – 39654AYLKQ…SPEQI → KLMGSTPTLETSPLTTTVEE GGCSSRAVLQAWCLEPLANV VPGAKFLEPHPTPV in isoform 2.
VSP_020143
Alternative sequence397 – 46468Missing in isoform 2.
VSP_020144

Experimental info

Mutagenesis1361D → N: Loss of activity; when associated with Q-140. Ref.1
Mutagenesis1401E → Q: Loss of activity; when associated with N-136. Ref.1

Sequences

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

Last modified September 5, 2006. Version 2.
Checksum: 6276B6A414B4E96A

FASTA46451,112
        10         20         30         40         50         60 
MVQSLAWAGV MTLLMVQWGS AAKLVCYLTN WSQYRTEAVR FFPRDVDPNL CTHVIFAFAG 

        70         80         90        100        110        120 
MDNHQLSTVE HNDELLYQEL NSLKTKNPKL KTLLAVGGWT FGTQKFTDMV ATASNRQTFV 

       130        140        150        160        170        180 
KSALSFLRTQ GFDGLDLDWE FPGGRGSPTV DKERFTALIQ DLAKAFQEEA QSSGKERLLL 

       190        200        210        220        230        240 
TAAVPSDRGL VDAGYEVDKI AQSLDFINLM AYDFHSSLEK TTGHNSPLYK RQGESGAAAE 

       250        260        270        280        290        300 
QNVDAAVTLW LQKGTPASKL ILGMPTYGRS FTLASSSDNG VGAPATGPGA PGPYTKDKGV 

       310        320        330        340        350        360 
LAYYEACSWK ERHRIEDQKV PYAFQDNQWV SFDDVESFKA KAAYLKQKGL GGAMVWVLDL 

       370        380        390        400        410        420 
DDFKGSFCNQ GPYPLIRTLR QELNLPSETP RSPEQIIPEP RPSSMPEQGP SPGLDNFCQG 

       430        440        450        460 
KADGVYPNPG DESTYYNCGG GRLFQQSCPP GLVFRASCKC CTWS 

« Hide

Isoform 2 [UniParc].

Checksum: 32BB674B61AF7123
Show »

FASTA39643,413

References

« Hide 'large scale' references
[1]"Molecular cloning and functional characterization of mouse chitotriosidase."
Zheng T., Rabach M., Chen N.Y., Rabach L., Hu X., Elias J.A., Zhu Z.
Gene 357:37-46(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF ASP-136 AND GLU-140.
Strain: C57BL/6.
Tissue: Tongue.
[2]"Marked differences in tissue-specific expression of chitinases in mouse and man."
Boot R.G., Bussink A.P., Verhoek M., de Boer P.A.J., Moorman A.F., Aerts J.M.F.G.
J. Histochem. Cytochem. 53:1283-1292(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
Strain: C57BL/6.
Tissue: Tongue.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Strain: C57BL/6J.
Tissue: Tongue.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY458654 mRNA. Translation: AAR14312.1.
AY536287 mRNA. Translation: AAS47832.1.
AK009012 mRNA. Translation: BAB26025.1.
CCDSCCDS15304.1. [Q9D7Q1-1]
CCDS69943.1. [Q9D7Q1-2]
RefSeqNP_001271453.1. NM_001284524.1. [Q9D7Q1-2]
NP_001271454.1. NM_001284525.1. [Q9D7Q1-1]
NP_082255.1. NM_027979.2. [Q9D7Q1-1]
XP_006529942.1. XM_006529879.1. [Q9D7Q1-1]
XP_006529943.1. XM_006529880.1. [Q9D7Q1-1]
XP_006529944.1. XM_006529881.1. [Q9D7Q1-2]
UniGeneMm.328268.

3D structure databases

ProteinModelPortalQ9D7Q1.
SMRQ9D7Q1. Positions 22-383.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000083666.

Protein family/group databases

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

Proteomic databases

MaxQBQ9D7Q1.
PaxDbQ9D7Q1.
PRIDEQ9D7Q1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000086475; ENSMUSP00000083666; ENSMUSG00000026450. [Q9D7Q1-1]
ENSMUST00000159963; ENSMUSP00000123979; ENSMUSG00000026450. [Q9D7Q1-1]
ENSMUST00000160060; ENSMUSP00000124331; ENSMUSG00000026450. [Q9D7Q1-2]
GeneID71884.
KEGGmmu:71884.
UCSCuc007crf.1. mouse. [Q9D7Q1-1]

Organism-specific databases

CTD1118.
MGIMGI:1919134. Chit1.

Phylogenomic databases

eggNOGCOG3325.
GeneTreeENSGT00550000074323.
HOGENOMHOG000111109.
HOVERGENHBG011684.
InParanoidQ9D7Q1.
KOK01183.
OMAHRIKDQK.
OrthoDBEOG7ZGX3G.
PhylomeDBQ9D7Q1.
TreeFamTF315610.

Gene expression databases

BgeeQ9D7Q1.
CleanExMM_CHIT1.
GenevestigatorQ9D7Q1.

Family and domain databases

Gene3D2.170.140.10. 1 hit.
3.10.50.10. 1 hit.
3.20.20.80. 2 hits.
InterProIPR002557. Chitin-bd_dom.
IPR011583. Chitinase_II.
IPR029070. Chitinase_insertion.
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.
SSF54556. SSF54556. 1 hit.
SSF57625. SSF57625. 1 hit.
PROSITEPS50940. CHIT_BIND_II. 1 hit.
PS01095. CHITINASE_18. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio334840.
PROQ9D7Q1.
SOURCESearch...

Entry information

Entry nameCHIT1_MOUSE
AccessionPrimary (citable) accession number: Q9D7Q1
Secondary accession number(s): Q6QJD2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 24, 2003
Last sequence update: September 5, 2006
Last modified: July 9, 2014
This is version 121 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries