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P36222 (CH3L1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Chitinase-3-like protein 1
Alternative name(s):
39 kDa synovial protein
Cartilage glycoprotein 39
Short name=CGP-39
Short name=GP-39
Short name=hCGP-39
YKL-40
Gene names
Name:CHI3L1
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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. Ref.8

Subunit structure

Monomer.

Subcellular location

Secretedextracellular space Ref.8.

Tissue specificity

Present in activated macrophages, articular chondrocytes, synovial cells as well as in liver. Undetectable in muscle tissues, lung, pancreas, mononuclear cells, or fibroblasts. Ref.8

Post-translational modification

Glycosylated. Ref.9

Involvement in disease

A genetic variation in CHI3L1 is associated with susceptibility to asthma-related traits type 7 (ASRT7) [MIM:611960]. Asthma-related traits include clinical symptoms of asthma, such as coughing, wheezing and dyspnea, bronchial hyperresponsiveness (BHR) as assessed by methacholine challenge test, serum IgE levels, atopy, and atopic dermatitis.

Sequence similarities

Belongs to the glycosyl hydrolase 18 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Ref.7
Chain22 – 383362Chitinase-3-like protein 1
PRO_0000011965

Regions

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

Sites

Binding site1411Chitooligosaccharide
Binding site2631Chitooligosaccharide
Binding site3521Chitooligosaccharide

Amino acid modifications

Glycosylation601N-linked (GlcNAc...) Ref.9
Disulfide bond26 ↔ 51 Ref.9 Ref.10
Disulfide bond300 ↔ 364 Ref.9 Ref.10

Natural variations

Natural variant1451R → G. Ref.3 Ref.6
Corresponds to variant rs880633 [ dbSNP | Ensembl ].
VAR_019838
Natural variant3111I → T. Ref.1 Ref.2
Corresponds to variant rs1049407 [ dbSNP | Ensembl ].
VAR_019839

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P36222 [UniParc].

Last modified December 20, 2005. Version 2.
Checksum: 6C9EF133BDC7C2D1

FASTA38342,625
        10         20         30         40         50         60 
MGVKASQTGF VVLVLLQCCS AYKLVCYYTS WSQYREGDGS CFPDALDRFL CTHIIYSFAN 

        70         80         90        100        110        120 
ISNDHIDTWE WNDVTLYGML NTLKNRNPNL KTLLSVGGWN FGSQRFSKIA SNTQSRRTFI 

       130        140        150        160        170        180 
KSVPPFLRTH GFDGLDLAWL YPGRRDKQHF TTLIKEMKAE FIKEAQPGKK QLLLSAALSA 

       190        200        210        220        230        240 
GKVTIDSSYD IAKISQHLDF ISIMTYDFHG AWRGTTGHHS PLFRGQEDAS PDRFSNTDYA 

       250        260        270        280        290        300 
VGYMLRLGAP ASKLVMGIPT FGRSFTLASS ETGVGAPISG PGIPGRFTKE AGTLAYYEIC 

       310        320        330        340        350        360 
DFLRGATVHR ILGQQVPYAT KGNQWVGYDD QESVKSKVQY LKDRQLAGAM VWALDLDDFQ 

