ID A0A484BII3_DRONA Unreviewed; 980 AA.
AC A0A484BII3;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Glutamate [NMDA] receptor subunit 1 {ECO:0000256|ARBA:ARBA00015895};
GN ORFNames=AWZ03_006010 {ECO:0000313|EMBL:TDG47571.1};
OS Drosophila navojoa (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7232 {ECO:0000313|EMBL:TDG47571.1, ECO:0000313|Proteomes:UP000295192};
RN [1] {ECO:0000313|EMBL:TDG47571.1, ECO:0000313|Proteomes:UP000295192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Navoj_Jal97 {ECO:0000313|EMBL:TDG47571.1};
RC TISSUE=Whole organism {ECO:0000313|EMBL:TDG47571.1};
RX PubMed=30423125; DOI=.1093/jhered/esy059;
RA Vanderlinde T., Dupim E.G., Nazario-Yepiz N.O., Carvalho A.B.;
RT "An Improved Genome Assembly for Drosophila navojoa, the Basal Species in
RT the mojavensis Cluster.";
RL J. Hered. 110:118-123(2019).
CC -!- FUNCTION: NMDA receptor subtype of glutamate-gated ion channels with
CC high calcium permeability and voltage-dependent sensitivity to
CC magnesium. Mediated by glycine. This protein plays a key role in
CC synaptic plasticity, synaptogenesis, excitotoxicity, memory acquisition
CC and learning. It mediates neuronal functions in glutamate
CC neurotransmission. Is involved in the cell surface targeting of NMDA
CC receptors. Plays a role in associative learning and in long-term memory
CC consolidation. {ECO:0000256|ARBA:ARBA00024675}.
CC -!- SUBUNIT: Forms a heteromeric NMDA channel with Nmdar2.
CC {ECO:0000256|ARBA:ARBA00011106}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}. Postsynaptic cell membrane
CC {ECO:0000256|ARBA:ARBA00034100}. Postsynaptic density
CC {ECO:0000256|ARBA:ARBA00034105}. Synaptic cell membrane
CC {ECO:0000256|ARBA:ARBA00034109}.
CC -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1)
CC family. {ECO:0000256|ARBA:ARBA00008685}.
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:TDG47571.1}.
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DR EMBL; LSRL02000042; TDG47571.1; -; Genomic_DNA.
DR RefSeq; XP_017963419.1; XM_018107930.1.
DR AlphaFoldDB; A0A484BII3; -.
DR STRING; 7232.A0A484BII3; -.
DR GeneID; 108656036; -.
DR KEGG; dnv:108656036; -.
DR OMA; AYKKHQI; -.
DR OrthoDB; 1034721at2759; -.
DR Proteomes; UP000295192; Unassembled WGS sequence.
DR GO; GO:0017146; C:NMDA selective glutamate receptor complex; IEA:UniProt.
DR GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
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 GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:UniProt.
DR GO; GO:0042221; P:response to chemical; IEA:UniProt.
DR CDD; cd06379; PBP1_iGluR_NMDA_NR1; 1.
DR CDD; cd13719; PBP2_iGluR_NMDA_Nr1; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 3.
DR InterPro; IPR001828; ANF_lig-bd_rcpt.
DR InterPro; IPR018882; CaM-bd_C0_NMDA_rcpt_NR1.
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:SF377; GLUTAMATE RECEPTOR IONOTROPIC, NMDA 1; 1.
DR PANTHER; PTHR18966; IONOTROPIC GLUTAMATE RECEPTOR; 1.
DR Pfam; PF01094; ANF_receptor; 2.
DR Pfam; PF10562; CaM_bdg_C0; 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 Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Ion channel {ECO:0000256|ARBA:ARBA00023303};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Ligand-gated ion channel {ECO:0000256|ARBA:ARBA00023286};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00023257};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000295192};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Synapse {ECO:0000256|ARBA:ARBA00023018};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..980
FT /note="Glutamate [NMDA] receptor subunit 1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019780720"
FT TRANSMEM 573..591
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 643..669
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 829..853
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 435..807
FT /note="Ionotropic glutamate receptor C-terminal"
FT /evidence="ECO:0000259|SMART:SM00079"
FT DOMAIN 449..518
FT /note="Ionotropic glutamate receptor L-glutamate and
FT glycine-binding"
FT /evidence="ECO:0000259|SMART:SM00918"
FT REGION 948..980
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 980 AA; 110164 MW; 8B4CF420841A1D2A CRC64;
MAAALAYRWL LCAAGIVNVL PIGGQRHTAS DNPSTYNIGG VLSSSESEEH FRTTIAHLNF
DQQYVPRKVT YYDKTIRMDK NPIKTVFNVC DKLIEKRVYA VVVSHGQTSG DLSPAAVSYT
TGFYSIPVIG ISSRDAAFSD KNIHVSFLRT VPPYYHQADV WLEMLSHFLY TKVIIIHSSD
TDGRAILGRF QTTSQTYYDD VDARATVELI VEFEPKLESF TEHLIDMKTA QSRVYLVYAS
TEDAQVIFRD AAEYNMTGEG HVWIVTEQAL HAKNTPDGAL GLQLEHAHSD KGHIRDSVYV
LASAIKEMIS NETIAEAPKD CGDSAVNWES GKRLFQYLKS RNITGETGQV AFDDNGDRIY
AGYDVINIRD HQKQHIVGKF SYDSLKAKMI MRINDSEIIW GGKQRRKPEG IMIPTHLKVL
TIEEKPFVYV RRMGDDEFRC EPDERPCPLF NASDATANEF CCRGYCIDLL IELSKRINFT
YDLALSPDGQ FGHYILKNNT GAMTLRKEWT GLIGELVNER ADMIVAPLTI NPERAEYIEF
SKPFKYQGIT ILEKKPSRSS TLVSFLQPFS NTLWILVMVS VHVVALVLYL LDRFSPFGRF
KLSHSDSNEE KALNLSSAIW FAWGVLLNSG IGEGTPRSFS ARVLGMVWAG FAMIIVASYT
ANLAAFLVLE RPKTKLSGIN DARLRNTMEN LTCATVKGSS VDMYFRRQVE LSNMYRTMES
NNYVTAEQAI QDVKKGKLMA FIWDSSRLEY EASKDCELVT AGELFGRSGY GIGLQKGSPW
TDAVTLAILE FHESGFMEKL DKQWIFHGHV QQNCELFEKT PNTLGLKNMA GVFILVGVGI
AGGVGLIIIE VIYKKHQVKK QKRLDIARHA ADKWRGTIEK RKTIRASLAM QRQYNVGLMA
SHAPGTISLA VDKRRYPRLG QRLGPERAWP GDAADVLRIR RPYDLTKSGQ LGLGRTRPQQ
NPLPPRYSPG YTSDVSHLVV
//
