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P10969

- AGI3_WHEAT

UniProt

P10969 - AGI3_WHEAT

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Protein
Agglutinin isolectin 3
Gene
N/A
Organism
Triticum aestivum (Wheat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

  1. 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 3
Alternative name(s):
WGA3
OrganismiTriticum aestivum (Wheat)
Taxonomic identifieri4565 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladePooideaeTriticeaeTriticum
ProteomesiUP000019116: Unplaced

Organism-specific databases

GrameneiP10969.

Pathology & Biotechi

Protein family/group databases

Allergomei650. Tri a 18.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 171171Agglutinin isolectin 3
PRO_0000005259Add
BLAST
Propeptidei172 – 18615
PRO_0000005260Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11Pyrrolidone carboxylic acid
Disulfide bondi3 ↔ 18
Disulfide bondi12 ↔ 24
Disulfide bondi17 ↔ 31
Disulfide bondi35 ↔ 40
Disulfide bondi46 ↔ 61
Disulfide bondi55 ↔ 67
Disulfide bondi60 ↔ 74
Disulfide bondi78 ↔ 83
Disulfide bondi89 ↔ 104
Disulfide bondi98 ↔ 110
Disulfide bondi103 ↔ 117
Disulfide bondi121 ↔ 126
Disulfide bondi132 ↔ 147
Disulfide bondi141 ↔ 153
Disulfide bondi146 ↔ 160
Disulfide bondi164 ↔ 169
Glycosylationi180 – 1801N-linked (GlcNAc...)

Keywords - PTMi

Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

Interactioni

Subunit structurei

Homodimer, u-shaped.1 Publication

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 63
Turni7 – 93
Helixi13 – 153
Beta strandi24 – 274
Helixi28 – 314
Beta strandi32 – 343
Beta strandi37 – 393
Helixi48 – 503
Helixi56 – 583
Beta strandi65 – 706
Helixi71 – 744
Beta strandi80 – 823
Helixi90 – 934
Helixi99 – 1013
Beta strandi108 – 1136
Helixi114 – 1174
Beta strandi123 – 1253
Helixi133 – 1353
Turni136 – 1383
Helixi142 – 1443
Beta strandi153 – 1564
Helixi157 – 1604
Beta strandi166 – 1683

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K7TX-ray2.40A/B1-186[»]
1K7UX-ray2.20A/B1-186[»]
1K7VX-ray2.20A/B2-186[»]
1WGTX-ray1.90A/B2-186[»]
2X52X-ray1.70A/B2-171[»]
ProteinModelPortaliP10969.
SMRiP10969. Positions 2-171.

Miscellaneous databases

EvolutionaryTraceiP10969.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 4242Chitin-binding type-1 1
Add
BLAST
Domaini43 – 8543Chitin-binding type-1 2
Add
BLAST
Domaini86 – 12843Chitin-binding type-1 3
Add
BLAST
Domaini129 – 17143Chitin-binding type-1 4
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni10 – 123Substrate binding By similarity
Regioni62 – 7312Substrate binding
Add
BLAST
Regioni114 – 1152Substrate binding

Sequence similaritiesi

Keywords - Domaini

Repeat

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: Fragment.

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

P10969-1 [UniParc]FASTAAdd to Basket

« Hide

QRCGEQGSGM ECPNNLCCSQ YGYCGMGGDY CGKGCQNGAC WTSKRCGSQA    50
GGKTCPNNHC CSQYGHCGFG AEYCGAGCQG GPCRADIKCG SQAGGKLCPN 100
NLCCSQWGYC GLGSEFCGEG CQNGACSTDK PCGKDAGGRV CTNNYCCSKW 150
GSCGIGPGYC GAGCQSGGCD GVFAEAIATN STLLAE 186
Length:186
Mass (Da):18,756
Last modified:July 1, 1989 - v1
Checksum:i68461A20339378FD
GO

Non-terminal residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J02961 mRNA. Translation: AAA34257.1.
PIRiA28401.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J02961 mRNA. Translation: AAA34257.1 .
PIRi A28401.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1K7T X-ray 2.40 A/B 1-186 [» ]
1K7U X-ray 2.20 A/B 1-186 [» ]
1K7V X-ray 2.20 A/B 2-186 [» ]
1WGT X-ray 1.90 A/B 2-186 [» ]
2X52 X-ray 1.70 A/B 2-171 [» ]
ProteinModelPortali P10969.
SMRi P10969. Positions 2-171.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

Allergomei 650. Tri a 18.
CAZyi CBM18. Carbohydrate-Binding Module Family 18.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Organism-specific databases

Gramenei P10969.

Miscellaneous databases

EvolutionaryTracei P10969.
PROi P10969.

Family and domain databases

Gene3Di 3.30.60.10. 4 hits.
InterProi IPR001002. Chitin-bd_1.
IPR018371. Chitin-binding_1_CS.
[Graphical view ]
Pfami PF00187. Chitin_bind_1. 4 hits.
[Graphical view ]
PRINTSi PR00451. CHITINBINDNG.
ProDomi PD000609. Chitin_bd_1. 3 hits.
[Graphical view ] [Entries sharing at least one domain ]
SMARTi SM00270. ChtBD1. 4 hits.
[Graphical view ]
SUPFAMi SSF57016. SSF57016. 4 hits.
PROSITEi PS00026. CHIT_BIND_I_1. 4 hits.
PS50941. CHIT_BIND_I_2. 4 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH SUBSTRATES.

Entry informationi

Entry nameiAGI3_WHEAT
AccessioniPrimary (citable) accession number: P10969
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: July 9, 2014
This is version 101 of the entry and version 1 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

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

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