Protein Details: Glutamate receptor 3.3
Protein ID
ICDB_Pro_1464
Protein Name
Glutamate receptor 3.3
Gene Name
GLR3.3; At1g42540; T8D8.1
Organism
Arabidopsis thaliana (Mouse-ear cress)
Length
933 amino acids
AlphaFoldDB
AF-Q9C8E7-F1-model_v4.pdb
Function
Glutamate-gated receptor that probably acts as a non-selective cation channel; at least in roots and hypocotyls (Probable). Can be triggered by Ala; Asn; Cys; Glu; Gly; Ser and glutathione (a tripeptide consisting of Glu-Gly-Cys). Mediates leaf-to-leaf wound signaling. May be involved in light-signal transduction and calcium homeostasis via the regulation of calcium influx into cells. Contributes to pathogen-associated molecular patterns (PAMP) elicitor-mediated resistance. Partially involved in free cytosolic calcium variations; nitric oxide (NO) production; reactive oxygen species (ROS) production and expression of defense-related genes in response to oligogalacturonide elicitors. Inovlved in resistance against Hyaloperonospora arabidopsidis. Required for glutathione-induced defense responses; and innate immunity responses against the bacterial pathogen Pseudomonas syringae pv tomato strain DC3000. Required for the transmission of wound-induced; phloem-propagated action potential to neighbor leaves.
Sequence
Ligand Binding
Binding Site
BINDING 473; /ligand="L-glutamate"; BINDING 543..545; /ligand="glycine"; BINDING 543..545; /ligand="L-cysteine"; BINDING 543..545; /ligand="L-glutamate"; BINDING 543..545; /ligand="L-methionine"; BINDING 550; /ligand="glycine"; BINDING 550; /ligand="L-cysteine"; BINDING 550; /ligand="L-glutamate"; BINDING 550; /ligand="L-methionine"; BINDING 702; /ligand="glycine"; BINDING 702; /ligand="L-cysteine"; BINDING 702; /ligand="L-glutamate"; BINDING 702; /ligand="L-methionine"; BINDING 746..749; /ligand="glycine"; BINDING 746..749; /ligand="L-cysteine"; BINDING 746..749; /ligand="L-glutamate"; BINDING 746..749; /ligand="L-methionine"
Disease
Location
Expressed predominantly in roots and siliques
DOI ID
10.1038/35048500; 10.1111/tpj.13415; 10.1126/science.292.5521.1486b; 10.1093/oxfordjournals.molbev.a004165; 10.1104/pp.106.088989; 10.1104/pp.107.108134; 10.1038/nature12478; 10.1105/tpc.113.110668; 10.1111/tpj.12311; 10.1104/pp.113.217208; 10.1111/nph.12807; 10.1073/pnas.1905142117
RefSeq
NP_001322169.1; NP_001322170.1; NP_174978.1