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Protein

Chitinase-3-like protein 1

Gene

CHI3L1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Carbohydrate-binding lectin with a preference for chitin. Has no chitinase activity. May play a role in tissue remodeling and in the capacity of cells to respond to and cope with changes in their environment. Plays a role in T-helper cell type 2 (Th2) inflammatory response and IL-13-induced inflammation, regulating allergen sensitization, inflammatory cell apoptosis, dendritic cell accumulation and M2 macrophage differentiation. Facilitates invasion of pathogenic enteric bacteria into colonic mucosa and lymphoid organs. Mediates activation of AKT1 signaling pathway and subsequent IL8 production in colonic epithelial cells. Regulates antibacterial responses in lung by contributing to macrophage bacterial killing, controlling bacterial dissemination and augmenting host tolerance. Also regulates hyperoxia-induced injury, inflammation and epithelial apoptosis in lung.4 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei141Chitooligosaccharide1
Binding sitei263Chitooligosaccharide1
Binding sitei352Chitooligosaccharide1

GO - Molecular functioni

  • carbohydrate binding Source: UniProtKB-KW
  • chitin binding Source: UniProtKB
  • extracellular matrix structural constituent Source: UniProtKB
  • hydrolase activity, hydrolyzing O-glycosyl compounds Source: InterPro

GO - Biological processi

  • activation of NF-kappaB-inducing kinase activity Source: UniProtKB
  • apoptotic process Source: UniProtKB-KW
  • carbohydrate metabolic process Source: InterPro
  • cartilage development Source: UniProtKB
  • cellular response to interleukin-1 Source: Ensembl
  • cellular response to tumor necrosis factor Source: UniProtKB
  • inflammatory response Source: UniProtKB
  • interleukin-8 secretion Source: UniProtKB
  • lung development Source: UniProtKB
  • positive regulation of angiogenesis Source: UniProtKB
  • positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
  • positive regulation of peptidyl-threonine phosphorylation Source: UniProtKB
  • positive regulation of protein kinase B signaling Source: UniProtKB
  • response to interleukin-1 Source: UniProtKB
  • response to interleukin-6 Source: UniProtKB
  • response to mechanical stimulus Source: UniProtKB
  • response to tumor necrosis factor Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Antimicrobial

Keywords - Biological processi

Apoptosis, Inflammatory response

Keywords - Ligandi

Lectin

Enzyme and pathway databases

BioCyciZFISH:ENSG00000133048-MONOMER.
ReactomeiR-HSA-6798695. Neutrophil degranulation.
SIGNORiP36222.

Protein family/group databases

CAZyiGH18. Glycoside Hydrolase Family 18.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:CHI3L1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:1932. CHI3L1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • endoplasmic reticulum Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • extracellular space Source: UniProtKB
  • perinuclear region of cytoplasm Source: UniProtKB-SubCell
  • proteinaceous extracellular matrix Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Secreted

Pathology & Biotechi

Involvement in diseasei

Asthma-related traits 7 (ASRT7)1 Publication
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionAsthma-related traits include clinical symptoms of asthma, such as coughing, wheezing, dyspnea, bronchial hyperresponsiveness as assessed by methacholine challenge test, serum IgE levels, atopy and atopic dermatitis.
See also OMIM:611960

Keywords - Diseasei

Asthma

Organism-specific databases

DisGeNETi1116.
MalaCardsiCHI3L1.
MIMi611960. phenotype.
OpenTargetsiENSG00000133048.
PharmGKBiPA26463.

Polymorphism and mutation databases

BioMutaiCHI3L1.
DMDMi84028186.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 212 PublicationsAdd BLAST21
ChainiPRO_000001196522 – 383Chitinase-3-like protein 1Add BLAST362

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi26 ↔ 51
Glycosylationi60N-linked (GlcNAc...)1 Publication1
Disulfide bondi300 ↔ 364

Post-translational modificationi

Glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP36222.
PeptideAtlasiP36222.
PRIDEiP36222.

PTM databases

iPTMnetiP36222.
PhosphoSitePlusiP36222.

