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Database: UniProt
Entry: Q90279_CARAU
LinkDB: Q90279_CARAU
Original site: Q90279_CARAU 
ID   Q90279_CARAU            Unreviewed;       459 AA.
AC   Q90279;
DT   01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 97.
DE   RecName: Full=Glutamate receptor {ECO:0000256|RuleBase:RU367118};
OS   Carassius auratus (Goldfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Cyprininae; Carassius.
OX   NCBI_TaxID=7957 {ECO:0000313|EMBL:AAA21578.1};
RN   [1] {ECO:0000313|EMBL:AAA21578.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain {ECO:0000313|EMBL:AAA21578.1};
RX   PubMed=8041762; DOI=10.1073/pnas.91.15.7154;
RA   Wo Z.G., Oswald R.E.;
RT   "Transmembrane topology of two kainate receptor subunits revealed by N-
RT   glycosylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:7154-7158(1994).
CC   -!- FUNCTION: Receptor for glutamate that functions as a ligand-gated ion
CC       channel in the central nervous system and plays an important role in
CC       excitatory synaptic transmission. L-glutamate acts as an excitatory
CC       neurotransmitter at many synapses in the central nervous system.
CC       {ECO:0000256|RuleBase:RU367118}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU367118};
CC       Multi-pass membrane protein {ECO:0000256|RuleBase:RU367118}.
CC       Postsynaptic cell membrane {ECO:0000256|RuleBase:RU367118}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1)
CC       family. {ECO:0000256|RuleBase:RU367118}.
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DR   EMBL; U08017; AAA21578.1; -; mRNA.
DR   PIR; A57720; A57720.
DR   AlphaFoldDB; Q90279; -.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015276; F:ligand-gated monoatomic ion channel activity; IEA:InterPro.
DR   GO; GO:0038023; F:signaling receptor activity; IEA:InterPro.
DR   CDD; cd13685; PBP2_iGluR_non_NMDA_like; 1.
DR   Gene3D; 1.10.287.70; -; 1.
DR   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR   InterPro; IPR019594; Glu/Gly-bd.
DR   InterPro; IPR001508; Iono_Glu_rcpt_met.
DR   InterPro; IPR015683; Ionotropic_Glu_rcpt.
DR   InterPro; IPR001320; Iontro_rcpt_C.
DR   PANTHER; PTHR18966:SF565; GLUTAMATE RECEPTOR; 1.
DR   PANTHER; PTHR18966; IONOTROPIC GLUTAMATE 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; SSF53850; Periplasmic binding protein-like II; 1.
DR   SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW   ECO:0000256|RuleBase:RU367118};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Ion channel {ECO:0000256|ARBA:ARBA00023303, ECO:0000256|RuleBase:RU367118};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW   ECO:0000256|RuleBase:RU367118};
KW   Ligand-gated ion channel {ECO:0000256|ARBA:ARBA00023286,
KW   ECO:0000256|RuleBase:RU367118};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU367118};
KW   Postsynaptic cell membrane {ECO:0000256|RuleBase:RU367118};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU367118};
KW   Signal {ECO:0000256|RuleBase:RU367118};
KW   Synapse {ECO:0000256|RuleBase:RU367118};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU367118};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU367118};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU367118}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT   CHAIN           21..459
FT                   /note="Glutamate receptor"
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT                   /id="PRO_5027157141"
FT   TRANSMEM        147..165
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT   TRANSMEM        216..236
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT   TRANSMEM        396..418
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT   DOMAIN          24..377
FT                   /note="Ionotropic glutamate receptor C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00079"
FT   DOMAIN          34..90
FT                   /note="Ionotropic glutamate receptor L-glutamate and
FT                   glycine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00918"
SQ   SEQUENCE   459 AA;  50494 MW;  2D4B6E6E4FE6CA79 CRC64;
     MTPLGLVLVS SALLAGLCAA GPNVLKVTTI KEEPYAMSKG SELEGFCIDL LSAIAKKLDF
     KYDVKLVKDG RYGKTDDSGN WNGMIGEVVR GEADIAVAPL TLTAKRETAV DMTKPFMQTG
     LSFVLRKDLV SDDSQFFSLL SLFSTEMWMG VLVAYLLTSV CIFLVSRISP CEWKQPEKEE
     NSFTLSHSFW YTMGAMTLQG AGPHPKALSG RVITSIWWLF SLVLLACYFA NLSLWLHSDN
     QQQSIKSFED LANQNLIEYG TIKDSSSFNF FKNSDNPTHH RIYEHIKNAQ SYSLNAEEGF
     RRALKGNYAF IGESVSLDLA VARYCNYLTR APEIIGMRGY SIAAPLGSPL VKNLSVAILN
     LSESGELDYF RSKWWASSCI AKNGKSAPLK PTSLKGIFLL LALGLGLGLF LALMELAAKS
     RKTANSQQKS CCSVMSAELS QRFRGGEAMT PEPSEKSKA
//
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