Reviewed, UniProtKB/Swiss-Prot P11218 (AGI_URTDI)

Names and origin

Protein names

Recommended name:
    Lectin/endochitinase 1
    EC=3.2.1.14
Alternative name(s):
    Agglutinin
    UDA
    chia5.1.1
Cleaved into the following chain:
    1- Recommended name:
            Lectin 1

Gene names

Name:

UDA1

Organism

Urtica dioica (Great nettle) (Stinging nettle)

Taxonomic identifier

3501 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids I › Rosales › Urticaceae › Urtica

Protein attributes

Sequence length	372 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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

Ontologies

Keywords
Biological process	Carbohydrate metabolism Chitin degradation Plant defense Polysaccharide degradation
Domain	Repeat Signal
Ligand	Chitin-binding Lectin Metal-binding Zinc
Molecular function	Antimicrobial Fungicide Glycosidase Hydrolase
PTM	Disulfide bond Glycoprotein Pyrrolidone carboxylic acid
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	cell wall macromolecule catabolic process Inferred from electronic annotation. Source: InterPro chitin catabolic process Inferred from electronic annotation. Source: UniProtKB-KW defense response to fungus Inferred from electronic annotation. Source: UniProtKB-KW polysaccharide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW xenobiotic metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	chitin binding Inferred from electronic annotation. Source: UniProtKB-KW chitinase activity Inferred from electronic annotation. Source: EC sugar binding Inferred from electronic annotation. Source: UniProtKB-KW zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 23

23

Ref.4 Ref.5

Chain

24 – 372

349

Lectin/endochitinase 1

PRO_0000005266

Chain

24 – 112

89

Lectin 1

PRO_0000005267

Regions

Domain

24 – 64

41

Chitin-binding type-1 1

Domain

69 – 111

43

Chitin-binding type-1 2

Region

42 – 53

12

Substrate binding

Region

113 – 128

16

Spacer

Region

129 – 372

244

Chitinase

Sites

Metal binding

70

1

Zinc 1; shared with dimeric partner

Metal binding

90

1

Zinc 2; shared with dimeric partner

Binding site

24

1

Substrate; via amide nitrogen

Amino acid modifications

Modified residue

24

1

Pyrrolidone carboxylic acid

Glycosylation

123

1

N-linked (GlcNAc...) Potential

Disulfide bond

26 ↔ 41

Disulfide bond

35 ↔ 47

Disulfide bond

40 ↔ 54

Disulfide bond

58 ↔ 62

Disulfide bond

72 ↔ 87

Disulfide bond

81 ↔ 93

Disulfide bond

86 ↔ 100

Disulfide bond

105 ↔ 109

Experimental info

Sequence conflict

7

1

S → A in AAD03614. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

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.

.

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.

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.

.

.

.

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372

Helix Strand Turn

Details...

Helix

27 – 30

4

Helix

36 – 38

3

Beta strand

40 – 42

3

Beta strand

45 – 50

6

Helix

51 – 54

4

Beta strand

58 – 61

4

Helix

63 – 65

3

Helix

74 – 76

3

Beta strand

85 – 88

4

Beta strand

91 – 96

6

Helix

97 – 100

4

Helix

102 – 104

3

Beta strand

105 – 108

4

Sequences

	Sequence		Length	Mass (Da)
	P11218-1 [UniParc]. Last modified December 1, 1992. Version 3. Checksum: 28E9A2312BF08FD2	FASTA	372	40,542
	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

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: 1375935] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	Erratum Lerner D.R., Raikhel N.V. J. Biol. Chem. 267:22694-22694(1992) [PubMed: 1429618] [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: 10080699] [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: 1544484] [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: 10873861] [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, DISULFID 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: 11679714] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 24-112, SUBUNIT, ZINC BINDING, DISULFID BONDS.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M87302 mRNA. Translation: AAA34219.1.
AF059535 Genomic DNA. Translation: AAD03614.1.

PIR

A42778. A44298.

3D structure databases

PDBPDBe

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	25-112	[»]

ModBase

Search...

Protein family/group databases

CAZy

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

Enzyme and pathway databases

BRENDA

3.2.1.14. 280002.

Family and domain databases

InterPro

IPR018371. Chitin-binding_1_CS.
IPR001002. Chitin_bd_1.
IPR016283. Glyco_hydro_19.
IPR000726. Glyco_hydro_19_cat.
[Graphical view]

PANTHER

PTHR22595. Glyco_hydro_19_cat. 1 hit.

Pfam

PF00187. Chitin_bind_1. 2 hits.
PF00182. Glyco_hydro_19. 1 hit.
[Graphical view]

PIRSF

PIRSF001060. Endochitinase. 1 hit.

ProDom

PD000609. Chitin_binding_1. 2 hits.
PD354900. Glyco_hydro_19. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00270. ChtBD1. 2 hits.
[Graphical view]

PROSITE

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]

ProtoNet

Search...

Entry information

Entry name

AGI_URTDI

Accession

Primary (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:	June 16, 2009
This is version 100 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)