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Protein

Chitinase-3-like protein 1

Gene

CHI3L1

Organism
Ovis aries (Sheep)
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 (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei120Chitooligosaccharide1
Binding sitei241Chitooligosaccharide1
Binding sitei330Chitooligosaccharide1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Antimicrobial

Keywords - Biological processi

Apoptosis, Inflammatory response

Keywords - Ligandi

Lectin

Protein family/group databases

CAZyiGH18. Glycoside Hydrolase Family 18.

Names & Taxonomyi

Protein namesi
Recommended name:
Chitinase-3-like protein 1
Alternative name(s):
Secretory glycoprotein of 40 kDa
Signal-processing protein
Gene namesi
Name:CHI3L1
OrganismiOvis aries (Sheep)
Taxonomic identifieri9940 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeCaprinaeOvis
Proteomesi
  • UP000002356 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000770551 – 361Chitinase-3-like protein 1Add BLAST361

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi5 ↔ 30
Glycosylationi39N-linked (GlcNAc...)2 Publications1
Disulfide bondi278 ↔ 342
Glycosylationi345N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiQ6TMG6.

Expressioni

Tissue specificityi

Detected in mammary gland.

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1361
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 8Combined sources7
Helixi9 – 13Combined sources5
Helixi16 – 18Combined sources3
Helixi22 – 24Combined sources3
Turni27 – 29Combined sources3
Beta strandi31 – 41Combined sources11
Beta strandi44 – 46Combined sources3
Helixi52 – 65Combined sources14
Beta strandi70 – 76Combined sources7
Turni77 – 79Combined sources3
Helixi82 – 89Combined sources8
Helixi92 – 109Combined sources18
Beta strandi112 – 117Combined sources6
Helixi123 – 125Combined sources3
Helixi126 – 144Combined sources19
Turni145 – 147Combined sources3
Beta strandi152 – 157Combined sources6
Helixi161 – 167Combined sources7
Helixi170 – 176Combined sources7
Beta strandi178 – 182Combined sources5
Beta strandi192 – 194Combined sources3
Beta strandi205 – 207Combined sources3
Beta strandi211 – 214Combined sources4
Helixi215 – 224Combined sources10
Helixi229 – 231Combined sources3
Beta strandi232 – 248Combined sources17
Beta strandi255 – 259Combined sources5
Turni264 – 266Combined sources3
Beta strandi271 – 273Combined sources3
Helixi274 – 280Combined sources7
Turni281 – 283Combined sources3
Beta strandi285 – 289Combined sources5
Turni290 – 293Combined sources4
Beta strandi294 – 299Combined sources6
Beta strandi302 – 305Combined sources4
Helixi309 – 321Combined sources13
Beta strandi325 – 330Combined sources6
Helixi332 – 334Combined sources3
Beta strandi337 – 339Combined sources3
Beta strandi341 – 344Combined sources4
Helixi349 – 359Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SR0X-ray3.05A1-361[»]
1ZBKX-ray2.90A1-360[»]
1ZL1X-ray3.50A1-360[»]
2DPEX-ray2.07A1-361[»]
2DSUX-ray2.20A1-361[»]
2DSVX-ray2.54A1-361[»]
2DSWX-ray2.80A1-361[»]
2FDMX-ray3.00A1-360[»]
2G41X-ray3.00A1-361[»]
2G8ZX-ray2.50A1-361[»]
2PI6X-ray1.65A1-361[»]
ProteinModelPortaliQ6TMG6.
SMRiQ6TMG6.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ6TMG6.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni49 – 50Chitooligosaccharide binding2
Regioni76 – 79Chitooligosaccharide binding4
Regioni183 – 186Chitooligosaccharide binding4
Regioni302 – 316Important for AKT1 activation and IL8 productionBy similarityAdd BLAST15

Sequence similaritiesi

Belongs to the glycosyl hydrolase 18 family.Curated

Phylogenomic databases

HOVERGENiHBG011684.

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.

Q6TMG6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
YKLICYYTSW SQYREGDGSC FPDAIDPFLC THVIYSFANI SNNEIDTWEW
60 70 80 90 100
NDVTLYDTLN TLKNRNPKLK TLLSVGGWNF GPERFSAIAS KTQSRRTFIK
110 120 130 140 150
SVPPFLRTHG FDGLDLAWLY PGRRDKRHLT TLVKEMKAEF IREAQAGTEQ
160 170 180 190 200
LLLSAAVSAG KIAIDRGYDI AQISRHLDFI SLLTYDFHGA WRQTVGHHSP
210 220 230 240 250
LFAGNEDASS RFSNADYAVS YMLRLGAPAN KLVMGIPTFG RSFTLASSKT
260 270 280 290 300
DVGAPVSGPG VPGRFTKEKG ILAYYEICDF LHGATTHRFR DQQVPYATKG
310 320 330 340 350
NQWVAYDDQE SVKNKARYLK NRQLAGAMVW ALDLDDFRGT FCGQNLTFPL
360
TSAVKDVLAE V
Length:361
Mass (Da):40,563
Last modified:July 5, 2004 - v1
Checksum:i8642AF873DC5EE3A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY392761 mRNA. Translation: AAQ94054.1.
UniGeneiOar.1069.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY392761 mRNA. Translation: AAQ94054.1.
UniGeneiOar.1069.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SR0X-ray3.05A1-361[»]
1ZBKX-ray2.90A1-360[»]
1ZL1X-ray3.50A1-360[»]
2DPEX-ray2.07A1-361[»]
2DSUX-ray2.20A1-361[»]
2DSVX-ray2.54A1-361[»]
2DSWX-ray2.80A1-361[»]
2FDMX-ray3.00A1-360[»]
2G41X-ray3.00A1-361[»]
2G8ZX-ray2.50A1-361[»]
2PI6X-ray1.65A1-361[»]
ProteinModelPortaliQ6TMG6.
SMRiQ6TMG6.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH18. Glycoside Hydrolase Family 18.

Proteomic databases

PRIDEiQ6TMG6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG011684.

Miscellaneous databases

EvolutionaryTraceiQ6TMG6.

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_SHEEP
AccessioniPrimary (citable) accession number: Q6TMG6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: July 5, 2004
Last modified: November 2, 2016
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

Although it belongs to the glycosyl hydrolase 18 family, Leu-119 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.