Expressioni

Tissue specificityi

Present in activated macrophages, articular chondrocytes, synovial cells as well as in liver. Very low or undetectable expression in non-inflammatory colon. Undetectable in muscle tissues, lung, pancreas, mononuclear cells, or fibroblasts.2 Publications

Inductioni

Up-regulated in colon under several inflammatory conditions. Down-regulated by hyperoxia in bronchial epithelial cells.2 Publications

Gene expression databases

BgeeiENSG00000133048.
CleanExiHS_CHI3L1.
ExpressionAtlasiP36222. baseline and differential.
GenevisibleiP36222. HS.

Interactioni

Subunit structurei

Monomer.2 Publications

Protein-protein interaction databases

BioGridi107540. 6 interactors.
STRINGi9606.ENSP00000255409.

Structurei

Secondary structure

1383
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi23 – 29Combined sources7
Helixi30 – 34Combined sources5
Helixi37 – 39Combined sources3
Helixi43 – 45Combined sources3
Turni48 – 50Combined sources3
Beta strandi52 – 62Combined sources11
Beta strandi65 – 67Combined sources3
Helixi73 – 82Combined sources10
Helixi83 – 85Combined sources3
Beta strandi91 – 97Combined sources7
Turni99 – 101Combined sources3
Helixi103 – 111Combined sources9
Helixi113 – 130Combined sources18
Beta strandi133 – 138Combined sources6
Helixi144 – 146Combined sources3
Helixi147 – 165Combined sources19
Turni166 – 168Combined sources3
Beta strandi173 – 179Combined sources7
Helixi182 – 188Combined sources7
Helixi191 – 197Combined sources7
Beta strandi199 – 204Combined sources6
Helixi211 – 213Combined sources3
Helixi227 – 229Combined sources3
Beta strandi233 – 236Combined sources4
Helixi237 – 247Combined sources11
Helixi251 – 253Combined sources3
Beta strandi254 – 270Combined sources17
Beta strandi277 – 281Combined sources5
Turni286 – 288Combined sources3
Beta strandi293 – 295Combined sources3
Helixi296 – 302Combined sources7
Turni303 – 305Combined sources3
Beta strandi307 – 310Combined sources4
Turni312 – 314Combined sources3
Beta strandi317 – 321Combined sources5
Beta strandi324 – 327Combined sources4
Helixi331 – 343Combined sources13
Beta strandi347 – 352Combined sources6
Helixi354 – 356Combined sources3
Beta strandi359 – 361Combined sources3
Beta strandi363 – 366Combined sources4
Helixi371 – 381Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliP36222.
SMRiP36222.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP36222.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni70 – 71Chitooligosaccharide binding2
Regioni97 – 100Chitooligosaccharide binding4
Regioni204 – 207Chitooligosaccharide binding4
Regioni324 – 338Important for AKT1 activation and IL8 productionBy similarityAdd BLAST15

Sequence similaritiesi

Belongs to the glycosyl hydrolase 18 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG2806. Eukaryota.
COG3325. LUCA.
GeneTreeiENSGT00550000074323.
HOGENOMiHOG000111109.
HOVERGENiHBG011684.
InParanoidiP36222.
KOiK17523.
OMAiIAKISQH.
OrthoDBiEOG091G014W.
PhylomeDBiP36222.
TreeFamiTF315610.

Family and domain databases

Gene3Di3.10.50.10. 1 hit.
3.20.20.80. 2 hits.
InterProiIPR028538. CHI3L1.
IPR011583. Chitinase_II.
IPR029070. Chitinase_insertion.
IPR001223. Glyco_hydro18_cat.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR11177:SF202. PTHR11177:SF202. 1 hit.
PfamiPF00704. Glyco_hydro_18. 1 hit.
[Graphical view]
SMARTiSM00636. Glyco_18. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 2 hits.
SSF54556. SSF54556. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P36222-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGVKASQTGF VVLVLLQCCS AYKLVCYYTS WSQYREGDGS CFPDALDRFL
60 70 80 90 100
CTHIIYSFAN ISNDHIDTWE WNDVTLYGML NTLKNRNPNL KTLLSVGGWN
110 120 130 140 150
FGSQRFSKIA SNTQSRRTFI KSVPPFLRTH GFDGLDLAWL YPGRRDKQHF
160 170 180 190 200
TTLIKEMKAE FIKEAQPGKK QLLLSAALSA GKVTIDSSYD IAKISQHLDF
210 220 230 240 250
ISIMTYDFHG AWRGTTGHHS PLFRGQEDAS PDRFSNTDYA VGYMLRLGAP
260 270 280 290 300
ASKLVMGIPT FGRSFTLASS ETGVGAPISG PGIPGRFTKE AGTLAYYEIC
310 320 330 340 350
DFLRGATVHR ILGQQVPYAT KGNQWVGYDD QESVKSKVQY LKDRQLAGAM
360 370 380
VWALDLDDFQ GSFCGQDLRF PLTNAIKDAL AAT
Length:383
Mass (Da):42,625
Last modified:December 20, 2005 - v2
Checksum:i6C9EF133BDC7C2D1
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_019838145R → G.2 PublicationsCorresponds to variant rs880633dbSNPEnsembl.1
Natural variantiVAR_019839311I → T.2 PublicationsCorresponds to variant rs1049407dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M80927 mRNA. Translation: AAA16074.1.
Y08374
, 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.
CCDSiCCDS1435.1.
PIRiA49562.
RefSeqiNP_001267.2. NM_001276.2.
UniGeneiHs.382202.
Hs.733359.

