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Reviewed, UniProtKB/Swiss-Prot P02876 (AGI2_WHEAT)

Last modified June 16, 2009. Version 89. 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

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Names and origin

Protein namesRecommended name:
    Agglutinin isolectin 2
Alternative name(s):
    WGA2
    Isolectin D
OrganismTriticum aestivum (Wheat)
Taxonomic identifier4565 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › BEP clade › Pooideae › Triticeae › Triticum

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Protein attributes

Sequence length213 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

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

Subunit structure

Homodimer, u-shaped.

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.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Ref.2
Chain28 – 198171Agglutinin isolectin 2
PRO_0000005257
Propeptide199 – 21315
PRO_0000005258

Regions

Domain28 – 6942Chitin-binding type-1 1
Domain70 – 11243Chitin-binding type-1 2
Domain113 – 15543Chitin-binding type-1 3
Domain156 – 19843Chitin-binding type-1 4
Region37 – 393Substrate binding By similarity
Region89 – 10012Substrate binding By similarity
Region141 – 1422Substrate binding

Amino acid modifications

Modified residue281Pyrrolidone carboxylic acid Ref.2
Disulfide bond30 ↔ 45 Ref.2
Disulfide bond39 ↔ 51 Ref.2
Disulfide bond44 ↔ 58 Ref.2
Disulfide bond62 ↔ 67 Ref.2
Disulfide bond73 ↔ 88 Ref.2
Disulfide bond82 ↔ 94 Ref.2
Disulfide bond87 ↔ 101 Ref.2
Disulfide bond105 ↔ 110 Ref.2
Disulfide bond116 ↔ 131 Ref.2
Disulfide bond125 ↔ 137 Ref.2
Disulfide bond130 ↔ 144 Ref.2
Disulfide bond148 ↔ 153 Ref.2
Disulfide bond159 ↔ 174 Ref.2
Disulfide bond168 ↔ 180 Ref.2
Disulfide bond173 ↔ 187 Ref.2
Disulfide bond191 ↔ 196 Ref.2

Experimental info

Sequence conflict641N → D AA sequence Ref.2

Secondary structure

1 ................................... 213
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P02876-1 [UniParc].

Last modified November 1, 1990. Version 3.
Checksum: F656A5C9277148AF

FASTA21321,356
        10         20         30         40         50         60 
MRKMMSTMAL TLGAAVFLAF AAATAQAQRC GEQGSNMECP NNLCCSQYGY CGMGGDYCGK 

        70         80         90        100        110        120 
GCQNGACWTS KRCGSQAGGA TCPNNHCCSQ YGHCGFGAEY CGAGCQGGPC RADIKCGSQS 

       130        140        150        160        170        180 
GGKLCPNNLC CSQWGFCGLG SEFCGGGCQS GACSTDKPCG KDAGGRVCTN NYCCSKWGSC 

       190        200        210 
GIGPGYCGAG CQSGGCDAVF AGAITANSTL LAE

« Hide

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References

[1]"Nucleotide sequences of cDNA clones encoding wheat germ agglutinin isolectins A and D."
Smith J.J., Raikhel N.V.
Plant Mol. Biol. 13:601-603(1989) [PubMed: 2491677] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Primary structure of wheat germ agglutinin isolectin 2. Peptide order deduced from X-ray structure."
Wright C.S., Gavilanes F., Peterson D.L.
Biochemistry 23:280-287(1984) [PubMed: 6546522] [Abstract]
Cited for: PROTEIN SEQUENCE OF 28-198.
Tissue: Germ.
[3]"Sequence variability in three wheat germ agglutinin isolectins: products of multiple genes in polyploid wheat."
Wright C.S., Raikhel N.V.
J. Mol. Evol. 28:327-336(1989) [PubMed: 2499688] [Abstract]
Cited for: SEQUENCE REVISION TO 68; 136; 161 AND 177.
[4]"The crystal structure of wheat germ agglutinin at 2.2-A resolution."
Wright C.S.
J. Mol. Biol. 111:439-457(1977) [PubMed: 871318] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[5]"Refinement of the crystal structure of wheat germ agglutinin isolectin 2 at 1.8-A resolution."
Wright C.S.
J. Mol. Biol. 194:501-529(1987) [PubMed: 3625772] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
[6]Erratum
Wright C.S.
J. Mol. Biol. 199:239-239(1988)

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Cross-references

Sequence databases

M25537 mRNA. Translation: AAA34258.1.
PIRAEWT2. S09624.
UniGeneTa.147

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2WGCX-ray2.20A/B29-198[»]
9WGAX-ray1.80A/B29-198[»]
ModBaseSearch...

Protein family/group databases

CAZyCBM18. Carbohydrate-Binding Module Family 18.

Organism-specific databases

GrameneP02876.

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...

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Entry information

Entry nameAGI2_WHEAT
AccessionPrimary (citable) accession number: P02876
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 1, 1990
Last modified: June 16, 2009
This is version 89 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

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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