GRIK2_XENLA
ID GRIK2_XENLA Reviewed; 913 AA.
AC Q91755; A0A1L8G3C5;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 17-JUN-2020, sequence version 2.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Glutamate receptor ionotropic, kainate 2;
DE Short=GluK2;
DE AltName: Full=Glutamate receptor 6;
DE Short=GluR-6;
DE Short=GluR6;
GN Name=grik2; Synonyms=glur6;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1] {ECO:0000312|Proteomes:UP000186698}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J {ECO:0000312|Proteomes:UP000186698};
RX PubMed=27762356; DOI=10.1038/nature19840;
RA Session A.M., Uno Y., Kwon T., Chapman J.A., Toyoda A., Takahashi S.,
RA Fukui A., Hikosaka A., Suzuki A., Kondo M., van Heeringen S.J., Quigley I.,
RA Heinz S., Ogino H., Ochi H., Hellsten U., Lyons J.B., Simakov O.,
RA Putnam N., Stites J., Kuroki Y., Tanaka T., Michiue T., Watanabe M.,
RA Bogdanovic O., Lister R., Georgiou G., Paranjpe S.S., van Kruijsbergen I.,
RA Shu S., Carlson J., Kinoshita T., Ohta Y., Mawaribuchi S., Jenkins J.,
RA Grimwood J., Schmutz J., Mitros T., Mozaffari S.V., Suzuki Y., Haramoto Y.,
RA Yamamoto T.S., Takagi C., Heald R., Miller K., Haudenschild C., Kitzman J.,
RA Nakayama T., Izutsu Y., Robert J., Fortriede J., Burns K., Lotay V.,
RA Karimi K., Yasuoka Y., Dichmann D.S., Flajnik M.F., Houston D.W.,
RA Shendure J., DuPasquier L., Vize P.D., Zorn A.M., Ito M., Marcotte E.M.,
RA Wallingford J.B., Ito Y., Asashima M., Ueno N., Matsuda Y., Veenstra G.J.,
RA Fujiyama A., Harland R.M., Taira M., Rokhsar D.S.;
RT "Genome evolution in the allotetraploid frog Xenopus laevis.";
RL Nature 538:336-343(2016).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 629-913.
RC TISSUE=Brain;
RX PubMed=8723645;
RA Ishimaru H., Kamboj R., Ambrosini A., Henley J.M., Soloviev M.M., Sudan H.,
RA Rossier J., Abutidze K., Rampersad V., Usherwood P.N.R., Bateson A.N.,
RA Barnard E.A.;
RT "A unitary non-NMDA receptor short subunit from Xenopus: DNA cloning and
RT expression.";
RL Recept. Channels 4:31-49(1996).
CC -!- FUNCTION: Ionotropic glutamate receptor (By similarity). L-glutamate
CC acts as an excitatory neurotransmitter at many synapses in the central
CC nervous system. Binding of the excitatory neurotransmitter L-glutamate
CC induces a conformation change, leading to the opening of the cation
CC channel, and thereby converts the chemical signal to an electrical
CC impulse. The receptor then desensitizes rapidly and enters a transient
CC inactive state, characterized by the presence of bound agonist (By
CC similarity). {ECO:0000250|UniProtKB:P39087}.
CC -!- FUNCTION: Independent of its ionotropic glutamate receptor activity,
CC acts as a thermoreceptor conferring sensitivity to cold temperatures
CC (By similarity). Functions in dorsal root ganglion neurons (By
CC similarity). {ECO:0000250|UniProtKB:P39087}.
CC -!- ACTIVITY REGULATION: Cold receptor activity activated by temperatures
CC between 10-19 degrees Celsius. {ECO:0000250|UniProtKB:P39087}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC Postsynaptic cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1)
CC family. GRIK2 subfamily. {ECO:0000305}.
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DR EMBL; CM004475; OCT78221.1; -; Genomic_DNA.
DR EMBL; X94116; CAA63838.1; -; mRNA.
DR AlphaFoldDB; Q91755; -.
DR SMR; Q91755; -.
DR STRING; 8355.A0A1L8G3C5; -.
DR OMA; FNYTFKL; -.
