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Reviewed, UniProtKB/Swiss-Prot P30922 (CH3L1_BOVIN)

Last modified June 16, 2009. Version 76. 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

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Names and origin

Protein namesRecommended name:
    Chitinase-3-like protein 1
Alternative name(s):
    Cartilage glycoprotein 39
      Short name=CGP-39
      Short name=GP-39
    39 kDa whey protein
    Signal-processing protein
    SPC-40
    Chitinase-like protein 1
      Short name=CLP-1
Gene names
Name: CHI3L1
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

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Protein attributes

Sequence length383 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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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

Secreted › extracellular space.

Tissue specificity

Mammary secretions collected during the non-lactating period.

Post-translational modification

Glycosylated.

Sequence similarities

Belongs to the glycosyl hydrolase 18 family.

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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...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Ref.3
Chain22 – 383362Chitinase-3-like protein 1
PRO_0000042787

Regions

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

Sites

Binding site1411Chitooligosaccharide By similarity
Binding site2631Chitooligosaccharide By similarity
Binding site3521Chitooligosaccharide By similarity

Amino acid modifications

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

Experimental info

Sequence conflict251I → V in AAB64304. Ref.4
Sequence conflict1041Q → E in AAP41220. Ref.2
Sequence conflict1641E → G in AAB64304. Ref.4
Sequence conflict1791P → T in AAP41220. Ref.2
Sequence conflict2111A → G in AAP41220. Ref.2
Sequence conflict2141Q → G in AAP41220. Ref.2
Sequence conflict226 – 2327QEDASSD → NSDGSS in AAP41220. Ref.2
Sequence conflict271 – 2733KTD → STR in AAP41220. Ref.2
Sequence conflict3071T → I in AAX46682. Ref.1
Sequence conflict3691T → A in AAX46682. Ref.1
Sequence conflict3821R → E in AAX46682. Ref.1

Secondary structure

1 ........................................................................ 383
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P30922-1 [UniParc].

Last modified November 8, 2005. Version 3.
Checksum: 391561804C371A10

FASTA38343,032
        10         20         30         40         50         60 
MGLRAAHTGF VVLVLLQSCA AYKLICYYTS WSQYREGDGS CFPDAIDPFL CTHVIYSFAN 

        70         80         90        100        110        120 
ISNNEIDTWE WNDVTLYDTL NTLKNRNPNL KTLLSVGGWN FGSQRFSKIA SKTQSRRTFI 

       130        140        150        160        170        180 
KSVPPFLRTH GFDGLDLAWL YPGWRDKRHL TTLVKEMKAE FVREAQAGTE QLLLSAAVPA 

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

       250        260        270        280        290        300 
VSYMLRLGAP ANKLVMGIPT FGRSYTLASS KTDVGAPISG PGIPGQFTKE KGILAYYEIC 

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

       370        380 
GTFCGQNLTF PLTSAIKDVL ARV

« Hide

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References

« Hide 'large scale' references
[1]"Characterization of 954 bovine full-CDS cDNA sequences."
Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.
BMC Genomics 6:166-166(2005) [PubMed: 16305752] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[2]"Signal processing protein from bovine mammary gland."
Srinivasan A., Kumar J., Singh T.P.
Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 22-383.
Tissue: Mammary gland.
[3]"Isolation and characterization of a novel 39 kilodalton whey protein from bovine mammary secretions collected during the nonlactating period."
Rejman J.J., Hurley W.L.
Biochem. Biophys. Res. Commun. 150:329-334(1988) [PubMed: 3122754] [Abstract]
Cited for: PROTEIN SEQUENCE OF 22-57.
[4]"Expression of chitinase-like protein 1 (CLP-1) in bovine chondrocytes."
Recklies A.D., White C.
Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 25-356.
[5]"Structure of a bovine secretory signalling glycoprotein (SPC-40) at 2.1 Angstrom resolution."
Kumar J., Ethayathulla A.S., Srivastava D.B., Sharma S., Singh S.B., Srinivasan A., Yadav M.P., Singh T.P.
Acta Crystallogr. D 62:953-963(2006) [PubMed: 16929095] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 22-383, GLYCOSYLATION AT ASN-60, DISULFIDE BONDS, FUNCTION.

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Cross-references

Sequence databases

BT021835 mRNA. Translation: AAX46682.1. Different initiation.
AY291312 mRNA. Translation: AAP41220.2.
AF011373 mRNA. Translation: AAB64304.1.
IPIIPI00717764.
PIRA27682.
RefSeqNP_001073688.1.
UniGeneBt.60417

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1OWQX-ray2.00A22-383[»]
2ESCX-ray2.10A22-383[»]
ModBaseSearch...

Protein family/group databases

CAZyGH18. Glycoside Hydrolase Family 18.

Genome annotation databases

EnsemblENSBTAG00000018223. Bos taurus. [Contig view]
GeneID286869.
KEGGbta:286869.

Phylogenomic databases

HOVERGENP30922.

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...

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Entry information

Entry nameCH3L1_BOVIN
AccessionPrimary (citable) accession number: P30922
Secondary accession number(s): O18949, Q58CW2, Q7YSE8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: November 8, 2005
Last modified: June 16, 2009
This is version 76 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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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