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Protein

Acidic mammalian chitinase

Gene

Chia

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

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 (By similarity).By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei140 – 1401Proton donorPROSITE-ProRule annotation
Binding sitei141 – 1411ChitooligosaccharideBy similarity
Binding sitei360 – 3601ChitooligosaccharideBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Apoptosis, Carbohydrate metabolism, Chitin degradation, Immunity, Inflammatory response, Polysaccharide degradation

Keywords - Ligandi

Chitin-binding

Protein family/group databases

CAZyiCBM14. Carbohydrate-Binding Module Family 14.
GH18. Glycoside Hydrolase Family 18.

Names & Taxonomyi

Protein namesi
Recommended name:
Acidic mammalian chitinase (EC:3.2.1.14)
Short name:
AMCase
Gene namesi
Name:Chia
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi1303058. Chia.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • extracellular region Source: RGD
  • extracellular space Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121By similarityAdd
BLAST
Chaini22 – 473452Acidic mammalian chitinasePRO_0000011946Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi26 ↔ 51PROSITE-ProRule annotation
Disulfide bondi49 ↔ 394PROSITE-ProRule annotation
Disulfide bondi307 ↔ 372PROSITE-ProRule annotation
Disulfide bondi457 ↔ 470PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiQ6RY07.
PRIDEiQ6RY07.

Interactioni

Subunit structurei

Interacts with EGFR.By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000044947.

Structurei

3D structure databases

ProteinModelPortaliQ6RY07.
SMRiQ6RY07. Positions 22-394.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini424 – 47350Chitin-binding type-2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni70 – 712Chitooligosaccharide bindingBy similarity
Regioni97 – 1004Chitooligosaccharide bindingBy similarity
Regioni210 – 2134Chitooligosaccharide bindingBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi409 – 42517Gly/Ser-richAdd
BLAST

Sequence similaritiesi

Contains 1 chitin-binding type-2 domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG2806. Eukaryota.
COG3325. LUCA.
HOGENOMiHOG000111109.
HOVERGENiHBG011684.
InParanoidiQ6RY07.
KOiK01183.
PhylomeDBiQ6RY07.

Family and domain databases

Gene3Di2.170.140.10. 1 hit.
3.10.50.10. 1 hit.
3.20.20.80. 2 hits.
InterProiIPR002557. Chitin-bd_dom.
IPR011583. Chitinase_II.
IPR029070. Chitinase_insertion.
IPR001223. Glyco_hydro18_cat.
IPR001579. Glyco_hydro_18_chit_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF01607. CBM_14. 1 hit.
PF00704. Glyco_hydro_18. 1 hit.
[Graphical view]
SMARTiSM00494. ChtBD2. 1 hit.
SM00636. Glyco_18. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 2 hits.
SSF54556. SSF54556. 1 hit.
SSF57625. SSF57625. 1 hit.
PROSITEiPS50940. CHIT_BIND_II. 1 hit.
PS01095. CHITINASE_18. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q6RY07-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKLILVTGL VLLLNVQLGS AYNLVCYFTN WAQYRPGLGS FKPDDINPCL
60 70 80 90 100
CTHLIYAFAG MQNNQITTIE WNDVTLYKAF NDLKNRNSKL KTLLAIGGWN
110 120 130 140 150
FGTAPFTTMV STSQNRQTFI TSVIKFLRQY GFDGLDLDWE YPGSRGSPPQ
160 170 180 190 200
DKHLFTVLVK ELREAFEQEA IESNRPRLMV TAAVAAGISN IQAGYEIPEL
210 220 230 240 250
SQYLDFIHVM TYDLHGSWDG YTGENSPLYK LPTETGSNAY LNVDYVMNYW
260 270 280 290 300
KDNGAPAEKL IVGFPEYGHT YILSNPSDTG IGAPTSGNGP AGPYTRQAGF
310 320 330 340 350
WAYYEICTFL RNGATQDWDA PQEVPYAYKG NEWVGYDNIK SFSVKAQWLK
360 370 380 390 400
QNNFGGAMIW AIDLDDFTGS FCDQGKFPLT STLNKALDIP TAGCTAPDLP
410 420 430 440 450
SEPVTTPPGS GSGGGSSGGG SEGSGFCAGK ADGLYPVADD RNAFWHCING
460 470
ITYQQHCQAG LVFDTSCNCC NWP
Length:473
Mass (Da):51,951
Last modified:July 5, 2004 - v1
Checksum:iFBB0DB91A42C1EFD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY486074 mRNA. Translation: AAR28968.1.
RefSeqiNP_997469.1. NM_207586.2.
UniGeneiRn.43692.

Genome annotation databases

GeneIDi113901.
KEGGirno:113901.
UCSCiRGD:1303058. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY486074 mRNA. Translation: AAR28968.1.
RefSeqiNP_997469.1. NM_207586.2.
UniGeneiRn.43692.

3D structure databases

ProteinModelPortaliQ6RY07.
SMRiQ6RY07. Positions 22-394.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000044947.

Protein family/group databases

CAZyiCBM14. Carbohydrate-Binding Module Family 14.
GH18. Glycoside Hydrolase Family 18.

Proteomic databases

PaxDbiQ6RY07.
PRIDEiQ6RY07.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi113901.
KEGGirno:113901.
UCSCiRGD:1303058. rat.

Organism-specific databases

CTDi27159.
RGDi1303058. Chia.

Phylogenomic databases

eggNOGiKOG2806. Eukaryota.
COG3325. LUCA.
HOGENOMiHOG000111109.
HOVERGENiHBG011684.
InParanoidiQ6RY07.
KOiK01183.
PhylomeDBiQ6RY07.

Miscellaneous databases

PROiQ6RY07.

Family and domain databases

Gene3Di2.170.140.10. 1 hit.
3.10.50.10. 1 hit.
3.20.20.80. 2 hits.
InterProiIPR002557. Chitin-bd_dom.
IPR011583. Chitinase_II.
IPR029070. Chitinase_insertion.
IPR001223. Glyco_hydro18_cat.
IPR001579. Glyco_hydro_18_chit_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF01607. CBM_14. 1 hit.
PF00704. Glyco_hydro_18. 1 hit.
[Graphical view]
SMARTiSM00494. ChtBD2. 1 hit.
SM00636. Glyco_18. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 2 hits.
SSF54556. SSF54556. 1 hit.
SSF57625. SSF57625. 1 hit.
PROSITEiPS50940. CHIT_BIND_II. 1 hit.
PS01095. CHITINASE_18. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Rattus norvegicus similar to acidic mammalian chitinase precursor."
    Chen X.-H., Cai G.-P.
    Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Stomach.

Entry informationi

Entry nameiCHIA_RAT
AccessioniPrimary (citable) accession number: Q6RY07
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: July 5, 2004
Last modified: July 6, 2016
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.