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
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)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):
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)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 21211 PublicationAdd
BLAST
Chaini22 – 383362Chitinase-3-like protein 1PRO_0000042787Add
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

Post-translational modificationi

Glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP30922.
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

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 – 1797Combined sources
Helixi182 – 1887Combined sources
Helixi191 – 1955Combined sources
Beta strandi199 – 2046Combined sources
Beta strandi211 – 2155Combined 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 – 38212Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OWQX-ray2.00A22-383[»]
2ESCX-ray2.10A22-383[»]
ProteinModelPortaliP30922.
SMRiP30922. Positions 22-383.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP30922.

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.
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 AAX46682.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti25 – 251I → V in AAB64304 (Ref. 4) Curated
Sequence conflicti104 – 1041Q → E in AAP41220 (Ref. 2) Curated
Sequence conflicti164 – 1641E → G in AAB64304 (Ref. 4) Curated
Sequence conflicti179 – 1791P → T in AAP41220 (Ref. 2) Curated
Sequence conflicti211 – 2111A → G in AAP41220 (Ref. 2) Curated
Sequence conflicti214 – 2141Q → G in AAP41220 (Ref. 2) Curated
Sequence conflicti226 – 2327QEDASSD → NSDGSS in AAP41220 (Ref. 2) Curated
Sequence conflicti271 – 2733KTD → STR in AAP41220 (Ref. 2) Curated
Sequence conflicti307 – 3071T → I in AAX46682 (PubMed:16305752).Curated
Sequence conflicti369 – 3691T → A in AAX46682 (PubMed:16305752).Curated
Sequence conflicti382 – 3821R → E in AAX46682 (PubMed:16305752).Curated

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1OWQX-ray2.00A22-383[»]
2ESCX-ray2.10A22-383[»]
ProteinModelPortaliP30922.
SMRiP30922. Positions 22-383.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000024253.

Protein family/group databases

CAZyiGH18. Glycoside Hydrolase Family 18.

Proteomic databases

PaxDbiP30922.
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.
NextBioi20806518.

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

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  2. "Signal processing protein from bovine mammary gland."
    Srinivasan A., Kumar J., Singh T.P.
    Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 22-383.
    Tissue: Mammary gland.
  3. "Isolation and characterization of a novel 39 kilodalton whey protein from bovine mammary secretions collected during the nonlactating period."
    Rejman J.J., Hurley W.L.
    Biochem. Biophys. Res. Commun. 150:329-334(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 22-57.
  4. "Expression of chitinase-like protein 1 (CLP-1) in bovine chondrocytes."
    Recklies A.D., White C.
    Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 25-356.
  5. "Structure of a bovine secretory signalling glycoprotein (SPC-40) at 2.1 Angstrom resolution."
    Kumar J., Ethayathulla A.S., Srivastava D.B., Sharma S., Singh S.B., Srinivasan A., Yadav M.P., Singh T.P.
    Acta Crystallogr. D 62:953-963(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 22-383, FUNCTION, GLYCOSYLATION AT ASN-60, DISULFIDE BONDS.

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: February 17, 2016
This is version 125 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.