DR Proteomes; UP000186698; Genome assembly.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005234; F:extracellularly glutamate-gated ion channel activity; ISS:UniProtKB.
DR GO; GO:0004970; F:ionotropic glutamate receptor activity; ISS:UniProtKB.
DR GO; GO:0120169; P:detection of cold stimulus involved in thermoception; ISS:UniProtKB.
DR InterPro; IPR001828; ANF_lig-bd_rcpt.
DR InterPro; IPR019594; Glu/Gly-bd.
DR InterPro; IPR001508; Iono_rcpt_met.
DR InterPro; IPR001320; Iontro_rcpt.
DR InterPro; IPR028082; Peripla_BP_I.
DR Pfam; PF01094; ANF_receptor; 1.
DR Pfam; PF00060; Lig_chan; 1.
DR Pfam; PF10613; Lig_chan-Glu_bd; 1.
DR PRINTS; PR00177; NMDARECEPTOR.
DR SMART; SM00918; Lig_chan-Glu_bd; 1.
DR SMART; SM00079; PBPe; 1.
DR SUPFAM; SSF53822; SSF53822; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; Ion channel; Ion transport;
KW Ligand-gated ion channel; Membrane; Postsynaptic cell membrane; Receptor;
KW Reference proteome; Synapse; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..913
FT /note="Glutamate receptor ionotropic, kainate 2"
FT /id="PRO_0000450267"
FT TOPO_DOM 1..566
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 567..587
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 588..643
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 644..664
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 665..824
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 825..845
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 846..913
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT BINDING 521..523
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P42260"
FT BINDING 528
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P42260"
FT BINDING 694..695
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P42260"
FT BINDING 743
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P42260"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 280
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 383
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 417
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 428
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 435
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 551
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 756
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 101..352
FT /evidence="ECO:0000250|UniProtKB:P42260"
SQ SEQUENCE 913 AA; 103106 MW; 0BD59723D40CA128 CRC64;
MCAGTMKIIS PSLTNSFFRC TLRFVACLFW IGYSQGTTHV LRFGGIFESV ESGPSGAEEL
AFRFAVNTIN RNRTLLPNTT ITYDTQRINL YDSFEASRKA CEQLSLGVAA IFGPSHSSSA
NAVQSICNAL GVPHIQTRWK HQVSDNKDSF YVSLYPDFSS LSRAILDLVQ FFKWKTVTIA
YDDSTGLIRL QELIKAPSRY NLRLKIRQLP IDTKDAKPLL KEMKRGKEFH VIFDCSHDMA
AGILKQALAM GMMTEYYHYI FTTLDLFALD VEPYRYSGVN MTGFRILNIE NSQVLSIIEK
WSMERLQAPP KPDSGLLDGF MTTDAALMYD AVHVASVAVQ QFPQMTVSSL QCNRHKPWRF
GARFINLIKE AHWEGLTGRI TFNKTNGLRT DFDLDVISLK EEGLEKIGTW DPTSGLNMTD
NQKGKPANIT DSLSNRSLIV TTILEEPYVM FKKSDKPLYG KARFEGYCID LLEKLSRILG
FEYEVRLVED GKYGAKDDST QQWNGMVREL MDHKADLAVA PLAITYVREQ VIDFTKPFMT
LGIGILYRKP NGTNPGVFSF LNPLSPDIWM YILLAYLGVS CVLFVIARFS PYEWYNPHPC
NPDSDVVENN FTLLNSFWFG VGALMQQGSE LMPKALSTRI VGGIWWFFTL IIISSYTANL
AAFLTVERME SPIDSADDLA KQTKIEYGAV QDGATMTFFK KSRIPTYEKM WAFMNSRSQS
VLVKNNEEGI QRALTSDYAF LMESTTIEFV TQRNCNLTQI GGLIDSKGYG VGTPMGSPYR
DKITIAILQL QEEGVLHMMK EKWWRGNGCP EEESKEASAL GVQNIGGIFI VLAAGLVLSV
FVAVGEFLYK SKKNAQLEKR SFCSAMVEEL RMSLKCQRRL KHKPQPPVIV KTEEVINMHT
FNDRRLPGKE TMA
