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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei141 – 1411ChitooligosaccharideBy similarity
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):
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)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 21211 PublicationAdd
BLAST
Chaini22 – 383362Chitinase-3-like protein 1PRO_0000011967Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi26 ↔ 51
Glycosylationi60 – 601N-linked (GlcNAc...)1 Publication
Disulfide bondi300 ↔ 364

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ29411.

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

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
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 strandi233 – 2364Combined sources
Helixi237 – 24711Combined sources
Helixi251 – 2533Combined sources
Beta strandi254 – 27017Combined sources
Beta strandi277 – 2815Combined sources
Turni286 – 2883Combined sources
Beta strandi293 – 2953Combined sources
Helixi296 – 3038Combined sources
Beta strandi307 – 3115Combined sources
Turni312 – 3154Combined sources
Beta strandi316 – 3216Combined sources
Beta strandi324 – 3274Combined sources
Helixi331 – 34313Combined sources
Beta strandi347 – 3526Combined sources
Turni354 – 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
1XHGX-ray2.90A22-381[»]
1XRVX-ray2.10A22-381[»]
1ZB5X-ray2.45A22-381[»]
1ZBCX-ray2.29A22-381[»]
ProteinModelPortaliQ29411.
SMRiQ29411. Positions 22-383.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ29411.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni70 – 712Chitooligosaccharide bindingBy similarity
Regioni97 – 1004Chitooligosaccharide bindingBy similarity
Regioni204 – 2074Chitooligosaccharide bindingBy similarity
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

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti69 – 691W → L in AAA86482 (PubMed:7768902).Curated
Sequence conflicti69 – 691W → L in CAA87764 (PubMed:7768902).Curated
Sequence conflicti112 – 1121K → N in AAA86482 (PubMed:7768902).Curated
Sequence conflicti112 – 1121K → N in CAA87764 (PubMed:7768902).Curated
Sequence conflicti140 – 1412LY → IS in AAA86482 (PubMed:7768902).Curated
Sequence conflicti140 – 1412LY → IS in CAA87764 (PubMed:7768902).Curated
Sequence conflicti162 – 1621I → V in AAA86482 (PubMed:7768902).Curated
Sequence conflicti162 – 1621I → V in CAA87764 (PubMed:7768902).Curated
Sequence conflicti166 – 1672QA → LP in AAA86482 (PubMed:7768902).Curated
Sequence conflicti166 – 1672QA → LP in CAA87764 (PubMed:7768902).Curated
Sequence conflicti171 – 1711Q → R in AAA86482 (PubMed:7768902).Curated
Sequence conflicti171 – 1711Q → R in CAA87764 (PubMed:7768902).Curated
Sequence conflicti176 – 1761A → G in AAA86482 (PubMed:7768902).Curated
Sequence conflicti176 – 1761A → G in CAA87764 (PubMed:7768902).Curated
Sequence conflicti227 – 2271E → G in AAA86482 (PubMed:7768902).Curated
Sequence conflicti227 – 2271E → G in CAA87764 (PubMed:7768902).Curated
Sequence conflicti278 – 2781V → A in AAA86482 (PubMed:7768902).Curated
Sequence conflicti278 – 2781V → A in CAA87764 (PubMed:7768902).Curated
Sequence conflicti308 – 3136THRFRD → VRRPLG in AAA86482 (PubMed:7768902).Curated
Sequence conflicti353 – 3531A → T in AAA86482 (PubMed:7768902).Curated
Sequence conflicti353 – 3531A → T in CAA87764 (PubMed:7768902).Curated

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1XHGX-ray2.90A22-381[»]
1XRVX-ray2.10A22-381[»]
1ZB5X-ray2.45A22-381[»]
1ZBCX-ray2.29A22-381[»]
ProteinModelPortaliQ29411.
SMRiQ29411. Positions 22-383.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000016408.

Protein family/group databases

CAZyiGH18. Glycoside Hydrolase Family 18.

Proteomic databases

PaxDbiQ29411.

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: February 17, 2016
This is version 107 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.