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Reviewed, UniProtKB/Swiss-Prot P10969 (AGI3_WHEAT)

Last modified June 16, 2009. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Agglutinin isolectin 3
Alternative name(s):
    WGA3
OrganismTriticum aestivum (Wheat)
Taxonomic identifier4565 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladePooideaeTriticeaeTriticum

Protein attributes

Sequence length186 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

N-acetyl-D-glucosamine / N-acetyl-D-neuraminic acid binding lectin.

Subunit structure

Homodimer, u-shaped. Ref.2

Miscellaneous

The 4 sites proposed for binding to carbohydrates (N-acetyl-D-glucosamine) of receptor molecules are on the surface of the agglutinin molecule.

Sequence similarities

Contains 4 chitin-binding type-1 domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 171171Agglutinin isolectin 3
PRO_0000005259
Propeptide172 – 18615
PRO_0000005260

Regions

Domain1 – 4242Chitin-binding type-1 1
Domain43 – 8543Chitin-binding type-1 2
Domain86 – 12843Chitin-binding type-1 3
Domain129 – 17143Chitin-binding type-1 4
Region10 – 123Substrate binding By similarity
Region62 – 7312Substrate binding
Region114 – 1152Substrate binding

Amino acid modifications

Modified residue11Pyrrolidone carboxylic acid
Glycosylation1801N-linked (GlcNAc...)
Disulfide bond3 ↔ 18
Disulfide bond12 ↔ 24
Disulfide bond17 ↔ 31
Disulfide bond35 ↔ 40
Disulfide bond46 ↔ 61
Disulfide bond55 ↔ 67
Disulfide bond60 ↔ 74
Disulfide bond78 ↔ 83
Disulfide bond89 ↔ 104
Disulfide bond98 ↔ 110
Disulfide bond103 ↔ 117
Disulfide bond121 ↔ 126
Disulfide bond132 ↔ 147
Disulfide bond141 ↔ 153
Disulfide bond146 ↔ 160
Disulfide bond164 ↔ 169

Experimental info

Non-terminal residue11

Secondary structure

................................. 186
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P10969-1 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: 68461A20339378FD

FASTA18618,756
        10         20         30         40         50         60 
QRCGEQGSGM ECPNNLCCSQ YGYCGMGGDY CGKGCQNGAC WTSKRCGSQA GGKTCPNNHC 

        70         80         90        100        110        120 
CSQYGHCGFG AEYCGAGCQG GPCRADIKCG SQAGGKLCPN NLCCSQWGYC GLGSEFCGEG 

       130        140        150        160        170        180 
CQNGACSTDK PCGKDAGGRV CTNNYCCSKW GSCGIGPGYC GAGCQSGGCD GVFAEAIATN 


STLLAE 

« Hide

References

[1]"Isolation and characterization of a cDNA clone encoding wheat germ agglutinin."
Raikhel N.V., Wilkins T.A.
Proc. Natl. Acad. Sci. U.S.A. 84:6745-6749(1987) [PubMed: 16578818] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"X-ray structure of wheat germ agglutinin isolectin 3."
Harata K., Nagahora H., Jigami Y.
Acta Crystallogr. D 51:1013-1019(1995) [PubMed: 15299769] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), SUBUNIT.
[3]"Interactions of wheat-germ agglutinin with GlcNAc beta 1,6Gal sequence."
Muraki M., Ishimura M., Harata K.
Biochim. Biophys. Acta 1569:10-20(2002) [PubMed: 11853952] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH SUBSTRATES.

Cross-references

Sequence databases

J02961 mRNA. Translation: AAA34257.1.
PIRA28401.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1K7TX-ray2.40A/B2-186[»]
1K7UX-ray2.20A/B2-186[»]
1K7VX-ray2.20A/B2-186[»]
1WGTX-ray1.90A/B2-186[»]
2UWZX-ray1.70A/B2-171[»]
ModBaseSearch...

Protein family/group databases

CAZyCBM18. Carbohydrate-Binding Module Family 18.

Organism-specific databases

GrameneP10969.

Family and domain databases

InterProIPR018371. Chitin-binding_1_CS.
IPR001002. Chitin_bd_1.
IPR000726. Glyco_hydro_19_cat.
[Graphical view]
Gene3DG3DSA:3.30.60.10. Chitin_bd_1. 4 hits.
PANTHERPTHR22595. Glyco_hydro_19_cat. 1 hit.
PfamPF00187. Chitin_bind_1. 4 hits.
[Graphical view]
PRINTSPR00451. CHITINBINDNG.
ProDomPD000609. Chitin_binding_1. 3 hits.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00270. ChtBD1. 4 hits.
[Graphical view]
PROSITEPS00026. CHIT_BIND_I_1. 4 hits.
PS50941. CHIT_BIND_I_2. 4 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAGI3_WHEAT
AccessionPrimary (citable) accession number: P10969
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: June 16, 2009
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents