GRIK2_DANRE
ID GRIK2_DANRE Reviewed; 908 AA.
AC A0A2R8QF68;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2018, sequence version 1.
DT 03-AUG-2022, entry version 21.
DE RecName: Full=Glutamate receptor ionotropic, kainate 2 {ECO:0000305};
DE Short=GluK2 {ECO:0000303|PubMed:31474366};
DE Flags: Precursor;
GN Name=grik2 {ECO:0000312|EMBL:LO018531};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000312|Proteomes:UP000000437};
RN [1] {ECO:0000312|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen {ECO:0000312|Proteomes:UP000000437};
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2] {ECO:0000305}
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=31474366; DOI=10.1016/j.cell.2019.07.034;
RA Gong J., Liu J., Ronan E.A., He F., Cai W., Fatima M., Zhang W., Lee H.,
RA Li Z., Kim G.H., Pipe K.P., Duan B., Liu J., Xu X.Z.S.;
RT "A Cold-Sensing Receptor Encoded by a Glutamate Receptor Gene.";
RL Cell 178:1375-1386.e11(2019).
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 (PubMed:31474366). Functions in dorsal root ganglion neurons (By
CC similarity). {ECO:0000250|UniProtKB:P39087,
CC ECO:0000269|PubMed:31474366}.
CC -!- ACTIVITY REGULATION: Cold receptor activity activated by temperatures
CC between 10-19 degrees Celsius. {ECO:0000269|PubMed:31474366}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P42260};
CC Multi-pass membrane protein {ECO:0000255}. Postsynaptic cell membrane
CC {ECO:0000250|UniProtKB:P42260}; Multi-pass membrane protein
CC {ECO:0000255}.
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; CABZ01076436; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABZ01076437; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABZ01076438; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABZ01076439; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABZ01076440; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABZ01076441; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABZ01076442; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABZ01085971; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABZ01085972; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; LO018531; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A2R8QF68; -.
DR SMR; A0A2R8QF68; -.
DR STRING; 7955.ENSDARP00000101999; -.
DR Ensembl; ENSDART00000180026; ENSDARP00000152462; ENSDARG00000113771.
DR Ensembl; ENSDART00000183974; ENSDARP00000149888; ENSDARG00000113771.
DR GeneTree; ENSGT00940000155610; -.
DR Reactome; R-DRE-451307; Activation of Na-permeable kainate receptors.
DR Reactome; R-DRE-451308; Activation of Ca-permeable Kainate Receptor.
DR PRO; PR:A0A2R8QF68; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 16.
DR Bgee; ENSDARG00000113771; Expressed in brain and 6 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0032983; C:kainate selective glutamate receptor complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0045211; C:postsynaptic membrane; IBA:GO_Central.
DR GO; GO:0042734; C:presynaptic membrane; IBA:GO_Central.
DR GO; GO:0008066; F:glutamate receptor activity; IBA:GO_Central.
DR GO; GO:0015277; F:kainate selective glutamate receptor activity; IBA:GO_Central.
DR GO; GO:0015276; F:ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:1904315; F:transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential; IBA:GO_Central.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0035249; P:synaptic transmission, glutamatergic; IBA:GO_Central.
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 3: Inferred from homology;
KW Cell membrane; Disulfide bond; Glycoprotein; Ion channel; Ion transport;
KW Ligand-gated ion channel; Membrane; Postsynaptic cell membrane; Receptor;
KW Reference proteome; Signal; Synapse; Transmembrane; Transmembrane helix;
KW Transport.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..908
FT /note="Glutamate receptor ionotropic, kainate 2"
FT /evidence="ECO:0000255"
FT /id="PRO_5022361179"
FT TOPO_DOM 32..561
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 562..582
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 583..638
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 639..659
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 660..819
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 820..840
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 841..908
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT BINDING 516..518
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P42260"
FT BINDING 523
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P42260"
FT BINDING 689..690
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P42260"
FT BINDING 738
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P42260"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 378
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 412
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 423
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 430
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 546
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 751
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 96..347
FT /evidence="ECO:0000250|UniProtKB:P42260"
SQ SEQUENCE 908 AA; 102520 MW; 6C673D910E3D6504 CRC64;
MQRIAGITKM VTHRRWLGLL LLLLCVGYSH GMPHVLRFGG IFESIESGPS GAEELAFKFA
LNTINRNRTL LPNTTLTYDI QRINIHDSFE ASRKACDQLS LGVAAIFGPS HSSSANAVQS
ICNALGVPHI QTKWKHQVSD NRDSFYVNLY PDFSSLSRAI LDLVHFFKWK TVTVVYDDST
GLIRLQELIK APSRYNIRLK IRQLPADTKD AKPLLKEMKR GKEFHVIFDC GHEMAAGILK
QALAMGMMTE YYHYIFTTLD LFALDVEPYR YSGVNMTGFR ILNTENSQVS SIIEKWSMER
LQAPPKPDSG LLDGFMTTDA ALMYDAVHVV AVAVQQSPQI TVSSLQCNRH KPWRFGNRFM
TLIKEAHWDG LTGRINFNRT NGLRTDFDLD VISLKEEGLE KIGTWDPASG LNMTENQKGK
TANVTDSLSN RSLVVSTILE EPYVMFKKSD KPLYGNDRFE GYCVDLLREL AAILGFGYEL
RLVEDGRYGA QDESSGQWNG MVRELMDHKA DLAVAPLAIT YVREKVIDFS KPFMTLGISI
LYRKPNGTNP GVFSFLNPLS PDIWMYILLA YLGVSCVLFV IARFSPYEWY NPHPCNPDSD
VVENNFTLLN SFWFGVGALM QQGSELMPKA LSTRIVGGIW WFFTLIIISS YTANLAAFLT
VERMESPIDS ADDLAKQTKI EYGVVEDGST MTFFKKTKIS TYDKMWEFMS SRRHSVMVKS
IEEGIERVLT SDYAFLMEST TIEFVTQRNC NLTQIGGLID SKAYGVGTPM GSPYRDKITI
AILQLQEEGK LHMMKEKWWR GNGCPEEENK EASALGVQNI GGIFIVLAAG LVLSVFVAVG
EFLYKSKQNA QLEKRSFCSA MVDELRVSLK CQRRLKHKPQ PPVMVKTDEV INMHTFNDRR
LPGKETMA
