Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Chitinase-3-like protein 1

Gene

CHI3L1

Organism
Capra hircus (Goat)
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 sitei141 – 1411Chitooligosaccharide
Binding sitei263 – 2631Chitooligosaccharide
Binding sitei352 – 3521Chitooligosaccharide

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):
BP40
Mammary gland protein 40
Short name:
MGP-40
Gene namesi
Name:CHI3L1
OrganismiCapra hircus (Goat)
Taxonomic identifieri9925 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeCaprinaeCapra

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 – 21211 PublicationAdd
BLAST
Chaini22 – 383362Chitinase-3-like protein 1PRO_0000011964Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi26 ↔ 511 Publication
Glycosylationi60 – 601N-linked (GlcNAc...)1 Publication
Disulfide bondi300 ↔ 3641 Publication
Glycosylationi367 – 3671N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Monomer.1 Publication

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
Helixi73 – 819Combined sources
Helixi82 – 854Combined sources
Beta strandi91 – 977Combined sources
Beta strandi99 – 1013Combined sources
Helixi103 – 1119Combined sources
Helixi113 – 13018Combined sources
Beta strandi133 – 1386Combined sources
Turni144 – 1463Combined sources
Helixi147 – 16418Combined sources
Helixi165 – 1673Combined sources
Beta strandi173 – 1786Combined sources
Helixi182 – 1887Combined sources
Helixi191 – 1955Combined sources
Beta strandi199 – 2035Combined sources
Beta strandi213 – 2153Combined sources
Beta strandi229 – 2313Combined sources
Beta strandi234 – 2363Combined sources
Helixi237 – 24711Combined 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 – 3675Combined sources
Helixi371 – 38111Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LJYX-ray2.90A22-383[»]
1SYTX-ray2.60A22-381[»]
1ZBVX-ray3.21A22-381[»]
1ZBWX-ray2.80A22-381[»]
1ZU8X-ray3.05A22-383[»]
2AOSX-ray2.90A22-381[»]
2B31X-ray3.10A22-381[»]
2DSZX-ray2.35A22-381[»]
2DT0X-ray2.45A22-381[»]
2DT1X-ray2.09A22-381[»]
2DT2X-ray2.90A22-381[»]
2DT3X-ray2.28A22-381[»]
2O92X-ray3.00A22-381[»]
2OLHX-ray2.78A22-381[»]
ProteinModelPortaliQ8SPQ0.
SMRiQ8SPQ0. Positions 22-381.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8SPQ0.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni70 – 712Chitooligosaccharide binding
Regioni97 – 1004Chitooligosaccharide binding
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.
KOiK17523.

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.

Q8SPQ0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGLRASGTGF VVLVLLQSCA AYKLICYYTS WSQYREGDGS CFPDAIDPFL
60 70 80 90 100
CTHIIYSFAN ISNNEIDTWE WNDVTLYDTL NTLKNRNPKL KTLLSVGGWN
110 120 130 140 150
FGPERFSKIA SKTQSRRTFI KSVPPFLRTH GFDGLDLAWL YPGRRDKRHL
160 170 180 190 200
TGLVKEMKAE FAREAQAGTE RLLLSAAVSA GKIAIDRGYD IAQISRHLDF
210 220 230 240 250
ISLLTYDFHG AWRQTVGHHS PLFRGQEDAS SDRFSNADYA VSYMLRLGAP
260 270 280 290 300
ANKLVMGIPT FGRSFTLASS KTDVGAPISG PGIPGRFTKE KGILAYYEIC
310 320 330 340 350
DFLHGATTHR FRDQQVPYAT KGNQWVAYDD QESVKNKARY LKNRQLAGAM
360 370 380
VWALDLDDFR GTFCGQNLTF PLTSAVKDVL AEV
Length:383
Mass (Da):42,894
Last modified:June 1, 2002 - v1
Checksum:i17655ED4BE4E9F5F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY081150 mRNA. Translation: AAL87007.1.
RefSeqiNP_001272618.1. NM_001285689.1.
UniGeneiChi.18273.

Genome annotation databases

GeneIDi100860825.
KEGGichx:100860825.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY081150 mRNA. Translation: AAL87007.1.
RefSeqiNP_001272618.1. NM_001285689.1.
UniGeneiChi.18273.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LJYX-ray2.90A22-383[»]
1SYTX-ray2.60A22-381[»]
1ZBVX-ray3.21A22-381[»]
1ZBWX-ray2.80A22-381[»]
1ZU8X-ray3.05A22-383[»]
2AOSX-ray2.90A22-381[»]
2B31X-ray3.10A22-381[»]
2DSZX-ray2.35A22-381[»]
2DT0X-ray2.45A22-381[»]
2DT1X-ray2.09A22-381[»]
2DT2X-ray2.90A22-381[»]
2DT3X-ray2.28A22-381[»]
2O92X-ray3.00A22-381[»]
2OLHX-ray2.78A22-381[»]
ProteinModelPortaliQ8SPQ0.
SMRiQ8SPQ0. Positions 22-381.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH18. Glycoside Hydrolase Family 18.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100860825.
KEGGichx:100860825.

Organism-specific databases

CTDi1116.

Phylogenomic databases

HOVERGENiHBG011684.
KOiK17523.

Miscellaneous databases

EvolutionaryTraceiQ8SPQ0.

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. "Crystal structure of a novel regulatory 40-kDa mammary gland protein (MGP-40) secreted during involution."
    Mohanty A.K., Singh G., Paramasivam M., Saravanan K., Jabeen T., Sharma S., Yadav S., Kaur P., Kumar P., Srinivasan A., Singh T.P.
    J. Biol. Chem. 278:14451-14460(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF N-TERMINUS, X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 22-383 IN COMPLEX WITH CHITIN OLIGOMERS.
    Tissue: Mammary gland.
  2. "Carbohydrate-binding properties of goat secretory glycoprotein (SPG-40) and its functional implications: structures of the native glycoprotein and its four complexes with chitin-like oligosaccharides."
    Kumar J., Ethayathulla A.S., Srivastava D.B., Singh N., Sharma S., Kaur P., Srinivasan A., Singh T.P.
    Acta Crystallogr. D 63:437-446(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS) OF 22-381 IN COMPLEXES WITH OLIGOSACCHARIDES, GLYCOSYLATION AT ASN-60, DISULFIDE BONDS.

Entry informationi

Entry nameiCH3L1_CAPHI
AccessioniPrimary (citable) accession number: Q8SPQ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: June 1, 2002
Last modified: November 11, 2015
This is version 80 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-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, Direct protein sequencing

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.