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P11218 (AGI_URTDI) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lectin/endochitinase 1

EC=3.2.1.14
Alternative name(s):
Agglutinin
UDA
chia5.1.1

Cleaved into the following chain:

  1. Lectin 1
Gene names
Name:UDA1
OrganismUrtica dioica (Great nettle) (Stinging nettle)
Taxonomic identifier3501 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsRosalesUrticaceaeUrtica

Protein attributes

Sequence length372 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Functions both as a chitinase and as a N-acetyl-D-glucosamine binding lectin. Inhibits the growth of several phytopathogenic chitin-containing fungi. Possesses also insecticidal activity and superantigenic properties. Ref.6

Catalytic activity

Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.

Subunit structure

Monomer and homodimer. Zinc favors dimerization. Active in the monomeric form but probably inactive in the dimeric form. The interaction with glycans on the mammalian TCR and MHC molecules of the T-cell and antigen-presenting cell, respectively, is inhibited by oligomers of GlcNAc. Ref.7

Tissue specificity

Rhizomes and inflorescence with immature seeds.

Post-translational modification

Proteolytically processed to yield a very small protein (8.5 kDa, 86 AA) containing only the two chitin-binding domains.

Sequence similarities

Contains 2 chitin-binding type-1 domains.

Mass spectrometry

Molecular mass is 9380 Da from positions 24 - 372. Determined by MALDI. Ref.3

Molecular mass is 9380.7±0.4 Da from positions 24 - 372. Determined by ESI. Ref.3

Binary interactions

With

Entry

#Exp.

IntAct

Notes

envQ757602EBI-8453649,EBI-8453491From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Ref.4 Ref.5
Chain24 – 372349Lectin/endochitinase 1
PRO_0000005266
Chain24 – 11289Lectin 1
PRO_0000005267

Regions

Domain24 – 6441Chitin-binding type-1 1
Domain69 – 11143Chitin-binding type-1 2
Region42 – 5312Substrate binding
Region113 – 12816Spacer
Region129 – 372244Chitinase

Sites

Metal binding701Zinc 1; shared with dimeric partner
Metal binding901Zinc 2; shared with dimeric partner
Binding site241Substrate; via amide nitrogen

Amino acid modifications

Modified residue241Pyrrolidone carboxylic acid
Glycosylation1231N-linked (GlcNAc...) Potential
Disulfide bond26 ↔ 41 Ref.6 Ref.7
Disulfide bond35 ↔ 47 Ref.6 Ref.7
Disulfide bond40 ↔ 54 Ref.6 Ref.7
Disulfide bond58 ↔ 62 Ref.6 Ref.7
Disulfide bond72 ↔ 87 Ref.6 Ref.7
Disulfide bond81 ↔ 93 Ref.6 Ref.7
Disulfide bond86 ↔ 100 Ref.6 Ref.7
Disulfide bond105 ↔ 109 Ref.6 Ref.7

Experimental info

Sequence conflict71S → A in AAD03614. Ref.3

Secondary structure

........................ 372
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P11218 [UniParc].

Last modified December 1, 1992. Version 3.
Checksum: 28E9A2312BF08FD2

FASTA37240,542
        10         20         30         40         50         60 
MMMRFLSAVV IMSSAMAVGL VSAQRCGSQG GGGTCPALWC CSIWGWCGDS EPYCGRTCEN 

        70         80         90        100        110        120 
KCWSGERSDH RCGAAVGNPP CGQDRCCSVH GWCGGGNDYC SGSKCQYRCS SSVRGPRVAL 

       130        140        150        160        170        180 
SGNSTANSIG NVVVTEPLFD QMFSHRKDCP SQGFYSYHSF LVAAESFPAF GTIGDVATRK 

       190        200        210        220        230        240 
REVAAFLAHI SQATSGERSD VENPHAWGLC HINTTTVTEN DFCTSSDWPC AAGKKYSPRG 

       250        260        270        280        290        300 
PIQLTHNFNY GLAGQAIGED LIQNPDLVEK DPIISFKTAL WFWMSQHDNK PSCHDIVLNA 

