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Reviewed, UniProtKB/Swiss-Prot Q95M17 (CHIA_BOVIN)

Last modified June 16, 2009. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Acidic mammalian chitinase
      Short name=AMCase
    EC=3.2.1.14
Alternative name(s):
    Chitin-binding protein b04
      Short name=CBPb04
Gene names
Name: CHIA
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length472 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. May participate in the defense against nematodes and other pathogens. Ref.1

Catalytic activity

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

Subcellular location

Secreted. Ref.1

Tissue specificity

Detected in liver and in serum. Ref.1

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 5.6-7.6.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Ref.1
Chain22 – 472451Acidic mammalian chitinase
PRO_0000011943

Regions

Domain423 – 47250Chitin-binding type-2
Compositional bias417 – 4204Poly-Ser

Sites

Active site1401Proton donor By similarity

Amino acid modifications

Glycosylation3951N-linked (GlcNAc...) Potential
Glycosylation4091N-linked (GlcNAc...) Potential
Glycosylation4151N-linked (GlcNAc...) Potential
Disulfide bond26 ↔ 51 By similarity
Disulfide bond307 ↔ 372 By similarity
Disulfide bond456 ↔ 469 By similarity

Experimental info

Sequence conflict1441F → S in AAI02932. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q95M17-1 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 7A4A600E8DA04B1E

FASTA47252,129
        10         20         30         40         50         60 
MAKLIFLTGL AFLLNAQLGS AYQLVCYFSN WAQYRPGLGS FKPDNIDPCL CTHLIYAFAG 

        70         80         90        100        110        120 
MSNSEITTIE WNDVALYSSF NDLKKKNSQL KILLAIGGWN FGTAPFTAMV ATPENRKTFI 

       130        140        150        160        170        180 
SSVIKFLHQY GFDGLDFDWE YPGFRGSPSQ DKHLFTVLVQ ETREAFEQEA KQTNKPRLLV 

       190        200        210        220        230        240 
TAAVAAGISN IQAGYEIPQL SQYLDFIHVM TYDFHGSWEG YTGENSPLYK YPTDTGSNTY 

       250        260        270        280        290        300 
LNVEYAMNYW KKNGAPAEKL IIGFPAYGHN FILRDASNNG IGAPTSGAGP AGPYTREAGF 

       310        320        330        340        350        360 
WAYYEICAFL KDGATEAWDD SQNVPYAYKG TEWVGYDNVN SFRIKAQWLK ENNFGGAMVW 

       370        380        390        400        410        420 
AIDLDDFTGT FCNQGKFPLI NTLKDALGLK SATCNASTQS SEPNSSPGNE SGSGNKSSSS 

       430        440        450        460        470 
EGRGYCAGKA DGLYPVADNR NAFWNCVNGI TYKQNCLTGL VFDTSCHCCN WA 

« Hide

References

« Hide 'large scale' references
[1]"A novel serum chitinase that is expressed in bovine liver."
Suzuki M., Morimatsu M., Yamashita T., Iwanaga T., Syuto B.
FEBS Lett. 506:127-130(2001) [PubMed: 11591385] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 22-40; 126-171 AND 312-350, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: Liver.
[2]NIH - Mammalian Gene Collection (MGC) project
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Fetal liver.

Cross-references

Sequence databases

AB051629 mRNA. Translation: BAB71805.1.
BC102931 mRNA. Translation: AAI02932.1.
IPIIPI00704127.
RefSeqNP_777124.1.
UniGeneBt.66344

3D structure databases

HSSPHSSP built from PDB template 1E9L based on UniProtKB O35744.
ModBaseSearch...

Protein family/group databases

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

Genome annotation databases

EnsemblENSBTAG00000000259. Bos taurus. [Contig view]
GeneID282645.
KEGGbta:282645.

Phylogenomic databases

HOVERGENQ95M17.

Enzyme and pathway databases

BRENDA3.2.1.14. 251.

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...

Entry information

Entry nameCHIA_BOVIN
AccessionPrimary (citable) accession number: Q95M17
Secondary accession number(s): Q3SZE1
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: December 1, 2001
Last modified: June 16, 2009
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

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