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Protein

Agglutinin isolectin 3

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 3
Alternative name(s):
WGA3
OrganismiTriticum aestivum (Wheat)
Taxonomic identifieri4565 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladePooideaeTriticeaeTriticum
ProteomesiUP000019116 Componenti: 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 3PRO_0000005259Add
BLAST
Propeptidei172 – 18615PRO_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.2 Publications

Structurei

Secondary structure

1
186
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 63Combined sources
Turni7 – 93Combined sources
Helixi13 – 153Combined sources
Beta strandi24 – 274Combined sources
Helixi28 – 314Combined sources
Beta strandi32 – 343Combined sources
Beta strandi37 – 393Combined sources
Helixi48 – 503Combined sources
Helixi56 – 583Combined sources
Beta strandi65 – 706Combined sources
Helixi71 – 744Combined sources
Beta strandi80 – 823Combined sources
Helixi90 – 934Combined sources
Helixi99 – 1013Combined sources
Beta strandi108 – 1136Combined sources
Helixi114 – 1174Combined sources
Beta strandi123 – 1253Combined sources
Helixi133 – 1353Combined sources
Turni136 – 1383Combined sources
Helixi142 – 1443Combined sources
Beta strandi153 – 1564Combined sources
Helixi157 – 1604Combined sources
Beta strandi166 – 1683Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10969.

Family & Domainsi

Domains and Repeats

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

Region

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

Sequence similaritiesi

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

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

        10         20         30         40         50
QRCGEQGSGM ECPNNLCCSQ YGYCGMGGDY CGKGCQNGAC WTSKRCGSQA
60 70 80 90 100
GGKTCPNNHC CSQYGHCGFG AEYCGAGCQG GPCRADIKCG SQAGGKLCPN
110 120 130 140 150
NLCCSQWGYC GLGSEFCGEG CQNGACSTDK PCGKDAGGRV CTNNYCCSKW
160 170 180
GSCGIGPGYC GAGCQSGGCD GVFAEAIATN STLLAE
Length:186
Mass (Da):18,756
Last modified:July 1, 1989 - v1
Checksum:i68461A20339378FD
GO

Experimental Info

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02961 mRNA. Translation: AAA34257.1.
PIRiA28401.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02961 mRNA. Translation: AAA34257.1.
PIRiA28401.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
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

GrameneiP10969.

Miscellaneous databases

EvolutionaryTraceiP10969.
PROiP10969.

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. "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: January 7, 2015
This is version 105 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, 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.