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Protein

Chitinase-3-like protein 1

Gene

CHI3L1

Organism
Sus scrofa (Pig)
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). Stimulates migration and adhesion of cultured vascular smooth muscle cells.By similarity1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei141ChitooligosaccharideBy similarity1
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):
38 kDa heparin-binding glycoprotein
Signal-processing protein
gp38k
Gene namesi
Name:CHI3L1
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 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
Signal peptidei1 – 211 PublicationAdd BLAST21
ChainiPRO_000001196722 – 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

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ29411.
PRIDEiQ29411.

Expressioni

Tissue specificityi

Detected in smooth muscle cells in atherosclerotic plaques. Detected in regions of vascular occlusion in the aorta.2 Publications

Inductioni

Up-regulated in cultured aortic smooth muscle cells upon transition to a nodular, multilayered culture.1 Publication

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000016408.

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 – 81Combined sources9
Helixi82 – 85Combined sources4
Beta strandi91 – 97Combined sources7
Helixi103 – 111Combined sources9
Helixi113 – 130Combined sources18
Beta strandi133 – 138Combined sources6
Turni144 – 146Combined sources3
Helixi147 – 164Combined sources18
Helixi165 – 167Combined sources3
Beta strandi173 – 178Combined sources6
Helixi182 – 188Combined sources7
Helixi191 – 195Combined sources5
Beta strandi199 – 203Combined sources5
Beta strandi213 – 215Combined 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 – 303Combined sources8
Beta strandi307 – 311Combined sources5
Turni312 – 315Combined sources4
Beta strandi316 – 321Combined sources6
Beta strandi324 – 327Combined sources4
Helixi331 – 343Combined sources13
Beta strandi347 – 352Combined sources6
Turni354 – 356Combined sources3
Beta strandi359 – 361Combined sources3
Beta strandi363 – 367Combined sources5
Helixi371 – 381Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1XHGX-ray2.90A22-381[»]
1XRVX-ray2.10A22-381[»]
1ZB5X-ray2.45A22-381[»]
1ZBCX-ray2.29A22-381[»]
ProteinModelPortaliQ29411.
SMRiQ29411.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ29411.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni70 – 71Chitooligosaccharide bindingBy similarity2
Regioni97 – 100Chitooligosaccharide bindingBy similarity4
Regioni204 – 207Chitooligosaccharide bindingBy similarity4
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.
HOGENOMiHOG000111109.
HOVERGENiHBG011684.
InParanoidiQ29411.
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.

Q29411-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGLRVAQTGF VALVLLQSCA AYKLVCYYTS WSQYREGDGS CFPDAIDPFL
60 70 80 90 100
CTHIIYSFAN ISNNEIDTWE WNDVTLYDTL NTLKNRNPNL KTLLSVGGWN
110 120 130 140 150
FGSQRFSKIA SKTQSRRTFI KSVPPFLRTH GFDGLDLAWL YPGRRDKRHL
160 170 180 190 200
TTLVKEMKAE FIREAQAGTE QLLLSAAVSA GKVAIDRGYD IAQISQHLDF
210 220 230 240 250
ISLLTYDFHG AWRQTTGHHS PLFRGQEDAS SDRFSNADYA VSYVLRLGAP
260 270 280 290 300
ANKLVMGIPT FGRSFTLASS KTDVGAPVSG PGIPGRFTKE KGILAYYEIC
310 320 330 340 350
DFLQGATTHR FRDQQVPYAT KGNQWVGYDD QESVKNKAKY LKSRQLAGAM
360 370 380
VWALDLDDFR GNFCGQNLRF PLTSAIKDVL AAA
Length:383
Mass (Da):42,800
Last modified:November 8, 2005 - v2
Checksum:iFC6F637E1FD8886E
GO

Sequence cautioni

The sequence AAV30548 differs from that shown. Sequencing errors.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti69W → L in AAA86482 (PubMed:7768902).Curated1
Sequence conflicti69W → L in CAA87764 (PubMed:7768902).Curated1
Sequence conflicti112K → N in AAA86482 (PubMed:7768902).Curated1
Sequence conflicti112K → N in CAA87764 (PubMed:7768902).Curated1
Sequence conflicti140 – 141LY → IS in AAA86482 (PubMed:7768902).Curated2
Sequence conflicti140 – 141LY → IS in CAA87764 (PubMed:7768902).Curated2
Sequence conflicti162I → V in AAA86482 (PubMed:7768902).Curated1
Sequence conflicti162I → V in CAA87764 (PubMed:7768902).Curated1
Sequence conflicti166 – 167QA → LP in AAA86482 (PubMed:7768902).Curated2
Sequence conflicti166 – 167QA → LP in CAA87764 (PubMed:7768902).Curated2
Sequence conflicti171Q → R in AAA86482 (PubMed:7768902).Curated1
Sequence conflicti171Q → R in CAA87764 (PubMed:7768902).Curated1
Sequence conflicti176A → G in AAA86482 (PubMed:7768902).Curated1
Sequence conflicti176A → G in CAA87764 (PubMed:7768902).Curated1
Sequence conflicti227E → G in AAA86482 (PubMed:7768902).Curated1
Sequence conflicti227E → G in CAA87764 (PubMed:7768902).Curated1
Sequence conflicti278V → A in AAA86482 (PubMed:7768902).Curated1
Sequence conflicti278V → A in CAA87764 (PubMed:7768902).Curated1
Sequence conflicti308 – 313THRFRD → VRRPLG in AAA86482 (PubMed:7768902).Curated6
Sequence conflicti353A → T in AAA86482 (PubMed:7768902).Curated1
Sequence conflicti353A → T in CAA87764 (PubMed:7768902).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U19900 mRNA. Translation: AAA86482.1.
Z47803 mRNA. Translation: CAA87764.1.
AY762599 mRNA. Translation: AAV30548.1. Sequence problems.
PIRiS51327.
RefSeqiNP_001001540.1. NM_001001540.1.
UniGeneiSsc.90.

Genome annotation databases

GeneIDi396865.
KEGGissc:396865.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U19900 mRNA. Translation: AAA86482.1.
Z47803 mRNA. Translation: CAA87764.1.
AY762599 mRNA. Translation: AAV30548.1. Sequence problems.
PIRiS51327.
RefSeqiNP_001001540.1. NM_001001540.1.
UniGeneiSsc.90.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1XHGX-ray2.90A22-381[»]
1XRVX-ray2.10A22-381[»]
1ZB5X-ray2.45A22-381[»]
1ZBCX-ray2.29A22-381[»]
ProteinModelPortaliQ29411.
SMRiQ29411.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000016408.

Protein family/group databases

CAZyiGH18. Glycoside Hydrolase Family 18.

Proteomic databases

PaxDbiQ29411.
PRIDEiQ29411.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi396865.
KEGGissc:396865.

Organism-specific databases

CTDi1116.

Phylogenomic databases

eggNOGiKOG2806. Eukaryota.
COG3325. LUCA.
HOGENOMiHOG000111109.
HOVERGENiHBG011684.
InParanoidiQ29411.
KOiK17523.

Miscellaneous databases

EvolutionaryTraceiQ29411.

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_PIG
AccessioniPrimary (citable) accession number: Q29411
Secondary accession number(s): Q5UC99
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: November 8, 2005
Last modified: November 2, 2016
This is version 109 of the entry and version 2 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, 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.