Q91XA9 (CHIA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Acidic mammalian chitinase
Short name=AMCase
EC=3.2.1.14

Alternative name(s):
YNL

Gene names

Name:

Chia

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 › Mus

Protein attributes

Sequence length	473 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, 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. Its function in the inflammatory response is inhibited by allosamidin, suggesting that the function of this protein depends on carbohydrate binding. Ref.1 Ref.5 Ref.8
Catalytic activity	Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins. Ref.6
Subunit structure	Interacts with EGFR By similarity.
Subcellular location	Secreted. Cytoplasm Ref.7.
Tissue specificity	Detected in macrophages and lung epithelial cells. Protein levels are increased upon airway inflammation involving T helper cell type 2 (at protein level). Highly expressed in submaxillary gland, and stomach. Expressed at lower levels in lung. Ref.1 Ref.5 Ref.7
Induction	Up-regulated upon pulmonary inflammation elicited by sensitization and aerosol challenge with the aeroallergen ovalbumin. Up-regulated during T helper cell type 2 (Th2) inflammation. Induction is mediated by IL-13. Ref.5
Sequence similarities	Belongs to the glycosyl hydrolase 18 family. Chitinase class II subfamily. Contains 1 chitin-binding type-2 domain.
Biophysicochemical properties	pH dependence: Optimum pH is below 2.5. Ref.6
Sequence caution	The sequence AAH11134.1 differs from that shown. Reason: Erroneous initiation. The sequence AAH34548.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Apoptosis Carbohydrate metabolism Chitin degradation Immunity Inflammatory response Polysaccharide degradation
Cellular component	Cytoplasm Secreted
Domain	Signal
Ligand	Chitin-binding
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW chitin catabolic process Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of chemokine secretion Inferred from sequence or structural similarity. Source: UniProtKB production of molecular mediator involved in inflammatory response Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	cytoplasm Inferred from direct assay Ref.7. Source: UniProtKB extracellular space Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	cation binding Inferred from electronic annotation. Source: InterPro chitin binding Inferred from electronic annotation. Source: UniProtKB-KW chitinase activity Inferred from direct assay Ref.7. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 21	21	Ref.1
	Chain	22 – 473	452	Acidic mammalian chitinase		PRO_0000011945
Regions
	Domain	424 – 473	50	Chitin-binding type-2
	Region	70 – 71	2	Chitooligosaccharide binding By similarity
	Region	97 – 100	4	Chitooligosaccharide binding By similarity
	Region	210 – 213	4	Chitooligosaccharide binding By similarity
Sites
	Active site	140	1	Proton donor By similarity
	Binding site	141	1	Chitooligosaccharide By similarity
	Binding site	360	1	Chitooligosaccharide By similarity
Amino acid modifications
	Disulfide bond	26 ↔ 51		By similarity
	Disulfide bond	49 ↔ 394		By similarity
	Disulfide bond	307 ↔ 372		By similarity
	Disulfide bond	457 ↔ 470		By similarity
Experimental info
	Mutagenesis	208	1	H → N: Strongly reduced activity at low pH, with minor effect on activity at neutral pH. Ref.6
	Sequence conflict	293	1	P → A in AAG60018. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q91XA9 [UniParc]. Last modified October 24, 2003. Version 2. Checksum: 333C874477476695	FASTA	473	52,003
