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Database: UniProt
Entry: A0A093R974_PYGAD
LinkDB: A0A093R974_PYGAD
Original site: A0A093R974_PYGAD 
ID   A0A093R974_PYGAD        Unreviewed;      1320 AA.
AC   A0A093R974;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=Glutamate receptor {ECO:0000256|RuleBase:RU367118};
DE   Flags: Fragment;
GN   ORFNames=AS28_14473 {ECO:0000313|EMBL:KFW67584.1};
OS   Pygoscelis adeliae (Adelie penguin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae; Pygoscelis.
OX   NCBI_TaxID=9238 {ECO:0000313|EMBL:KFW67584.1, ECO:0000313|Proteomes:UP000054081};
RN   [1] {ECO:0000313|EMBL:KFW67584.1, ECO:0000313|Proteomes:UP000054081}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_AS28 {ECO:0000313|EMBL:KFW67584.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) 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|ARBA:ARBA00034104,
CC       ECO:0000256|RuleBase:RU367118}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00034104}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}. Synaptic cell membrane
CC       {ECO:0000256|ARBA:ARBA00034099}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00034099}.
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; KL225117; KFW67584.1; -; Genomic_DNA.
DR   STRING; 9238.A0A093R974; -.
DR   Proteomes; UP000054081; Unassembled WGS sequence.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004970; F:glutamate-gated receptor activity; IEA:UniProt.
DR   GO; GO:0022890; F:inorganic cation transmembrane transporter activity; IEA:UniProt.
DR   CDD; cd13718; PBP2_iGluR_NMDA_Nr2; 1.
DR   Gene3D; 3.40.50.2300; -; 2.
DR   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 3.
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; IPR018884; NMDAR2_C.
DR   InterPro; IPR028082; Peripla_BP_I.
DR   InterPro; IPR001638; Solute-binding_3/MltF_N.
DR   PANTHER; PTHR18966:SF407; GLUTAMATE RECEPTOR IONOTROPIC, NMDA 2A; 1.
DR   PANTHER; PTHR18966; IONOTROPIC GLUTAMATE RECEPTOR; 1.
DR   Pfam; PF00060; Lig_chan; 1.
DR   Pfam; PF10613; Lig_chan-Glu_bd; 1.
DR   Pfam; PF10565; NMDAR2_C; 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.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW   ECO:0000256|RuleBase:RU367118};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
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|ARBA:ARBA00023257,
KW   ECO:0000256|RuleBase:RU367118};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU367118};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054081};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
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   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   TRANSMEM        416..438
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT   TRANSMEM        488..510
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT   TRANSMEM        679..702
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT   DOMAIN          290..657
FT                   /note="Ionotropic glutamate receptor C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00079"
FT   DOMAIN          298..361
FT                   /note="Ionotropic glutamate receptor L-glutamate and
FT                   glycine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00918"
FT   REGION          862..941
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        879..904
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFW67584.1"
FT   NON_TER         1320
FT                   /evidence="ECO:0000313|EMBL:KFW67584.1"
SQ   SEQUENCE   1320 AA;  150483 MW;  BB52C4BFB5A090DE CRC64;
     STFFQFGASI QQEAIVMLKI MQDYDWHVFS LVTTTFPGYQ DFINVIKTTV ENSFVGWDMQ
     NIIVLDTAFG DAKTQIQLKK IHSSVILLYC SKDEAVYILD EARSLGLTGY DFFWIVPSLV
     SGNTEITPKE FPSGLISASY DEWDYSLEAR VRDGLGIIAT AASAMLEKYS FIPEAKTSCY
     GQLEKNDRPS HTLHKFMMNV TWEGKDLSFT ADGYQAHPRL VVIVLNNDRE WEKVGKWENN
     SLSLKYSVWP RYSSFADSDP DDNHLSIVTL EEAPFVIVED VDPLMESCQK NTVPCRKFVK
     INNSTNEGTN VKKCCKGFCI DILKKLSKTV KFTYDLYLVT NGKHGKKVNN VWNGMIGEVV
     YHRAVMAVGS LTINEERSEV VDFSVPFVET GISVMVSRSN GTVSPSAFLE PFSASVWVMM
     FVMLLIVSAM AVFIFEYFSP VGYNRNLAQG RDPHGPSFTI GKAVWLLWGL VFNNSVPVQN
     PKGTTSKIMV SVWAFFAVIF LASYTANLAA FMIQEEFVDQ VTGLSDKKFQ RPYDYSPPFR
     FGTVPNGSTE RNIRNNYPDM HLYMTKYNQK GVEDALVSLK TGKLDAFIYD AAVLNYKAGR
     DEGCKLVTIG SGYIFATTGY GIALQKGSPW KRQIDLALLQ FVGDGEMEEL ETLWLTGICH
     NEKNEVMSSQ LDIDNMAGVF YMLAAAMALS LITFVWEHLF YWKLRFCFTG VCSDRPGLLF
     SISRGIYSCI HGVHIEEKKK SPDFTLTNSQ TNMLKLLRTA KNMTNINPSR INSPKRTADF
     IQRGSLIMDM VMDKGNLIFS DNRSFQTKDN FFGDNMSELQ TLPGNRHKDN LNNYVFQGQH
     PLTLNESNPN TVEVAVTAEA KVNSRPRQLW RKSVESLRQE SVRQSQGSQR ENGSDENRQL
     SVKSQRYLPE EIVHSDVSET SSRATCHMEP ENNNKHHKTK DNFKKRTVAS KYPKDCSEVE
     LTYLKTKQSS PRDKIYTIDA DKEPGFRLDT PQYIENIVLP ETIEFPDVYQ DHNDNYRKAE
     HADRTPLHNE DSLPNNDQYK LYAKHYTLKD KNASLVDMND RYRQNSTHCR SCLSNLPTYA
     GHYSSRSPYK CDACLRMGNL YDIEEDQMLQ DTTNLSLPEE IDEHSWSQNN ALQYHKKNKL
     RISRQHSFDN IADKSREIDI GRPSRSISLK EREKFLQSSP YASMFSVPSS KLLSNKTSLL
     THALEDSKRS KSLYPVHSDD NPFLHSYGDD QHLSLRRSPA DLYKHSLPTR GRNDNYLRSS
     IKSTASYCSR DGRIHNDMYI SEHVLPYVAN RNSLYSTPRV LNSCSNRRVY KKRPSIESDV
//
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