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Reviewed, UniProtKB/Swiss-Prot Q7YS85 (CH3L1_BUBBU)

Last modified June 16, 2009. Version 38. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
    Chitinase-3-like protein 1
Alternative name(s):
    Mammary gland protein 40
    SPB-40
Gene names
Name: CHI3L1
OrganismBubalus bubalis (Domestic water buffalo)
Taxonomic identifier89462 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBubalus

Protein attributes

Sequence length361 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Carbohydrate-binding lectin with a preference for chitin. May play a role in defense against pathogens, or in tissue remodeling. May play an important role in the capacity of cells to respond to and cope with changes in their environment By similarity.

Subunit structure

Monomer.

Subcellular location

Secretedextracellular space.

Tissue specificity

Detected in mammary gland.

Sequence similarities

Belongs to the glycosyl hydrolase 18 family.

Ontologies

Keywords
   Cellular componentSecreted
   LigandLectin
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Gene Ontology (GO)
   Biological processchitin catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentextracellular space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncation binding

Inferred from electronic annotation. Source: InterPro

chitinase activity

Inferred from electronic annotation. Source: InterPro

sugar binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 361361Chitinase-3-like protein 1
PRO_0000077054

Regions

Region49 – 502Chitooligosaccharide binding By similarity
Region76 – 794Chitooligosaccharide binding By similarity
Region183 – 1864Chitooligosaccharide By similarity

Sites

Binding site2411Chitooligosaccharide By similarity
Binding site3301Chitooligosaccharide By similarity

Amino acid modifications

Glycosylation391N-linked (GlcNAc...)
Glycosylation3451N-linked (GlcNAc...) Potential
Disulfide bond5 ↔ 30
Disulfide bond278 ↔ 342

Secondary structure

......................................................................... 361
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q7YS85-1 [UniParc].

Last modified July 5, 2004. Version 2.
Checksum: D7DAD2106F34C0A6

FASTA36140,891
        10         20         30         40         50         60 
YKLICYYTSW SQYREGDGSC FPDAIDPFLC THVIYSFANI SNNEIDTWEW NDVTLYDTLN 

        70         80         90        100        110        120 
TLKNRNPNLK TLLSVGGWNY GSQRFSKIAS KTQSRRTFIK SVPPFLRTHG FDGLDLAWLW 

       130        140        150        160        170        180 
PGWRDKRHLT TLVKEMKAEF VREAQAGTEQ LLLSAAVTAG KIAIDRGYDI AQISRHLDFI 

       190        200        210        220        230        240 
SLLTYDFHGA WRQTVGHHSP LFRGNEDASS RFSNADYAVS YMLRLGAPAN KLVMGIPTFG 

       250        260        270        280        290        300 
RSYTLASSKT DVGAPISGPG IPGRFTKWKG ILAYYEICDF LHGATTHRFR DQQVPYATKG 

       310        320        330        340        350        360 
NQWVAYDDQE SVKNKARYLK NRQLAGAMVW ALDLDDFRGT FCGQNLTFPL TSAIKDVLAR 


V 

« Hide

References

[1]"Buffalo mammary gland protein."
Bilgrami S., Saravanan K., Yadav S., Kaur P., Srinivasan A., Singh T.P.
Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Mammary gland.
[2]"Structure of the buffalo secretory signalling glycoprotein at 2.8 A resolution."
Ethayathulla A.S., Srivastava D.B., Kumar J., Saravanan K., Bilgrami S., Sharma S., Kaur P., Srinivasan A., Singh T.P.
Acta Crystallogr. F 63:258-265(2007) [PubMed: 17401190] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS), GLYCOSYLATION AT ASN-39, DISULFIDE BONDS.

Cross-references

Sequence databases

AY295929 mRNA. Translation: AAP42568.2.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1TFVX-ray2.90A1-361[»]
2O9OX-ray2.80A1-361[»]
2QF8X-ray2.80A1-361[»]
ModBaseSearch...

Protein family/group databases

CAZyGH18. Glycoside Hydrolase Family 18.

Phylogenomic databases

HOVERGENQ7YS85.

Family and domain databases

InterProIPR011583. 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.
PfamPF00704. Glyco_hydro_18. 1 hit.
[Graphical view]
ProDomPD000471. Chitinase_II. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00636. Glyco_18. 1 hit.
[Graphical view]
PROSITEPS01095. CHITINASE_18. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCH3L1_BUBBU
AccessionPrimary (citable) accession number: Q7YS85
Entry history
Integrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: July 5, 2004
Last modified: June 16, 2009
This is version 38 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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