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Protein

Agglutinin isolectin 2

Gene
N/A
Organism
Triticum aestivum (Wheat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

  1. carbohydrate binding Source: UniProtKB-KW
  2. chitin binding Source: UniProtKB-KW
Complete GO annotation...

Keywords - Ligandi

Chitin-binding, Lectin

Protein family/group databases

CAZyiCBM18. Carbohydrate-Binding Module Family 18.

Names & Taxonomyi

Protein namesi
Recommended name:
Agglutinin isolectin 2
Alternative name(s):
Isolectin D
WGA2
OrganismiTriticum aestivum (Wheat)
Taxonomic identifieri4565 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladePooideaeTriticeaeTriticum
ProteomesiUP000019116 Componenti: Unplaced

Organism-specific databases

GrameneiP02876.

Pathology & Biotechi

Protein family/group databases

Allergomei650. Tri a 18.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 27271 PublicationAdd
BLAST
Chaini28 – 198171Agglutinin isolectin 2PRO_0000005257Add
BLAST
Propeptidei199 – 21315PRO_0000005258Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei28 – 281Pyrrolidone carboxylic acid1 Publication
Disulfide bondi30 ↔ 45PROSITE-ProRule annotation1 Publication
Disulfide bondi39 ↔ 51PROSITE-ProRule annotation1 Publication
Disulfide bondi44 ↔ 58PROSITE-ProRule annotation1 Publication
Disulfide bondi62 ↔ 67PROSITE-ProRule annotation1 Publication
Disulfide bondi73 ↔ 88PROSITE-ProRule annotation1 Publication
Disulfide bondi82 ↔ 94PROSITE-ProRule annotation1 Publication
Disulfide bondi87 ↔ 101PROSITE-ProRule annotation1 Publication
Disulfide bondi105 ↔ 110PROSITE-ProRule annotation1 Publication
Disulfide bondi116 ↔ 131PROSITE-ProRule annotation1 Publication
Disulfide bondi125 ↔ 137PROSITE-ProRule annotation1 Publication
Disulfide bondi130 ↔ 144PROSITE-ProRule annotation1 Publication
Disulfide bondi148 ↔ 153PROSITE-ProRule annotation1 Publication
Disulfide bondi159 ↔ 174PROSITE-ProRule annotation1 Publication
Disulfide bondi168 ↔ 180PROSITE-ProRule annotation1 Publication
Disulfide bondi173 ↔ 187PROSITE-ProRule annotation1 Publication
Disulfide bondi191 ↔ 196PROSITE-ProRule annotation1 Publication

Keywords - PTMi

Disulfide bond, Pyrrolidone carboxylic acid

Interactioni

Subunit structurei

Homodimer, u-shaped.

Structurei

Secondary structure

1
213
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi31 – 344Combined sources
Helixi40 – 423Combined sources
Helixi55 – 584Combined sources
Beta strandi64 – 663Combined sources
Helixi74 – 774Combined sources
Helixi83 – 853Combined sources
Beta strandi92 – 954Combined sources
Helixi98 – 1014Combined sources
Beta strandi107 – 1093Combined sources
Helixi118 – 1203Combined sources
Helixi126 – 1283Combined sources
Beta strandi135 – 1384Combined sources
Helixi141 – 1444Combined sources
Beta strandi150 – 1523Combined sources
Helixi161 – 1633Combined sources
Helixi169 – 1713Combined sources
Beta strandi173 – 1753Combined sources
Turni176 – 1783Combined sources
Beta strandi179 – 1813Combined sources
Helixi184 – 1874Combined sources
Beta strandi193 – 1953Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2WGCX-ray2.20A/B29-198[»]
9WGAX-ray1.80A/B29-198[»]
ProteinModelPortaliP02876.
SMRiP02876. Positions 28-198.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02876.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini28 – 6942Chitin-binding type-1 1PROSITE-ProRule annotationAdd
BLAST
Domaini70 – 11243Chitin-binding type-1 2PROSITE-ProRule annotationAdd
BLAST
Domaini113 – 15543Chitin-binding type-1 3PROSITE-ProRule annotationAdd
BLAST
Domaini156 – 19843Chitin-binding type-1 4PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni37 – 393Substrate bindingBy similarity
Regioni89 – 10012Substrate bindingBy similarityAdd
BLAST
Regioni141 – 1422Substrate binding

Sequence similaritiesi

Contains 4 chitin-binding type-1 domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Family and domain databases

Gene3Di3.30.60.10. 4 hits.
InterProiIPR001002. Chitin-bd_1.
IPR018371. Chitin-binding_1_CS.
[Graphical view]
PfamiPF00187. Chitin_bind_1. 4 hits.
[Graphical view]
PRINTSiPR00451. CHITINBINDNG.
ProDomiPD000609. Chitin_bd_1. 3 hits.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00270. ChtBD1. 4 hits.
[Graphical view]
SUPFAMiSSF57016. SSF57016. 4 hits.
PROSITEiPS00026. CHIT_BIND_I_1. 4 hits.
PS50941. CHIT_BIND_I_2. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P02876-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRKMMSTMAL TLGAAVFLAF AAATAQAQRC GEQGSNMECP NNLCCSQYGY
60 70 80 90 100
CGMGGDYCGK GCQNGACWTS KRCGSQAGGA TCPNNHCCSQ YGHCGFGAEY
110 120 130 140 150
CGAGCQGGPC RADIKCGSQS GGKLCPNNLC CSQWGFCGLG SEFCGGGCQS
160 170 180 190 200
GACSTDKPCG KDAGGRVCTN NYCCSKWGSC GIGPGYCGAG CQSGGCDAVF
210
AGAITANSTL LAE
Length:213
Mass (Da):21,356
Last modified:November 1, 1990 - v3
Checksum:iF656A5C9277148AF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti64 – 641N → D AA sequence (PubMed:6546522).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M25537 mRNA. Translation: AAA34258.1.
PIRiS09624. AEWT2.
UniGeneiTa.147.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M25537 mRNA. Translation: AAA34258.1.
PIRiS09624. AEWT2.
UniGeneiTa.147.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2WGCX-ray2.20A/B29-198[»]
9WGAX-ray1.80A/B29-198[»]
ProteinModelPortaliP02876.
SMRiP02876. Positions 28-198.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

Allergomei650. Tri a 18.
CAZyiCBM18. Carbohydrate-Binding Module Family 18.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

GrameneiP02876.

Miscellaneous databases

EvolutionaryTraceiP02876.
PROiP02876.

Family and domain databases

Gene3Di3.30.60.10. 4 hits.
InterProiIPR001002. Chitin-bd_1.
IPR018371. Chitin-binding_1_CS.
[Graphical view]
PfamiPF00187. Chitin_bind_1. 4 hits.
[Graphical view]
PRINTSiPR00451. CHITINBINDNG.
ProDomiPD000609. Chitin_bd_1. 3 hits.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00270. ChtBD1. 4 hits.
[Graphical view]
SUPFAMiSSF57016. SSF57016. 4 hits.
PROSITEiPS00026. CHIT_BIND_I_1. 4 hits.
PS50941. CHIT_BIND_I_2. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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(1988) [PubMed] [Europe PMC] [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(1983) [PubMed] [Europe PMC] [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(1988) [PubMed] [Europe PMC] [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(1976) [PubMed] [Europe PMC] [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(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
  6. Erratum
    Wright C.S.
    J. Mol. Biol. 199:239-239(1987)

Entry informationi

Entry nameiAGI2_WHEAT
AccessioniPrimary (citable) accession number: P02876
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 1, 1990
Last modified: March 4, 2015
This is version 112 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.