Genome annotation databases

EnsembliENST00000255409; ENSP00000255409; ENSG00000133048.
GeneIDi1116.
KEGGihsa:1116.
UCSCiuc001gzi.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M80927 mRNA. Translation: AAA16074.1.
Y08374
, 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.
CCDSiCCDS1435.1.
PIRiA49562.
RefSeqiNP_001267.2. NM_001276.2.
UniGeneiHs.382202.
Hs.733359.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliP36222.
SMRiP36222.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107540. 6 interactors.
STRINGi9606.ENSP00000255409.

Protein family/group databases

CAZyiGH18. Glycoside Hydrolase Family 18.

PTM databases

iPTMnetiP36222.
PhosphoSitePlusiP36222.

Polymorphism and mutation databases

BioMutaiCHI3L1.
DMDMi84028186.

Proteomic databases

PaxDbiP36222.
PeptideAtlasiP36222.
PRIDEiP36222.

Protocols and materials databases

DNASUi1116.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000255409; ENSP00000255409; ENSG00000133048.
GeneIDi1116.
KEGGihsa:1116.
UCSCiuc001gzi.3. human.

Organism-specific databases

CTDi1116.
DisGeNETi1116.
GeneCardsiCHI3L1.
HGNCiHGNC:1932. CHI3L1.
MalaCardsiCHI3L1.
MIMi601525. gene.
611960. phenotype.
neXtProtiNX_P36222.
OpenTargetsiENSG00000133048.
PharmGKBiPA26463.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2806. Eukaryota.
COG3325. LUCA.
GeneTreeiENSGT00550000074323.
HOGENOMiHOG000111109.
HOVERGENiHBG011684.
InParanoidiP36222.
KOiK17523.
OMAiIAKISQH.
OrthoDBiEOG091G014W.
PhylomeDBiP36222.
TreeFamiTF315610.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000133048-MONOMER.
ReactomeiR-HSA-6798695. Neutrophil degranulation.
SIGNORiP36222.

Miscellaneous databases

ChiTaRSiCHI3L1. human.
EvolutionaryTraceiP36222.
GeneWikiiCHI3L1.
GenomeRNAii1116.
PROiP36222.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000133048.
CleanExiHS_CHI3L1.
ExpressionAtlasiP36222. baseline and differential.
GenevisibleiP36222. HS.

Family and domain databases

Gene3Di3.10.50.10. 1 hit.
3.20.20.80. 2 hits.
InterProiIPR028538. CHI3L1.
IPR011583. Chitinase_II.
IPR029070. Chitinase_insertion.
IPR001223. Glyco_hydro18_cat.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR11177:SF202. PTHR11177:SF202. 1 hit.
PfamiPF00704. Glyco_hydro_18. 1 hit.
[Graphical view]
SMARTiSM00636. Glyco_18. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 2 hits.
SSF54556. SSF54556. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiCH3L1_HUMAN
AccessioniPrimary (citable) accession number: P36222
Secondary accession number(s): B2R7B0
, P30923, Q8IVA4, Q96HI7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: December 20, 2005
Last modified: November 30, 2016
This is version 163 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Caution

Although it belongs to the glycosyl hydrolase 18 family, Leu-140 is present instead of the conserved Glu which is an active site residue. Therefore this protein lacks chitinase activity.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.