GRID2_DANRE
ID GRID2_DANRE Reviewed; 1009 AA.
AC Q68Y21;
DT 09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Glutamate receptor ionotropic, delta-2;
DE Short=GluD2;
DE Short=GluR delta-2 subunit;
DE Flags: Precursor;
GN Name=grid2 {ECO:0000312|EMBL:BAD36785.1};
GN Synonyms=glurd2 {ECO:0000312|ZFIN:ZDB-GENE-040913-1};
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;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAD36785.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=15313188; DOI=10.1016/j.bbrc.2004.07.095;
RA Mikami Y., Yoshida T., Matsuda N., Mishina M.;
RT "Expression of zebrafish glutamate receptor delta2 in neurons with
RT cerebellum-like wiring.";
RL Biochem. Biophys. Res. Commun. 322:168-176(2004).
CC -!- FUNCTION: Receptor for glutamate. L-glutamate acts as an excitatory
CC neurotransmitter at many synapses in the central nervous system. The
CC postsynaptic actions of Glu are mediated by a variety of receptors that
CC are named according to their selective agonists (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}. Postsynaptic cell membrane {ECO:0000250}; Multi-
CC pass membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in cerebellar Purkinje cells, in crest
CC cells in the medial octavolateral nucleus and in type I neurons of the
CC optic tectum. {ECO:0000269|PubMed:15313188}.
CC -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1)
CC family. GRID2 subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB154207; BAD36785.1; -; mRNA.
DR RefSeq; NP_001004123.1; NM_001004123.1.
DR AlphaFoldDB; Q68Y21; -.
DR SMR; Q68Y21; -.
DR STRING; 7955.ENSDARP00000116997; -.
DR PaxDb; Q68Y21; -.
DR GeneID; 448841; -.
DR KEGG; dre:448841; -.
DR CTD; 2895; -.
DR ZFIN; ZDB-GENE-040913-1; grid2.
DR eggNOG; KOG1052; Eukaryota.
DR InParanoid; Q68Y21; -.
DR OrthoDB; 122304at2759; -.
DR PhylomeDB; Q68Y21; -.
DR PRO; PR:Q68Y21; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
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:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0045211; C:postsynaptic membrane; IBA:GO_Central.
DR GO; GO:0008066; F:glutamate receptor activity; IBA:GO_Central.
DR GO; GO:0004970; F:ionotropic glutamate receptor activity; IEA:InterPro.
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 2: Evidence at transcript level;
KW Cell membrane; 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..23
FT /evidence="ECO:0000255"
FT CHAIN 24..1009
FT /note="Glutamate receptor ionotropic, delta-2"
FT /id="PRO_0000011567"
FT TOPO_DOM 24..566
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 567..587
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 588..635
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 636..656
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 657..830
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 831..851
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 852..1009
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 989..1009
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 293
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 306
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 390
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 426
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 713
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1009 AA; 113625 MW; 7BD2BD664EB371BE CRC64;
MKVFPAVLFL ITFWSLEWEP VLPDSIIHIG AIFDESAKKD DEVFRMAVAD LNLNNEILET
EKITVSVEFV DGNNPFQAVQ EACELMNRGI LALVSSIGCM SAGSLQSLAD AMHIPHLFIQ
RAPAGTPRSS CPPTTRAQPD DYTLFVRPPV YLNDVIFQVV MEYTWQKFII FYDTDYDIRG
IENFLDQTSQ QGMDVSLQKV ESNINMMITG MFRTMRVEEL HRYRDTLRRA VLFMSPATAK
AFITEVVETN LVAFDCQWII INEEISDMDV QELVMKSIGR LTLVRQTFPL PQNTSQRCVR
NNHRINTSLC DPKDPKAQML EITNRYIYDT VLLLANTFHR KLEDRKWHSM ASLSCIRKGS
KPWQGGKSML ETVKKGGVSG LTSLLEFNDN GSNPNIHFEI LGTNYGEDRG RGVSRLATWD
PIHGLNGTLT DRKLENNMRG VVLRVVTVLE EPFVMVSENV LGKPKKYQGF SIDVLDALAN
YLGFKYEIYV APDHKYGSQQ ADGTWNGLIG ELVFKRADVG LSALTITPER ESVVDFTTRY
MDYSVGVLLR KAERTVDMFA CLAPFDLSLW ACIAGTVLLV GTLVYLLNWL NPPRLPMGSV
SSTTLYNSMW FVYGSFVQQG GEVPYTTLAT RMMMGVWWLF ALIVISSYTA NLAAFLTISR
IENSIQSLQD LAKQTDLPYG TVLDSAVYDQ VRSKGMNPFE RDPMYSQMWR MINRTGGAEN
NVEESKEGIR KVKYGRFAFV WDAAVLEYVA INDEDCSLYT VSNNVADRGY GMAMQHGSPY
RDIFSQRILE LQQNGDMDIL KLKWWPRDSP CDLYSPVGTR KSGSALDIHS FAGVFFVLAA
GVVLSCLIAT VETWWTRRKG SRVPSKEDDK EIDLEHLHHR VNSLCTEDES PHKQFSTSSI
DLTPLDMDSL PAARQALEQI SDFRNTHITT TTFIPEQIQT LSRSLSAKAA AGFAFGAVQD
HRTGGPFRQR APNGGFFRSP VKTMSSIPYQ PTPAPNFSYG NDPDRGTSI
