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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

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 lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBOP cladePooideaeTriticodaeTriticeaeTriticinaeTriticum
Proteomesi
  • UP000019116 Componenti: Unassembled WGS sequence

Pathology & Biotechi

Protein family/group databases

Allergomei650. Tri a 18.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000052591 – 171Agglutinin isolectin 3Add BLAST171
PropeptideiPRO_0000005260172 – 186Add BLAST15

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1Pyrrolidone carboxylic acid1
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
Glycosylationi180N-linked (GlcNAc...)1

Keywords - PTMi

Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

Interactioni

Subunit structurei

Homodimer, u-shaped.2 Publications

Structurei

Secondary structure

1186
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 6Combined sources3
Turni7 – 9Combined sources3
Helixi13 – 15Combined sources3
Beta strandi24 – 27Combined sources4
Helixi28 – 31Combined sources4
Beta strandi32 – 34Combined sources3
Beta strandi37 – 39Combined sources3
Helixi48 – 50Combined sources3
Helixi56 – 58Combined sources3
Beta strandi65 – 70Combined sources6
Helixi71 – 74Combined sources4
Beta strandi80 – 82Combined sources3
Helixi90 – 93Combined sources4
Helixi99 – 101Combined sources3
Beta strandi108 – 113Combined sources6
Helixi114 – 117Combined sources4
Beta strandi123 – 125Combined sources3
Helixi133 – 135Combined sources3
Turni136 – 138Combined sources3
Helixi142 – 144Combined sources3
Beta strandi153 – 156Combined sources4
Helixi157 – 160Combined sources4
Beta strandi166 – 168Combined sources3

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP10969.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 42Chitin-binding type-1 1PROSITE-ProRule annotationAdd BLAST42
Domaini43 – 85Chitin-binding type-1 2PROSITE-ProRule annotationAdd BLAST43
Domaini86 – 128Chitin-binding type-1 3PROSITE-ProRule annotationAdd BLAST43
Domaini129 – 171Chitin-binding type-1 4PROSITE-ProRule annotationAdd BLAST43

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni10 – 12Substrate bindingBy similarity3
Regioni62 – 73Substrate bindingAdd BLAST12
Regioni114 – 115Substrate binding2

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)DescriptionActionsGraphical viewLength
Non-terminal residuei11

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

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

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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...

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: November 2, 2016
This is version 112 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

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 one 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.