Q91755 · GRIK2_XENLA
- ProteinGlutamate receptor ionotropic, kainate 2
- Genegrik2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids913 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score4/5
Function
function
Ionotropic glutamate receptor that functions as a cation-permeable ligand-gated ion channel, gated by L-glutamate and the glutamatergic agonist kainic acid. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. Binding of the excitatory neurotransmitter L-glutamate induces a conformation change, leading to the opening of the cation channel, and thereby converts the chemical signal to an electrical impulse. The receptor then desensitizes rapidly and enters a transient inactive state, characterized by the presence of bound agonist.
Independent of its ionotropic glutamate receptor activity, acts as a thermoreceptor conferring sensitivity to cold temperatures (By similarity).
Functions in dorsal root ganglion neurons (By similarity).
Functions in dorsal root ganglion neurons (By similarity).
Catalytic activity
- Ca2+(in) = Ca2+(out)
- Na+(in) = Na+(out)
Activity regulation
Cold receptor activity activated by temperatures between 10-19 degrees Celsius.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 521 | L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: P | ||||||
Binding site | 523 | L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 528 | L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 694 | L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 695 | L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 743 | L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | plasma membrane | |
Cellular Component | postsynaptic membrane | |
Molecular Function | extracellularly glutamate-gated ion channel activity | |
Molecular Function | glutamate-gated calcium ion channel activity | |
Molecular Function | glutamate-gated receptor activity | |
Molecular Function | kainate selective glutamate receptor activity | |
Biological Process | detection of cold stimulus involved in thermoception |
Keywords
- Molecular function
- Biological process
Names & Taxonomy
Protein names
- Recommended nameGlutamate receptor ionotropic, kainate 2
- Short namesGluK2
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Amphibia > Batrachia > Anura > Pipoidea > Pipidae > Xenopodinae > Xenopus > Xenopus
Accessions
- Primary accessionQ91755
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Multi-pass membrane protein
Postsynaptic cell membrane ; Multi-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-566 | Extracellular | ||||
Sequence: MCAGTMKIISPSLTNSFFRCTLRFVACLFWIGYSQGTTHVLRFGGIFESVESGPSGAEELAFRFAVNTINRNRTLLPNTTITYDTQRINLYDSFEASRKACEQLSLGVAAIFGPSHSSSANAVQSICNALGVPHIQTRWKHQVSDNKDSFYVSLYPDFSSLSRAILDLVQFFKWKTVTIAYDDSTGLIRLQELIKAPSRYNLRLKIRQLPIDTKDAKPLLKEMKRGKEFHVIFDCSHDMAAGILKQALAMGMMTEYYHYIFTTLDLFALDVEPYRYSGVNMTGFRILNIENSQVLSIIEKWSMERLQAPPKPDSGLLDGFMTTDAALMYDAVHVASVAVQQFPQMTVSSLQCNRHKPWRFGARFINLIKEAHWEGLTGRITFNKTNGLRTDFDLDVISLKEEGLEKIGTWDPTSGLNMTDNQKGKPANITDSLSNRSLIVTTILEEPYVMFKKSDKPLYGKARFEGYCIDLLEKLSRILGFEYEVRLVEDGKYGAKDDSTQQWNGMVRELMDHKADLAVAPLAITYVREQVIDFTKPFMTLGIGILYRKPNGTNPGVFSFLNPLSP | ||||||
