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Database: UniProt
Entry: A0A218UG42_9PASE
LinkDB: A0A218UG42_9PASE
Original site: A0A218UG42_9PASE 
ID   A0A218UG42_9PASE        Unreviewed;       883 AA.
AC   A0A218UG42;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Glutamate receptor {ECO:0000256|RuleBase:RU367118};
GN   Name=GRIA2 {ECO:0000313|EMBL:OWK52705.1};
GN   ORFNames=RLOC_00014100 {ECO:0000313|EMBL:OWK52705.1};
OS   Lonchura striata domestica (Bengalese finch).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC   Estrildinae; Lonchura.
OX   NCBI_TaxID=299123 {ECO:0000313|EMBL:OWK52705.1, ECO:0000313|Proteomes:UP000197619};
RN   [1] {ECO:0000313|EMBL:OWK52705.1, ECO:0000313|Proteomes:UP000197619}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=White83orange57 {ECO:0000313|EMBL:OWK52705.1};
RA   Colquitt B.M., Brainard M.S.;
RT   "Genome of assembly of the Bengalese finch, Lonchura striata domestica.";
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
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}. Endoplasmic
CC       reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane
CC       protein {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}. Postsynaptic density membrane
CC       {ECO:0000256|ARBA:ARBA00037872}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00037872}.
CC   -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1)
CC       family. GRIA2 subfamily. {ECO:0000256|ARBA:ARBA00037989}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OWK52705.1}.
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DR   EMBL; MUZQ01000328; OWK52705.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A218UG42; -.
DR   STRING; 299123.ENSLSDP00000008332; -.
DR   Proteomes; UP000197619; Unassembled WGS sequence.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0098839; C:postsynaptic density membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0022824; F:transmitter-gated monoatomic ion channel activity; IEA:UniProt.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:UniProt.
DR   CDD; cd06389; PBP1_iGluR_AMPA_GluR2; 1.
DR   CDD; cd13715; PBP2_iGluR_AMPA; 1.
DR   Gene3D; 1.10.287.70; -; 2.
DR   Gene3D; 3.40.50.2300; -; 2.
DR   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR   InterPro; IPR001828; ANF_lig-bd_rcpt.
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   InterPro; IPR028082; Peripla_BP_I.
DR   InterPro; IPR001638; Solute-binding_3/MltF_N.
DR   PANTHER; PTHR18966:SF99; GLUTAMATE RECEPTOR 2; 1.
DR   PANTHER; PTHR18966; IONOTROPIC GLUTAMATE RECEPTOR; 1.
DR   Pfam; PF01094; ANF_receptor; 1.
DR   Pfam; PF00060; Lig_chan; 1.
DR   Pfam; PF10613; Lig_chan-Glu_bd; 1.
DR   Pfam; PF00497; SBP_bac_3; 1.
DR   PRINTS; PR00177; NMDARECEPTOR.
DR   SMART; SM00918; Lig_chan-Glu_bd; 1.
DR   SMART; SM00079; PBPe; 1.
DR   SUPFAM; SSF53822; Periplasmic binding protein-like I; 1.
DR   SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR   SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW   ECO:0000256|RuleBase:RU367118};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
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   Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU367118};
KW   Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW   Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00023257,
KW   ECO:0000256|RuleBase:RU367118};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU367118};
KW   Reference proteome {ECO:0000313|Proteomes:UP000197619};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU367118};
KW   Synapse {ECO:0000256|ARBA:ARBA00023018, 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};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT   CHAIN           25..883
FT                   /note="Glutamate receptor"
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT                   /id="PRO_5027155334"
FT   TRANSMEM        542..564
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT   TRANSMEM        625..647
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT   TRANSMEM        815..837
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT   DOMAIN          415..790
FT                   /note="Ionotropic glutamate receptor C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00079"
FT   DOMAIN          425..490
FT                   /note="Ionotropic glutamate receptor L-glutamate and
FT                   glycine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00918"
SQ   SEQUENCE   883 AA;  98846 MW;  3FD16EC7E5BDE777 CRC64;
     MQKIMHISVF LAPVLWGLIW GVNSNSIQIG GLFPRGADQE YSAFRVGMVQ YSTSEFRLTP
     HIDNLEVANS FAVTNAFCSQ FSRGVFAIFG FYDKKSVNTI TSFCGTLHVS FITPSFPTDG
     THPFVIQMRP DLKGALLSLI EYYQWTKFAY LYDSDRGLST LQAVLDSAAE KKWQVTAINV
     GNINNERKDE TYRSLFQDLE VKKERRVILD CERDKVNDIV DQVITIGKHV KGYHYIIANL
     GFTDGDLSKI QFGGANVSGF QIVDYDDPVV SKFIQRWSTL EEKEYPGAHT STIKYTSALT
     YDAVQVMTEA FRNLRKQRIE ISRRGNAGDC LANPAVPWGH GVEIERALKQ VQVEGLTGNI
     KFDQNGKRIN FTINVMELKS TGPRKIGYWS EVDKMVVNPL DGPLGNESSG LENKTIIVTT
     ILESPYVMMK KNHEMLEGND RYEGYCVDLA TEIAKHCGFK YKLTIVGDGK YGARDADTKI
     WNGMVGELVY GKADIAIAPL TITLVREEVI DFSKPFMSLG ISIMIKKPQK SKPGVFSFLD
     PLAYEIWMCI VFAYIGVSVV LFLVSRFSPY EWHTEEFEDG RETQTNESTN EFGIFNSLWF
     SLGAFMQQGC DISPRSLSGR IVGGVWWFFT LIIISSYTAN LAAFLTVERM VSPIESAEDL
     SKQTEIAYGT LDSGSTKEFF RRSKIAVFDK MWTYMKSAEP SVFVRTTAEG VARVRKSKGK
     YAYLLESTMN EYIEQRKPCD TMKVGGNLDS KGYGIATPKG SSLRNAVNLA VLKLNEQGLL
     DKLKNKWWYD KGECGSGGGD SKEKTSALSL SNVAGVFYIL VGGLGLAMLV ALIEFCYKSR
     AEAKRMKVAK NAQNINPTSS QNSQNFATYK EGYNVYGIES VKI
//
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