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Protein

Lectin/endochitinase 1

Gene

UDA1

Organism
Urtica dioica (Great nettle) (Stinging nettle)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Binding sitei24Substrate; via amide nitrogen1
Metal bindingi70Zinc 1; shared with dimeric partner1
Metal bindingi90Zinc 2; shared with dimeric partner1

GO - Molecular functioni

GO - Biological processi

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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 231 PublicationAdd BLAST23
ChainiPRO_000000526624 – 372Lectin/endochitinase 1Add BLAST349
ChainiPRO_000000526724 – 112Lectin 1Add BLAST89

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei24Pyrrolidone carboxylic acid1
Disulfide bondi26 ↔ 41
Disulfide bondi35 ↔ 47
Disulfide bondi40 ↔ 54
Disulfide bondi58 ↔ 62
Disulfide bondi72 ↔ 87
Disulfide bondi81 ↔ 93
Disulfide bondi86 ↔ 100
Disulfide bondi105 ↔ 109
Glycosylationi123N-linked (GlcNAc...)Sequence analysis1

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.2 Publications

Binary interactionsi

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

Protein-protein interaction databases

IntActiP11218. 1 interactor.
MINTiMINT-8414736.

Structurei

Secondary structure

1372
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi27 – 30Combined sources4
Helixi36 – 38Combined sources3
Beta strandi40 – 42Combined sources3
Beta strandi45 – 50Combined sources6
Helixi51 – 54Combined sources4
Beta strandi58 – 61Combined sources4
Helixi63 – 65Combined sources3
Helixi74 – 76Combined sources3
Beta strandi85 – 88Combined sources4
Beta strandi91 – 96Combined sources6
Helixi97 – 100Combined sources4
Helixi102 – 104Combined sources3
Beta strandi105 – 108Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EN2X-ray1.40A25-112[»]
1ENMX-ray1.90A25-112[»]
1IQBX-ray1.90A/B24-112[»]
ProteinModelPortaliP11218.
SMRiP11218.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11218.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini24 – 64Chitin-binding type-1 1PROSITE-ProRule annotationAdd BLAST41
Domaini69 – 111Chitin-binding type-1 2PROSITE-ProRule annotationAdd BLAST43

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni42 – 53Substrate bindingAdd BLAST12
Regioni113 – 128SpacerAdd BLAST16
Regioni129 – 372ChitinaseAdd BLAST244

Sequence similaritiesi

Contains 2 chitin-binding type-1 domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Family and domain databases

CDDicd00325. chitinase_glyco_hydro_19. 1 hit.
Gene3Di3.30.60.10. 2 hits.
InterProiIPR001002. Chitin-bd_1.
IPR018371. Chitin-binding_1_CS.
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]
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

        10         20         30         40         50
MMMRFLSAVV IMSSAMAVGL VSAQRCGSQG GGGTCPALWC CSIWGWCGDS
60 70 80 90 100
EPYCGRTCEN KCWSGERSDH RCGAAVGNPP CGQDRCCSVH GWCGGGNDYC
110 120 130 140 150
SGSKCQYRCS SSVRGPRVAL SGNSTANSIG NVVVTEPLFD QMFSHRKDCP
160 170 180 190 200
SQGFYSYHSF LVAAESFPAF GTIGDVATRK REVAAFLAHI SQATSGERSD
210 220 230 240 250
VENPHAWGLC HINTTTVTEN DFCTSSDWPC AAGKKYSPRG PIQLTHNFNY
260 270 280 290 300
GLAGQAIGED LIQNPDLVEK DPIISFKTAL WFWMSQHDNK PSCHDIVLNA
310 320 330 340 350
NSAANRIPNK GVIGNIISRA FGHDDFAVRS SSIGFYKRYC DMLGVSYGHD
360 370
LKYWFDNTPS SEFQRIQMRV AA
Length:372
Mass (Da):40,542
Last modified:December 1, 1992 - v3
Checksum:i28E9A2312BF08FD2
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti7S → A in AAD03614 (PubMed:10080699).Curated1

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 databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M87302 mRNA. Translation: AAA34219.1.
AF059535 Genomic DNA. Translation: AAD03614.1.
PIRiA44298. A42778.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M87302 mRNA. Translation: AAA34219.1.
AF059535 Genomic DNA. Translation: AAD03614.1.
PIRiA44298. A42778.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EN2X-ray1.40A25-112[»]
1ENMX-ray1.90A25-112[»]
1IQBX-ray1.90A/B24-112[»]
ProteinModelPortaliP11218.
SMRiP11218.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP11218. 1 interactor.
MINTiMINT-8414736.

Protein family/group databases

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

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP11218.

Family and domain databases

CDDicd00325. chitinase_glyco_hydro_19. 1 hit.
Gene3Di3.30.60.10. 2 hits.
InterProiIPR001002. Chitin-bd_1.
IPR018371. Chitin-binding_1_CS.
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]
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]
ProtoNetiSearch...

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: November 2, 2016
This is version 135 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

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.