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Protein

Chitinase-3-like protein 1

Gene

CHI3L1

Organism
Bos taurus (Bovine)
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 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):
39 kDa whey protein
Cartilage glycoprotein 39
Short name:
CGP-39
Short name:
GP-39
Chitinase-like protein 1
Short name:
CLP-1
SPC-40
Signal-processing protein
Gene namesi
Name:CHI3L1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 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_000004278722 – 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
Glycosylationi367N-linked (GlcNAc...)Sequence analysis1

Post-translational modificationi

Glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP30922.
PeptideAtlasiP30922.
PRIDEiP30922.

Expressioni

Tissue specificityi

Mammary secretions collected during the non-lactating period.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000024253.

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 – 179Combined sources7
Helixi182 – 188Combined sources7
Helixi191 – 195Combined sources5
Beta strandi199 – 204Combined sources6
Beta strandi211 – 215Combined sources5
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 – 382Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1OWQX-ray2.00A22-383[»]
2ESCX-ray2.10A22-383[»]
ProteinModelPortaliP30922.
SMRiP30922.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP30922.

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.
InParanoidiP30922.
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.

P30922-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGLRAAHTGF VVLVLLQSCA AYKLICYYTS WSQYREGDGS CFPDAIDPFL
60 70 80 90 100
CTHVIYSFAN ISNNEIDTWE WNDVTLYDTL NTLKNRNPNL 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 FGRSYTLASS KTDVGAPISG PGIPGQFTKE KGILAYYEIC
310 320 330 340 350
DFLHGATTHR FRDQQVPYAT KGNQWVAYDD QESVKNKARY LKNRQLAGAM
360 370 380
VWALDLDDFR GTFCGQNLTF PLTSAIKDVL ARV
Length:383
Mass (Da):43,032
Last modified:November 8, 2005 - v3
Checksum:i391561804C371A10
GO

Sequence cautioni

The sequence AAX46682 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti25I → V in AAB64304 (Ref. 4) Curated1
Sequence conflicti104Q → E in AAP41220 (Ref. 2) Curated1
Sequence conflicti164E → G in AAB64304 (Ref. 4) Curated1
Sequence conflicti179P → T in AAP41220 (Ref. 2) Curated1
Sequence conflicti211A → G in AAP41220 (Ref. 2) Curated1
Sequence conflicti214Q → G in AAP41220 (Ref. 2) Curated1
Sequence conflicti226 – 232QEDASSD → NSDGSS in AAP41220 (Ref. 2) Curated7
Sequence conflicti271 – 273KTD → STR in AAP41220 (Ref. 2) Curated3
Sequence conflicti307T → I in AAX46682 (PubMed:16305752).Curated1
Sequence conflicti369T → A in AAX46682 (PubMed:16305752).Curated1
Sequence conflicti382R → E in AAX46682 (PubMed:16305752).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT021835 mRNA. Translation: AAX46682.1. Different initiation.
AY291312 mRNA. Translation: AAP41220.2.
AF011373 mRNA. Translation: AAB64304.1.
PIRiA27682.
RefSeqiNP_001073688.1. NM_001080219.1.
UniGeneiBt.60417.

Genome annotation databases

GeneIDi286869.
KEGGibta:286869.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT021835 mRNA. Translation: AAX46682.1. Different initiation.
AY291312 mRNA. Translation: AAP41220.2.
AF011373 mRNA. Translation: AAB64304.1.
PIRiA27682.
RefSeqiNP_001073688.1. NM_001080219.1.
UniGeneiBt.60417.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1OWQX-ray2.00A22-383[»]
2ESCX-ray2.10A22-383[»]
ProteinModelPortaliP30922.
SMRiP30922.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000024253.

Protein family/group databases

CAZyiGH18. Glycoside Hydrolase Family 18.

Proteomic databases

PaxDbiP30922.
PeptideAtlasiP30922.
PRIDEiP30922.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi286869.
KEGGibta:286869.

Organism-specific databases

CTDi1116.

Phylogenomic databases

eggNOGiKOG2806. Eukaryota.
COG3325. LUCA.
HOGENOMiHOG000111109.
HOVERGENiHBG011684.
InParanoidiP30922.
KOiK17523.

Miscellaneous databases

EvolutionaryTraceiP30922.

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_BOVIN
AccessioniPrimary (citable) accession number: P30922
Secondary accession number(s): O18949, Q58CW2, Q7YSE8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: November 8, 2005
Last modified: November 2, 2016
This is version 129 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, 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.