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Protein

Chitinase-3-like protein 1

Gene

CHI3L1

Organism
Bubalus bubalis (Domestic water buffalo)
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 sitei263ChitooligosaccharideBy similarity1
Binding sitei352ChitooligosaccharideBy similarity1

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):
Mammary gland protein 40
SPB-40
Gene namesi
Name:CHI3L1
Synonyms:MGP-40
OrganismiBubalus bubalis (Domestic water buffalo)
Taxonomic identifieri89462 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBubalus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 21Add BLAST21
ChainiPRO_000007705422 – 383Chitinase-3-like protein 1Add BLAST362

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi26 ↔ 511 Publication
Glycosylationi60N-linked (GlcNAc...)1 Publication1
Disulfide bondi300 ↔ 3641 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Expressioni

Tissue specificityi

Detected in mammary gland.

Interactioni

Subunit structurei

Monomer.

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
Beta strandi70 – 72Combined sources3
Helixi73 – 82Combined sources10
Helixi83 – 85Combined sources3
Beta strandi91 – 97Combined sources7
Beta strandi99 – 101Combined sources3
Helixi103 – 110Combined sources8
Helixi113 – 130Combined sources18
Beta strandi133 – 138Combined sources6
Turni144 – 146Combined sources3
Helixi147 – 165Combined sources19
Beta strandi173 – 178Combined sources6
Helixi182 – 188Combined sources7
Helixi191 – 197Combined sources7
Beta strandi199 – 203Combined sources5
Beta strandi213 – 215Combined sources3
Beta strandi233 – 236Combined sources4
Helixi237 – 246Combined sources10
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 – 311Combined sources5
Turni312 – 315Combined sources4
Beta strandi316 – 321Combined sources6
Beta strandi324 – 327Combined sources4
Helixi331 – 343Combined sources13
Beta strandi347 – 352Combined sources6
Helixi354 – 356Combined sources3
Beta strandi359 – 361Combined sources3
Beta strandi363 – 366Combined sources4
Helixi371 – 380Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1TFVX-ray2.90A22-381[»]
2O9OX-ray2.80A22-381[»]
2QF8X-ray2.80A22-381[»]
4MAVX-ray2.79A22-381[»]
4ML4X-ray2.50A22-381[»]
4MPKX-ray2.65A22-381[»]
4MTVX-ray2.80A22-381[»]
4NSBX-ray3.05A22-381[»]
4Q7NX-ray1.79A22-381[»]
4S06X-ray1.49A22-381[»]
4S19X-ray1.65A22-381[»]
SMRiQ7YS85.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ7YS85.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni70 – 71Chitooligosaccharide bindingBy similarity2
Regioni97 – 100Chitooligosaccharide bindingBy similarity4
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

HOVERGENiHBG011684.
OrthoDBiEOG091G014W.

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.

Q7YS85-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGLRVAQTGF VVLVLLQSCA AYKLICYYTS WSQYREGDGS CFPDAIDPFL
60 70 80 90 100
CTHVIYSFAN ISNNEIDTWE WNDVTLYDTL NTLKNRNPKL KTLLSVGGWN
110 120 130 140 150
FGSQRFSKIA SKTQSRRTFI KSVPPFLRTH GFDGLDLAWL YPGWRDKRHL
160 170 180 190 200
TTLVKEMKAE FVREAQAGTE QLLLSAAVPA GKIAIDRGYD IAQISRHLDF
210 220 230 240 250
ISLLTYDFHG AWRQTVGHHS PLFRGQEDAS SDRFSNADYA VSYMLRLGAP
260 270 280 290 300
ANKLVMGIPT FGKSYTLASS KTDVGAPISG PGIPGQFTKE KGILAYYEIC
310 320 330 340 350
DFLHGATTHR FRDQQVPYAT KGNQWVAYDD QESVKNKARY LKNRQLAGAM
360 370 380
VWALDLDDFR GTFCGQNLAF PLTNAIKDVL AGV
Length:383
Mass (Da):42,935
Last modified:May 14, 2014 - v3
Checksum:i8FE18A55F586AF4D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti89K → N in AAP42568 (Ref. 1) Curated1
Sequence conflicti101F → Y in AAP42568 (Ref. 1) Curated1
Sequence conflicti141Y → W in AAP42568 (Ref. 1) Curated1
Sequence conflicti179P → T in AAP42568 (Ref. 1) Curated1
Sequence conflicti226Q → N in AAP42568 (Ref. 1) Curated1
Sequence conflicti232Missing in AAP42568 (Ref. 1) Curated1
Sequence conflicti263K → R in AAP42568 (Ref. 1) Curated1
Sequence conflicti286Q → R in AAP42568 (Ref. 1) Curated1
Sequence conflicti290E → W in AAP42568 (Ref. 1) Curated1
Sequence conflicti369A → T in AAP42568 (Ref. 1) Curated1
Sequence conflicti374N → S in AAP42568 (Ref. 1) Curated1
Sequence conflicti382G → R in AAP42568 (Ref. 1) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY295929 mRNA. Translation: AAP42568.2.
JQ796280 mRNA. Translation: AFN52415.1.
RefSeqiNP_001277897.1. NM_001290968.1.

Genome annotation databases

GeneIDi102399197.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY295929 mRNA. Translation: AAP42568.2.
JQ796280 mRNA. Translation: AFN52415.1.
RefSeqiNP_001277897.1. NM_001290968.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1TFVX-ray2.90A22-381[»]
2O9OX-ray2.80A22-381[»]
2QF8X-ray2.80A22-381[»]
4MAVX-ray2.79A22-381[»]
4ML4X-ray2.50A22-381[»]
4MPKX-ray2.65A22-381[»]
4MTVX-ray2.80A22-381[»]
4NSBX-ray3.05A22-381[»]
4Q7NX-ray1.79A22-381[»]
4S06X-ray1.49A22-381[»]
4S19X-ray1.65A22-381[»]
SMRiQ7YS85.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH18. Glycoside Hydrolase Family 18.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi102399197.

Organism-specific databases

CTDi1116.

Phylogenomic databases

HOVERGENiHBG011684.
OrthoDBiEOG091G014W.

Miscellaneous databases

EvolutionaryTraceiQ7YS85.

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_BUBBU
AccessioniPrimary (citable) accession number: Q7YS85
Secondary accession number(s): I6YIV5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: May 14, 2014
Last modified: November 2, 2016
This is version 72 of the entry and version 3 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-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

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.