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P11218

- AGI_URTDI

UniProt

P11218 - AGI_URTDI

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Protein

Lectin/endochitinase 1

Gene
UDA1
Organism
Urtica dioica (Great nettle) (Stinging nettle)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei24 – 241Substrate; via amide nitrogen
Metal bindingi70 – 701Zinc 1; shared with dimeric partner
Metal bindingi90 – 901Zinc 2; shared with dimeric partner

GO - Molecular functioni

  1. chitinase activity Source: UniProtKB-EC
  2. chitin binding Source: UniProtKB-KW
  3. metal ion binding Source: UniProtKB-KW
  4. protein binding Source: IntAct

GO - Biological processi

  1. cell wall macromolecule catabolic process Source: InterPro
  2. chitin catabolic process Source: UniProtKB-KW
  3. defense response to fungus Source: UniProtKB-KW
  4. killing of cells of other organism Source: UniProtKB-KW
  5. polysaccharide catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Antimicrobial, Fungicide, Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Chitin degradation, Plant defense, Polysaccharide degradation

Keywords - Ligandi

Chitin-binding, Lectin, Metal-binding, Zinc

Protein family/group databases

CAZyiCBM18. Carbohydrate-Binding Module Family 18.
GH19. Glycoside Hydrolase Family 19.

Names & Taxonomyi

Protein namesi
Recommended name:
Lectin/endochitinase 1 (EC:3.2.1.14)
Alternative name(s):
Agglutinin
UDA
chia5.1.1
Cleaved into the following chain:
Gene namesi
Name:UDA1
OrganismiUrtica dioica (Great nettle) (Stinging nettle)
Taxonomic identifieri3501 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsRosalesUrticaceaeUrtica

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 23232 PublicationsAdd
BLAST
Chaini24 – 372349Lectin/endochitinase 1PRO_0000005266Add
BLAST
Chaini24 – 11289Lectin 1PRO_0000005267Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei24 – 241Pyrrolidone carboxylic acid
Disulfide bondi26 ↔ 412 Publications
Disulfide bondi35 ↔ 472 Publications
Disulfide bondi40 ↔ 542 Publications
Disulfide bondi58 ↔ 622 Publications
Disulfide bondi72 ↔ 872 Publications
Disulfide bondi81 ↔ 932 Publications
Disulfide bondi86 ↔ 1002 Publications
Disulfide bondi105 ↔ 1092 Publications
Glycosylationi123 – 1231N-linked (GlcNAc...) Reviewed prediction

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

Expressioni

Tissue specificityi

Rhizomes and inflorescence with immature seeds.

Interactioni

Subunit structurei

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.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
envQ757602EBI-8453649,EBI-8453491From a different organism.

Protein-protein interaction databases

IntActiP11218. 1 interaction.
MINTiMINT-8414736.

Structurei

Secondary structure

1
372
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi27 – 304
Helixi36 – 383
Beta strandi40 – 423
Beta strandi45 – 506
Helixi51 – 544
Beta strandi58 – 614
Helixi63 – 653
Helixi74 – 763
Beta strandi85 – 884
Beta strandi91 – 966
Helixi97 – 1004
Helixi102 – 1043
Beta strandi105 – 1084

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EN2X-ray1.40A25-112[»]
1ENMX-ray1.90A25-112[»]
1IQBX-ray1.90A/B24-112[»]
ProteinModelPortaliP11218.
SMRiP11218. Positions 24-112, 132-359.