       370        380 
GSFCGQDLRF PLTNAIKDAL AAT 

« Hide

References

« Hide 'large scale' references
[1]"Human cartilage gp-39, a major secretory product of articular chondrocytes and synovial cells, is a mammalian member of a chitinase protein family."
Hakala B.E., White C., Recklies A.D.
J. Biol. Chem. 268:25803-25810(1993) [PubMed: 8245017] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, VARIANT THR-311.
Tissue: Cartilage.
[2]"Molecular characterization of the gene for human cartilage gp-39 (CHI3L1), a member of the chitinase protein family and marker for late stages of macrophage differentiation."
Rehli M., Krause S.W., Andressen R.
Genomics 43:221-225(1997) [PubMed: 9244440] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT THR-311.
Tissue: Blood.
[3]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT GLY-145.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT GLY-145.
Tissue: Brain.
[7]"Human synovial cells secrete a 39 kDa protein similar to a bovine mammary protein expressed during the non-lactating period."
Nyirkos P., Golds E.E.
Biochem. J. 269:265-268(1990) [PubMed: 2375755] [Abstract]
Cited for: PROTEIN SEQUENCE OF 22-45.
[8]"Chitotriosidase, a chitinase, and the 39-kDa human cartilage glycoprotein, a chitin-binding lectin, are homologues of family 18 glycosyl hydrolases secreted by human macrophages."
Renkema G.H., Boot R.G., Au F.L., Donker-Koopman W.E., Strijland A., Muijsers A.O., Hrebicek M., Aerts J.M.F.G.
Eur. J. Biochem. 251:504-509(1998) [PubMed: 9492324] [Abstract]
Cited for: PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[9]"Structure and ligand-induced conformational change of the 39-kDa glycoprotein from human articular chondrocytes."
Houston D.R., Recklies A.D., Krupa J.C., van Aalten D.M.F.
J. Biol. Chem. 278:30206-30212(2003) [PubMed: 12775711] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 22-383 IN COMPLEX WITH CHITIN OLIGOMERS, DISULFIDE BONDS, GLYCOSYLATION AT ASN-60.
[10]"Crystal structure and carbohydrate-binding properties of the human cartilage glycoprotein-39."
Fusetti F., Pijning T., Kalk K.H., Bos E., Dijkstra B.W.
J. Biol. Chem. 278:37753-37760(2003) [PubMed: 12851408] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 22-383 IN COMPLEX WITH CHITIN OLIGOMERS, DISULFIDE BONDS.
[11]"Effect of variation in CHI3L1 on serum YKL-40 level, risk of asthma, and lung function."
Ober C., Tan Z., Sun Y., Possick J.D., Pan L., Nicolae R., Radford S., Parry R.R., Heinzmann A., Deichmann K.A., Lester L.A., Gern J.E., Lemanske R.F. Jr., Nicolae D.L., Elias J.A., Chupp G.L.
N. Engl. J. Med. 358:1682-1691(2008) [PubMed: 18403759] [Abstract]
Cited for: INVOLVEMENT IN SUSCEPTIBILITY TO ASTHMA-RELATED TRAITS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M80927 mRNA. Translation: AAA16074.1.
Y08374 expand/collapse EMBL AC list , Y08375, Y08376, Y08377, Y08378 Genomic DNA. Translation: CAA69661.1.
BT007223 mRNA. Translation: AAP35887.1.
AK312911 mRNA. Translation: BAG35757.1.
CH471067 Genomic DNA. Translation: EAW91467.1.
BC008568 mRNA. Translation: AAH08568.1.
BC038354 mRNA. Translation: AAH38354.1.
BC039132 mRNA. Translation: AAH39132.1.
IPIIPI00002147.
PIRA49562.
RefSeqNP_001267.2. NM_001276.2.
UniGeneHs.382202.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1HJVX-ray2.75A/B/C/D22-383[»]
1HJWX-ray2.30A/B22-383[»]
1HJXX-ray1.85A/B/C/D22-383[»]
1LA7model-A22-383[»]
1NWRX-ray2.70A/B/C/D22-383[»]
1NWSX-ray2.70A/B/C/D22-383[»]
1NWTX-ray2.50A/B/C/D22-383[»]
1NWUX-ray2.20A/B/C/D22-383[»]
ProteinModelPortalP36222.
SMRP36222. Positions 22-382.
ModBaseSearch...

Protein-protein interaction databases

STRINGP36222.

Protein family/group databases

CAZyGH18. Glycoside Hydrolase Family 18.

PTM databases

PhosphoSiteP36222.

Polymorphism databases

DMDM84028186.

Proteomic databases

PeptideAtlasP36222.
PRIDEP36222.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000255409; ENSP00000255409; ENSG00000133048.
GeneID1116.
KEGGhsa:1116.
UCSCuc001gzi.2. human.

Organism-specific databases

CTD1116.
GeneCardsGC01M203148.
H-InvDBHIX0001487.
HGNCHGNC:1932. CHI3L1.
MIM601525. gene.
611960. phenotype.
neXtProtNX_P36222.
PharmGKBPA26463.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG13745.
HOGENOMHBG443716.
HOVERGENHBG011684.
InParanoidP36222.
OMATQSRRTF.
OrthoDBEOG40K7ZX.
PhylomeDBP36222.

Gene expression databases

ArrayExpressP36222.
BgeeP36222.
CleanExHS_CHI3L1.
GenevestigatorP36222.
GermOnlineENSG00000133048. Homo sapiens.

Family and domain databases

InterProIPR011583. Chitinase_II.
IPR001223. Glyco_hydro18cat.
IPR013781. Glyco_hydro_subgr_catalytic.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
Gene3DG3DSA:3.20.20.80. Glyco_hydro_cat. 2 hits.
KOK01183.
PfamPF00704. Glyco_hydro_18. 1 hit.
[Graphical view]
SMARTSM00636. Glyco_18. 1 hit.
[Graphical view]
SUPFAMSSF51445. Glyco_hydro_cat. 1 hit.
PROSITEPS01095. CHITINASE_18. False negative.
[Graphical view]
ProtoNetSearch...

Other

NextBio4626.
SOURCESearch...

Entry information

Entry nameCH3L1_HUMAN
AccessionPrimary (citable) accession number: P36222
Secondary accession number(s): B2R7B0 expand/collapse secondary AC list , P30923, Q8IVA4, Q96HI7
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: December 20, 2005
Last modified: January 25, 2012
This is version 119 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families