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Reviewed, UniProtKB/Swiss-Prot Q8SPQ0 (CH3L1_CAPHI)

Last modified June 16, 2009. Version 47. 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
      Short name=MGP-40
    BP40
Gene names
Name: CHI3L1
OrganismCapra hircus (Goat)
Taxonomic identifier9925 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeCaprinaeCapra

Protein attributes

Sequence length383 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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.

Subunit structure

Monomer.

Subcellular location

Secretedextracellular space.

Sequence similarities

Belongs to the glycosyl hydrolase 18 family.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   LigandLectin
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Direct protein sequencing
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

Signal peptide1 – 2121
Chain22 – 383362Chitinase-3-like protein 1
PRO_0000011964

Regions

Region70 – 712Chitooligosaccharide binding
Region97 – 1004Chitooligosaccharide binding
Region204 – 2074Chitooligosaccharide

Sites

Binding site1411Chitooligosaccharide
Binding site2631Chitooligosaccharide
Binding site3521Chitooligosaccharide

Amino acid modifications

Glycosylation601N-linked (GlcNAc...)
Glycosylation3671N-linked (GlcNAc...) Potential
Disulfide bond26 ↔ 51
Disulfide bond300 ↔ 364

Secondary structure

..................................................................... 383
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8SPQ0-1 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 17655ED4BE4E9F5F

FASTA38342,894
        10         20         30         40         50         60 
MGLRASGTGF VVLVLLQSCA AYKLICYYTS WSQYREGDGS CFPDAIDPFL CTHIIYSFAN 

        70         80         90        100        110        120 
ISNNEIDTWE WNDVTLYDTL NTLKNRNPKL KTLLSVGGWN FGPERFSKIA SKTQSRRTFI 

       130        140        150        160        170        180 
KSVPPFLRTH GFDGLDLAWL YPGRRDKRHL TGLVKEMKAE FAREAQAGTE RLLLSAAVSA 

       190        200        210        220        230        240 
GKIAIDRGYD IAQISRHLDF ISLLTYDFHG AWRQTVGHHS PLFRGQEDAS SDRFSNADYA 

       250        260        270        280        290        300 
VSYMLRLGAP ANKLVMGIPT FGRSFTLASS KTDVGAPISG PGIPGRFTKE KGILAYYEIC 

       310        320        330        340        350        360 
DFLHGATTHR FRDQQVPYAT KGNQWVAYDD QESVKNKARY LKNRQLAGAM VWALDLDDFR 

       370        380 
GTFCGQNLTF PLTSAVKDVL AEV 

« Hide

References

[1]"Crystal structure of a novel regulatory 40-kDa mammary gland protein (MGP-40) secreted during involution."
Mohanty A.K., Singh G., Paramasivam M., Saravanan K., Jabeen T., Sharma S., Yadav S., Kaur P., Kumar P., Srinivasan A., Singh T.P.
J. Biol. Chem. 278:14451-14460(2003) [PubMed: 12529329] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF N-TERMINUS, X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 22-383 IN COMPLEX WITH CHITIN OLIGOMERS.
Tissue: Mammary gland.
[2]"Carbohydrate-binding properties of goat secretory glycoprotein (SPG-40) and its functional implications: structures of the native glycoprotein and its four complexes with chitin-like oligosaccharides."
Kumar J., Ethayathulla A.S., Srivastava D.B., Singh N., Sharma S., Kaur P., Srinivasan A., Singh T.P.
Acta Crystallogr. D 63:437-446(2007) [PubMed: 17372347] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS) OF 22-381 IN COMPLEXES WITH OLIGOSACCHARIDES, GLYCOSYLATION AT ASN-60, DISULFIDE BONDS.

Cross-references

Sequence databases

AY081150 mRNA. Translation: AAL87007.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1LJYX-ray2.90A22-383[»]
1SYTX-ray2.60A22-381[»]
1ZBVX-ray3.21A22-381[»]
1ZBWX-ray2.80A22-381[»]
1ZU8X-ray3.05A22-381[»]
2AOSX-ray2.90A22-381[»]
2B31X-ray3.10A22-381[»]
2DSZX-ray2.35A22-381[»]
2DT0X-ray2.45A22-381[»]
2DT1X-ray2.09A22-381[»]
2DT2X-ray2.90A22-381[»]
2DT3X-ray2.28A22-381[»]
2O92X-ray3.00A22-381[»]
2OLHX-ray2.78A22-381[»]
ModBaseSearch...

Protein family/group databases

CAZyGH18. Glycoside Hydrolase Family 18.

Phylogenomic databases

HOVERGENQ8SPQ0.

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_CAPHI
AccessionPrimary (citable) accession number: Q8SPQ0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: June 1, 2002
Last modified: June 16, 2009
This is version 47 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

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