	10 20 30 40 50 60 MAKLLLVTGL ALLLNAQLGS AYNLICYFTN WAQYRPGLGS FKPDDINPCL CTHLIYAFAG 70 80 90 100 110 120 MQNNEITTIE WNDVTLYKAF NDLKNRNSKL KTLLAIGGWN FGTAPFTTMV STSQNRQTFI 130 140 150 160 170 180 TSVIKFLRQY GFDGLDLDWE YPGSRGSPPQ DKHLFTVLVK EMREAFEQEA IESNRPRLMV 190 200 210 220 230 240 TAAVAGGISN IQAGYEIPEL SKYLDFIHVM TYDLHGSWEG YTGENSPLYK YPTETGSNAY 250 260 270 280 290 300 LNVDYVMNYW KNNGAPAEKL IVGFPEYGHT FILRNPSDNG IGAPTSGDGP AGPYTRQAGF 310 320 330 340 350 360 WAYYEICTFL RSGATEVWDA SQEVPYAYKA NEWLGYDNIK SFSVKAQWLK QNNFGGAMIW 370 380 390 400 410 420 AIDLDDFTGS FCDQGKFPLT STLNKALGIS TEGCTAPDVP SEPVTTPPGS GSGGGSSGGS 430 440 450 460 470 SGGSGFCADK ADGLYPVADD RNAFWQCING ITYQQHCQAG LVFDTSCNCC NWP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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: 11085997] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 22-43, TISSUE SPECIFICITY, FUNCTION. Strain: BALB/c. Tissue: Lung.
[2]	"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]. Strain: C57BL/6J and NOD. Tissue: Stomach.
[3]	"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]. Tissue: Salivary gland.
[4]	"YNL, a putative mouse chitinase." Price P.A., Harris S.C., Williamson M.K. Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-473. Tissue: Skin.
[5]	"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: 15192232] [Abstract] Cited for: FUNCTION, INDUCTION, TISSUE SPECIFICITY.
[6]	"A single histidine residue modulates enzymatic activity in acidic mammalian chitinase." Bussink A.P., Vreede J., Aerts J.M., Boot R.G. FEBS Lett. 582:931-935(2008) [PubMed: 18294964] [Abstract] Cited for: MUTAGENESIS OF HIS-208, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
[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: 18824549] [Abstract] Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[8]	"Expression, purification and in vitro antifungal activity of acidic mammalian chitinase against Candida albicans, Aspergillus fumigatus and Trichophyton rubrum strains." Chen L., Shen Z., Wu J. Clin. Exp. Dermatol. 34:55-60(2009) [PubMed: 19076793] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF290003 mRNA. Translation: AAG60018.1. AK008633 mRNA. Translation: BAB25795.1. AK160173 mRNA. Translation: BAE35672.1. BC011134 mRNA. Translation: AAH11134.1. Different initiation. BC034548 mRNA. Translation: AAH34548.1. Different initiation. AF154571 mRNA. Translation: AAF31644.1.
IPI	IPI00346516.
RefSeq	NP_075675.2. NM_023186.3.
UniGene	Mm.46418.
3D structure databases
ProteinModelPortal	Q91XA9.
SMR	Q91XA9. Positions 21-397, 425-473.
ModBase	Search...
Protein-protein interaction databases
STRING	Q91XA9.
Protein family/group databases
CAZy	CBM14. Carbohydrate-Binding Module Family 14. GH18. Glycoside Hydrolase Family 18.
Proteomic databases
PRIDE	Q91XA9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000079132; ENSMUSP00000078134; ENSMUSG00000062778.
GeneID	81600.
KEGG	mmu:81600.
Organism-specific databases
CTD	27159.
MGI	MGI:1932052. Chia.
Phylogenomic databases
GeneTree	ENSGT00550000074323.
HOGENOM	HBG443716.
HOVERGEN	HBG011684.
InParanoid	Q91XA9.
OMA	GITYQQH.
OrthoDB	EOG476K16.
PhylomeDB	Q91XA9.
Gene expression databases
ArrayExpress	Q91XA9.
Bgee	Q91XA9.
CleanEx	MM_CHIA.
Genevestigator	Q91XA9.
GermOnline	ENSMUSG00000062778. Mus musculus.
Family and domain databases
InterPro	IPR002557. Chitin-bd_dom. IPR011583. Chitinase_II. IPR001223. Glyco_hydro18cat. IPR001579. Glyco_hydro_18_chit_AS. IPR013781. Glyco_hydro_subgr_catalytic. IPR017853. Glycoside_hydrolase_SF. [Graphical view]
Gene3D	G3DSA:2.170.140.10. Chitin-bd_dom. 1 hit. G3DSA:3.20.20.80. Glyco_hydro_cat. 2 hits.
KO	K01183.
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]
SUPFAM	SSF57625. Chitin_bind_PerA. 1 hit. SSF51445. Glyco_hydro_cat. 1 hit.
PROSITE	PS50940. CHIT_BIND_II. 1 hit. PS01095. CHITINASE_18. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	350410.
SOURCE	Search...

Entry information

Entry name

CHIA_MOUSE

Accession

Primary (citable) accession number: Q91XA9
Secondary accession number(s): Q3TVE7 , Q99PH2, Q9D803, Q9JLN1

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 24, 2003
Last sequence update:	October 24, 2003
Last modified:	November 16, 2011
This is version 99 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program