Transmembrane | 567-587 | Helical | ||||
Sequence: DIWMYILLAYLGVSCVLFVIA | ||||||
Topological domain | 588-643 | Cytoplasmic | ||||
Sequence: RFSPYEWYNPHPCNPDSDVVENNFTLLNSFWFGVGALMQQGSELMPKALSTRIVGG | ||||||
Transmembrane | 644-664 | Helical | ||||
Sequence: IWWFFTLIIISSYTANLAAFL | ||||||
Topological domain | 665-824 | Extracellular | ||||
Sequence: TVERMESPIDSADDLAKQTKIEYGAVQDGATMTFFKKSRIPTYEKMWAFMNSRSQSVLVKNNEEGIQRALTSDYAFLMESTTIEFVTQRNCNLTQIGGLIDSKGYGVGTPMGSPYRDKITIAILQLQEEGVLHMMKEKWWRGNGCPEEESKEASALGVQN | ||||||
Transmembrane | 825-845 | Helical | ||||
Sequence: IGGIFIVLAAGLVLSVFVAVG | ||||||
Topological domain | 846-913 | Cytoplasmic | ||||
Sequence: EFLYKSKKNAQLEKRSFCSAMVEELRMSLKCQRRLKHKPQPPVIVKTEEVINMHTFNDRRLPGKETMA |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000450267 | 1-913 | Glutamate receptor ionotropic, kainate 2 | |||
Sequence: MCAGTMKIISPSLTNSFFRCTLRFVACLFWIGYSQGTTHVLRFGGIFESVESGPSGAEELAFRFAVNTINRNRTLLPNTTITYDTQRINLYDSFEASRKACEQLSLGVAAIFGPSHSSSANAVQSICNALGVPHIQTRWKHQVSDNKDSFYVSLYPDFSSLSRAILDLVQFFKWKTVTIAYDDSTGLIRLQELIKAPSRYNLRLKIRQLPIDTKDAKPLLKEMKRGKEFHVIFDCSHDMAAGILKQALAMGMMTEYYHYIFTTLDLFALDVEPYRYSGVNMTGFRILNIENSQVLSIIEKWSMERLQAPPKPDSGLLDGFMTTDAALMYDAVHVASVAVQQFPQMTVSSLQCNRHKPWRFGARFINLIKEAHWEGLTGRITFNKTNGLRTDFDLDVISLKEEGLEKIGTWDPTSGLNMTDNQKGKPANITDSLSNRSLIVTTILEEPYVMFKKSDKPLYGKARFEGYCIDLLEKLSRILGFEYEVRLVEDGKYGAKDDSTQQWNGMVRELMDHKADLAVAPLAITYVREQVIDFTKPFMTLGIGILYRKPNGTNPGVFSFLNPLSPDIWMYILLAYLGVSCVLFVIARFSPYEWYNPHPCNPDSDVVENNFTLLNSFWFGVGALMQQGSELMPKALSTRIVGGIWWFFTLIIISSYTANLAAFLTVERMESPIDSADDLAKQTKIEYGAVQDGATMTFFKKSRIPTYEKMWAFMNSRSQSVLVKNNEEGIQRALTSDYAFLMESTTIEFVTQRNCNLTQIGGLIDSKGYGVGTPMGSPYRDKITIAILQLQEEGVLHMMKEKWWRGNGCPEEESKEASALGVQNIGGIFIVLAAGLVLSVFVAVGEFLYKSKKNAQLEKRSFCSAMVEELRMSLKCQRRLKHKPQPPVIVKTEEVINMHTFNDRRLPGKETMA | ||||||
Glycosylation | 72 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 78 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 101↔352 | |||||
Sequence: CEQLSLGVAAIFGPSHSSSANAVQSICNALGVPHIQTRWKHQVSDNKDSFYVSLYPDFSSLSRAILDLVQFFKWKTVTIAYDDSTGLIRLQELIKAPSRYNLRLKIRQLPIDTKDAKPLLKEMKRGKEFHVIFDCSHDMAAGILKQALAMGMMTEYYHYIFTTLDLFALDVEPYRYSGVNMTGFRILNIENSQVLSIIEKWSMERLQAPPKPDSGLLDGFMTTDAALMYDAVHVASVAVQQFPQMTVSSLQC | ||||||
Glycosylation | 280 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 383 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 417 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 428 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 435 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 551 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 755↔809 | |||||
Sequence: CNLTQIGGLIDSKGYGVGTPMGSPYRDKITIAILQLQEEGVLHMMKEKWWRGNGC | ||||||
Glycosylation | 756 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Homotetramer and heterotetramer with GRIK5. Tetramers may be formed by the dimerization of dimers.
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length913
- Mass (Da)103,106
- Last updated2020-06-17 v2
- Checksum0BD59723D40CA128
Keywords
- Technical term