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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei263 – 2631ChitooligosaccharideBy similarity
Binding sitei352 – 3521ChitooligosaccharideBy similarity

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)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Add
BLAST
Chaini22 – 383362Chitinase-3-like protein 1PRO_0000077054Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi26 ↔ 511 Publication
Glycosylationi60 – 601N-linked (GlcNAc...)1 Publication
Disulfide bondi300 ↔ 3641 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Expressioni

Tissue specificityi

Detected in mammary gland.

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1
383
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi23 – 297Combined sources
Helixi30 – 345Combined sources
Helixi37 – 393Combined sources
Helixi43 – 453Combined sources
Turni48 – 503Combined sources
Beta strandi52 – 6211Combined sources
Beta strandi65 – 673Combined sources
Beta strandi70 – 723Combined sources
Helixi73 – 8210Combined sources
Helixi83 – 853Combined sources
Beta strandi91 – 977Combined sources
Beta strandi99 – 1013Combined sources
Helixi103 – 1108Combined sources
Helixi113 – 13018Combined sources
Beta strandi133 – 1386Combined sources
Turni144 – 1463Combined sources
Helixi147 – 16519Combined sources
Beta strandi173 – 1786Combined sources
Helixi182 – 1887Combined sources
Helixi191 – 1977Combined sources
Beta strandi199 – 2035Combined sources
Beta strandi213 – 2153Combined sources
Beta strandi233 – 2364Combined sources
Helixi237 – 24610Combined sources
Helixi251 – 2533Combined sources
Beta strandi254 – 27017Combined sources
Beta strandi277 – 2815Combined sources
Turni286 – 2883Combined sources
Beta strandi293 – 2953Combined sources
Helixi296 – 3027Combined sources
Turni303 – 3053Combined sources
Beta strandi307 – 3115Combined sources
Turni312 – 3154Combined sources
Beta strandi316 – 3216Combined sources
Beta strandi324 – 3274Combined sources
Helixi331 – 34313Combined sources
Beta strandi347 – 3526Combined sources
Helixi354 – 3563Combined sources
Beta strandi359 – 3613Combined sources
Beta strandi363 – 3664Combined sources
Helixi371 – 38010Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ7YS85.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni70 – 712Chitooligosaccharide bindingBy similarity
Regioni97 – 1004Chitooligosaccharide bindingBy similarity
Regioni204 – 2074Chitooligosaccharide binding
Regioni324 – 33815Important for AKT1 activation and IL8 productionBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the glycosyl hydrolase 18 family.Curated

Keywords - Domaini

Signal

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.

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti89 – 891K → N in AAP42568 (Ref. 1) Curated
Sequence conflicti101 – 1011F → Y in AAP42568 (Ref. 1) Curated
Sequence conflicti141 – 1411Y → W in AAP42568 (Ref. 1) Curated
Sequence conflicti179 – 1791P → T in AAP42568 (Ref. 1) Curated
Sequence conflicti226 – 2261Q → N in AAP42568 (Ref. 1) Curated
Sequence conflicti232 – 2321Missing in AAP42568 (Ref. 1) Curated
Sequence conflicti263 – 2631K → R in AAP42568 (Ref. 1) Curated
Sequence conflicti286 – 2861Q → R in AAP42568 (Ref. 1) Curated
Sequence conflicti290 – 2901E → W in AAP42568 (Ref. 1) Curated
Sequence conflicti369 – 3691A → T in AAP42568 (Ref. 1) Curated
Sequence conflicti374 – 3741N → S in AAP42568 (Ref. 1) Curated
Sequence conflicti382 – 3821G → R in AAP42568 (Ref. 1) Curated

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
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[»]
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.

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...

Publicationsi

  1. "Buffalo mammary gland protein."
    Bilgrami S., Saravanan K., Yadav S., Kaur P., Srinivasan A., Singh T.P.
    Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Mammary gland.
  2. Singh S., Anand V., Jena M.K., Jamwal M., Kumar S., Dang A.K., Malakar D., Mohanty T.K., Kaushik J.K., Mohanty A.K.
    Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Mammary gland.
  3. Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 22-383, GLYCOSYLATION AT ASN-60, DISULFIDE BONDS.

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 11, 2015
This is version 70 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.