Miscellaneous databases

EvolutionaryTraceiP11218.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini24 – 6441Chitin-binding type-1 1Add
BLAST
Domaini69 – 11143Chitin-binding type-1 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni42 – 5312Substrate bindingAdd
BLAST
Regioni113 – 12816SpacerAdd
BLAST
Regioni129 – 372244ChitinaseAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Repeat, Signal

Family and domain databases

Gene3Di3.30.60.10. 2 hits.
InterProiIPR001002. Chitin-bd_1.
IPR018371. Chitin-binding_1_CS.
IPR016283. Glyco_hydro_19.
IPR000726. Glyco_hydro_19_cat.
IPR023346. Lysozyme-like_dom.
[Graphical view]
PfamiPF00187. Chitin_bind_1. 1 hit.
PF00182. Glyco_hydro_19. 1 hit.
[Graphical view]
PIRSFiPIRSF001060. Endochitinase. 1 hit.
ProDomiPD000609. Chitin_bd_1. 2 hits.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00270. ChtBD1. 2 hits.
[Graphical view]
SUPFAMiSSF53955. SSF53955. 1 hit.
SSF57016. SSF57016. 2 hits.
PROSITEiPS00026. 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]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P11218-1 [UniParc]FASTAAdd to Basket

« Hide

MMMRFLSAVV IMSSAMAVGL VSAQRCGSQG GGGTCPALWC CSIWGWCGDS    50
EPYCGRTCEN KCWSGERSDH RCGAAVGNPP CGQDRCCSVH GWCGGGNDYC 100
SGSKCQYRCS SSVRGPRVAL SGNSTANSIG NVVVTEPLFD QMFSHRKDCP 150
SQGFYSYHSF LVAAESFPAF GTIGDVATRK REVAAFLAHI SQATSGERSD 200
VENPHAWGLC HINTTTVTEN DFCTSSDWPC AAGKKYSPRG PIQLTHNFNY 250
GLAGQAIGED LIQNPDLVEK DPIISFKTAL WFWMSQHDNK PSCHDIVLNA 300
NSAANRIPNK GVIGNIISRA FGHDDFAVRS SSIGFYKRYC DMLGVSYGHD 350
LKYWFDNTPS SEFQRIQMRV AA 372
Length:372
Mass (Da):40,542
Last modified:December 1, 1992 - v3
Checksum:i28E9A2312BF08FD2
GO

Mass spectrometryi

Molecular mass is 9380 Da from positions 24 - 372. Determined by MALDI. 1 Publication
Molecular mass is 9380.7±0.4 Da from positions 24 - 372. Determined by ESI. 1 Publication

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti7 – 71S → A in AAD03614. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M87302 mRNA. Translation: AAA34219.1.
AF059535 Genomic DNA. Translation: AAD03614.1.
PIRiA44298. A42778.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M87302 mRNA. Translation: AAA34219.1 .
AF059535 Genomic DNA. Translation: AAD03614.1 .
PIRi A44298. A42778.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1EN2 X-ray 1.40 A 25-112 [» ]
1ENM X-ray 1.90 A 25-112 [» ]
1IQB X-ray 1.90 A/B 24-112 [» ]
ProteinModelPortali P11218.
SMRi P11218. Positions 24-112, 132-359.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P11218. 1 interaction.
MINTi MINT-8414736.

Protein family/group databases

CAZyi CBM18. Carbohydrate-Binding Module Family 18.
GH19. Glycoside Hydrolase Family 19.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P11218.

Family and domain databases

Gene3Di 3.30.60.10. 2 hits.
InterProi IPR001002. Chitin-bd_1.
IPR018371. Chitin-binding_1_CS.
IPR016283. Glyco_hydro_19.
IPR000726. Glyco_hydro_19_cat.
IPR023346. Lysozyme-like_dom.
[Graphical view ]
Pfami PF00187. Chitin_bind_1. 1 hit.
PF00182. Glyco_hydro_19. 1 hit.
[Graphical view ]
PIRSFi PIRSF001060. Endochitinase. 1 hit.
ProDomi PD000609. Chitin_bd_1. 2 hits.
[Graphical view ] [Entries sharing at least one domain ]
SMARTi SM00270. ChtBD1. 2 hits.
[Graphical view ]
SUPFAMi SSF53955. SSF53955. 1 hit.
SSF57016. SSF57016. 2 hits.
PROSITEi PS00026. 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 ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiAGI_URTDI
AccessioniPrimary (citable) accession number: P11218
Secondary accession number(s): Q9SYR1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: December 1, 1992
Last modified: July 9, 2014
This is version 126 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

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

External Data

Dasty 3

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