       310        320        330        340        350        360 
NSAANRIPNK GVIGNIISRA FGHDDFAVRS SSIGFYKRYC DMLGVSYGHD LKYWFDNTPS 

       370 
SEFQRIQMRV AA 

« Hide

References

[1]"The gene for stinging nettle lectin (Urtica dioica agglutinin) encodes both a lectin and a chitinase."
Lerner D.R., Raikhel N.V.
J. Biol. Chem. 267:11085-11091(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]Erratum
Lerner D.R., Raikhel N.V.
J. Biol. Chem. 267:22694-22694(1992) [PubMed] [Europe PMC] [Abstract]
[3]"Characterization of Urtica dioica agglutinin isolectins and the encoding gene family."
Does M.P., Ng D.K., Dekker H.L., Peumans W.J., Houterman P.M., Van Damme E.J., Cornelissen B.J.
Plant Mol. Biol. 39:335-347(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MASS SPECTROMETRY.
Strain: cv. Weerselo.
[4]"The primary structure of stinging nettle (Urtica dioica) agglutinin. A two-domain member of the hevein family."
Beintema J.J., Peumans W.J.
FEBS Lett. 299:131-134(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 24-112.
[5]"Extensive homologies between lectins from non-leguminous plants."
Chapot M.-P., Peumans W.J., Strosberg A.D.
FEBS Lett. 195:231-234(1986)
Cited for: PRELIMINARY PROTEIN SEQUENCE OF 24-54.
[6]"Crystal structure of Urtica dioica agglutinin, a superantigen presented by MHC molecules of class I and class II."
Saul F.A., Rovira P., Boulot G., van Damme E.J.M., Peumans W.J., Truffa-Bachi P., Bentley G.A.
Structure 8:593-603(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 24-112 IN COMPLEX WITH TRI-ACETYLCHITOTRIOSE AND TETRA-ACETYLCHITOTETRAOSE, FUNCTION, INTERACTION WITH HUMAN TCR AND MHC, DISULFIDE BONDS.
[7]"Structure of Urtica dioica agglutinin isolectin I: dimer formation mediated by two zinc ions bound at the sugar-binding site."
Harata K., Schubert W.-D., Muraki M.
Acta Crystallogr. D 57:1513-1517(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 24-112, SUBUNIT, ZINC BINDING, DISULFIDE BONDS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M87302 mRNA. Translation: AAA34219.1.
AF059535 Genomic DNA. Translation: AAD03614.1.
PIRA42778. A44298.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EN2X-ray1.40A25-112[»]
1ENMX-ray1.90A25-112[»]
1IQBX-ray1.90A/B25-112[»]
ProteinModelPortalP11218.
SMRP11218. Positions 24-112, 132-359.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP11218. 1 interaction.
MINTMINT-8414736.

Protein family/group databases

CAZyCBM18. Carbohydrate-Binding Module Family 18.
GH19. Glycoside Hydrolase Family 19.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.30.60.10. 2 hits.
InterProIPR001002. Chitin-bd_1.
IPR018371. Chitin-binding_1_CS.
IPR016283. Glyco_hydro_19.
IPR000726. Glyco_hydro_19_cat.
IPR023346. Lysozyme-like_dom.
[Graphical view]
PfamPF00187. Chitin_bind_1. 1 hit.
PF00182. Glyco_hydro_19. 1 hit.
[Graphical view]
PIRSFPIRSF001060. Endochitinase. 1 hit.
ProDomPD000609. Chitin_bd_1. 2 hits.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00270. ChtBD1. 2 hits.
[Graphical view]
SUPFAMSSF53955. SSF53955. 1 hit.
SSF57016. SSF57016. 2 hits.
PROSITEPS00026. CHIT_BIND_I_1. 2 hits.
PS50941. CHIT_BIND_I_2. 2 hits.
PS00773. CHITINASE_19_1. 1 hit.
PS00774. CHITINASE_19_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP11218.

Entry information

Entry nameAGI_URTDI
AccessionPrimary (citable) accession number: P11218
Secondary accession number(s): Q9SYR1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: December 1, 1992
Last modified: February 19, 2014
This is version 124 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries