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Database: UniProt
Entry: A0A493TMP2_ANAPP
LinkDB: A0A493TMP2_ANAPP
Original site: A0A493TMP2_ANAPP 
ID   A0A493TMP2_ANAPP        Unreviewed;       813 AA.
AC   A0A493TMP2;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Glutamate receptor {ECO:0000256|RuleBase:RU367118};
GN   Name=GRIA2 {ECO:0000313|Ensembl:ENSAPLP00000026870.1};
OS   Anas platyrhynchos platyrhynchos (Northern mallard).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC   Anatinae; Anas.
OX   NCBI_TaxID=8840 {ECO:0000313|Ensembl:ENSAPLP00000026870.1, ECO:0000313|Proteomes:UP000016666};
RN   [1] {ECO:0000313|Ensembl:ENSAPLP00000026870.1, ECO:0000313|Proteomes:UP000016666}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Hou Z.-C., Zhou Z.-K., Zhu F., Hou S.-S.;
RT   "A new Pekin duck reference genome.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSAPLP00000026870.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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}.
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DR   AlphaFoldDB; A0A493TMP2; -.
DR   Ensembl; ENSAPLT00000046791.1; ENSAPLP00000026870.1; ENSAPLG00000012953.2.
DR   GeneTree; ENSGT00940000156950; -.
DR   Proteomes; UP000016666; Chromosome 4.
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; -; 1.
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:UP000016666};
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..17
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT   CHAIN           18..813
FT                   /note="Glutamate receptor"
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT                   /id="PRO_5027148728"
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   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"
FT   REGION          794..813
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   813 AA;  91200 MW;  E1389C8A4AF6EF17 CRC64;
     MQKIMHISVF LAPVVWGLIW GVDSNSIQIG GLFPRGADQE YSAFRVGMVQ FSTSEFRLTP
     HIDNLEVANS FAVTNAFCSQ FSRGVFAIFG FYDKKSVNTI TSFCGTLHVS FITPSFPTDG
     THPFVIQMRP DLKGALLSLI EYYQWTKFAY LYDSDRGLST LQAVLDSAAE KKWQVTAINV
     GNINNDRKDE TYRSLFQDLE VKKERRVILD CERDKVNDIV DQVITIGKHV KGYHYIIANL
     GFTDGDLSKI QFGGANVSGF QIVDYDDPLV 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 SKNPSKSCSI ETQ
//
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