Reviewed, UniProtKB/Swiss-Prot Q9D7Q1 (CHIT1_MOUSE)

Names and origin

Protein names

Recommended name:
    Chitotriosidase-1
    EC=3.2.1.14
Alternative name(s):
    Chitinase-1

Gene names

Name:

Chit1

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	464 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Degrades chitin and chitotriose. 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 process	Carbohydrate metabolism Chitin degradation Polysaccharide degradation
Cellular component	Lysosome Secreted
Coding sequence diversity	Alternative splicing
Domain	Signal
Ligand	Chitin-binding
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond
Gene Ontology (GO)
Biological process	chitin catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell lysosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	cation binding Inferred from electronic annotation. Source: InterPro chitin binding Inferred from electronic annotation. Source: UniProtKB-KW chitinase activity Inferred from electronic annotation. Source: EC
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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 21	21	By similarity
	Chain	22 – 464	443	Chitotriosidase-1		PRO_0000011942
Regions
	Domain	415 – 464	50	Chitin-binding type-2
Sites
	Active site	140	1	Proton donor By similarity
Amino acid modifications
	Disulfide bond	26 ↔ 51		By similarity
	Disulfide bond	307 ↔ 368		By similarity
	Disulfide bond	448 ↔ 461		By similarity
Natural variations
	Alternative sequence	343 – 396	54	AYLKQ…SPEQI → KLMGSTPTLETSPLTTTVEE GGCSSRAVLQAWCLEPLANV VPGAKFLEPHPTPV in isoform 2.		VSP_020143
	Alternative sequence	397 – 464	68	Missing in isoform 2.		VSP_020144
Experimental info
	Mutagenesis	136	1	D → N: Loss of activity; when associated with Q-140. Ref.1
	Mutagenesis	140	1	E → Q: Loss of activity; when associated with N-136. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified September 5, 2006. Version 2. Checksum: 6276B6A414B4E96A	FASTA	464	51,112
	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
	Isoform 2. Checksum: 32BB674B61AF7123	FASTA	396	43,413
	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 KAKLMGSTPT LETSPLTTTV 370 380 390 EEGGCSSRAV LQAWCLEPLA NVVPGAKFLE PHPTPV

References

	« Hide 'large scale' referencesShow '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: 16005164] [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: 15923370] [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. , 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: 16141072] [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.
IPI	IPI00110612. IPI00623675.
RefSeq	NP_082255.1.
UniGene	Mm.328268
3D structure databases
SMR	Q9D7Q1. Positions 22-383, 415-464.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9D7Q1.
Protein family/group databases
CAZy	CBM14. Carbohydrate-Binding Module Family 14. GH18. Glycoside Hydrolase Family 18.
Proteomic databases
PRIDE	Q9D7Q1.
Genome annotation databases
Ensembl	ENSMUST00000086475; ENSMUSP00000083666; ENSMUSG00000026450; Mus musculus. [Genome view] ENSMUST00000112256; ENSMUSP00000107875; ENSMUSG00000026450; Mus musculus. [Genome view] ENSMUST00000112259; ENSMUSP00000107878; ENSMUSG00000026450; Mus musculus. [Genome view]
GeneID	71884.
KEGG	mmu:71884.
UCSC	uc007crf.1. mouse.
Organism-specific databases
CTD	71884.
MGI	MGI:1919134. Chit1.
Phylogenomic databases
eggNOG	maNOG04956.
HOGENOM	HBG443716.
HOVERGEN	Q9D7Q1.
InParanoid	Q9D7Q1.
OMA	FHAMAKN.
OrthoDB	EOG90CM35.
PhylomeDB	Q9D7Q1.
Enzyme and pathway databases
BRENDA	3.2.1.14. 244.
Gene expression databases
ArrayExpress	Q9D7Q1.
Bgee	Q9D7Q1.
CleanEx	MM_CHIT1.
Genevestigator	Q9D7Q1.
GermOnline	ENSMUSG00000026450. Mus musculus.
Family and domain databases
InterPro	IPR002557. Chitin-bd_peritrophin-A. IPR011583. Chitinase_II. IPR001223. Glyco_hydro18cat. IPR001579. Glyco_hydro_18_chit_AS. IPR017853. Glyco_hydro_catalytic_core. IPR013781. Glyco_hydro_sg_catalytic. [Graphical view]
Gene3D	G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
Pfam	PF01607. CBM_14. 1 hit. PF00704. Glyco_hydro_18. 1 hit. [Graphical view]
SMART	SM00494. ChtBD2. 1 hit. SM00636. Glyco_18. 1 hit. [Graphical view]
PROSITE	PS50940. CHIT_BIND_II. 1 hit. PS01095. CHITINASE_18. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	334840.
SOURCE	Search...

Entry information

Entry name

CHIT1_MOUSE

Accession

Primary (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:	January 19, 2010
This is version 78 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)