ID A0A182N9Z4_9DIPT Unreviewed; 963 AA.
AC A0A182N9Z4;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Glutamate [NMDA] receptor subunit 1 {ECO:0000256|ARBA:ARBA00015895};
OS Anopheles dirus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7168 {ECO:0000313|EnsemblMetazoa:ADIR004470-PA, ECO:0000313|Proteomes:UP000075884};
RN [1] {ECO:0000313|Proteomes:UP000075884}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WRAIR2 {ECO:0000313|Proteomes:UP000075884};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Walton C., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles dirus WRAIR2.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:ADIR004470-PA}
RP IDENTIFICATION.
RC STRAIN=WRAIR2 {ECO:0000313|EnsemblMetazoa:ADIR004470-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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}.
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DR AlphaFoldDB; A0A182N9Z4; -.
DR STRING; 7168.A0A182N9Z4; -.
DR EnsemblMetazoa; ADIR004470-RA; ADIR004470-PA; ADIR004470.
DR VEuPathDB; VectorBase:ADIR004470; -.
DR OrthoDB; 1034721at2759; -.
DR Proteomes; UP000075884; 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; 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; 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; 1.
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 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..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..963
FT /note="Glutamate [NMDA] receptor subunit 1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008129550"
FT TRANSMEM 574..592
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 644..670
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 829..853
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 441..808
FT /note="Ionotropic glutamate receptor C-terminal"
FT /evidence="ECO:0000259|SMART:SM00079"
FT DOMAIN 448..519
FT /note="Ionotropic glutamate receptor L-glutamate and
FT glycine-binding"
FT /evidence="ECO:0000259|SMART:SM00918"
FT REGION 928..951
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 963 AA; 108130 MW; 3A5D10094EFFA351 CRC64;
MKLTRMLPAS CLLLSLMIPQ ALLAQKPASS ESPSYYNIGG VLSNNESESH FGTVIAHLNF
DQQYVPRGTT YYDKTIRIDK NPIKTALNVC KHLISRRVYA VVVSHEPTGD LSPAAVSYTS
GFYQIPVIGI SSREAAFSDK NIHVSFLRTV PPYYHQADVW LEILSHFGYT KVIIIHSSDT
DGRAVLGRFQ TTSQTNYDDI DVRATVESIV EFEPKLDSFS SYLMDMKTAQ SRVYLLYASQ
EDAYVIFRDA AIHNMTEYGH IWIVTEQALS ANNTPTGIIG LKLNNAENET DHIKDAIYIL
ASAIKEMTVN ETITEAPKDC DDSGVIWESG KRLFGYLKTR NIRGETGQVA FDDNGDRMYA
EYDVINVHEN HSFVKVGSFY YESEKRKMRL KINDSSITWP GNTGKKPEGI MIPTHLKVLT
IEEKPFVYAR KLLDDEIDCA DDEVVCPHFN ITNGNEQEYC CKGYCIDLLK ALAQRINFTY
DLALSPDGQF GHYQLKNHTT GIGTTVKKEW NGLIGELVAE RADLIVAPLT INPERAEFIE
FSKPFKYQGI TILEKKPSRS STLVSFLQPF SNTLWILVMV SVHVVALVLY LLDRFSPFGR
FKLSSNDGTE EDALNLSSAI WFAWGVLLNS GIGEGTPRSF SARVLGMVWA GFAMIIVASY
TANLAAFLVL ERPKTKLTGI NDARLRNTME NLTCATVKGS SVDMYFRRQV ELSNMYRTME
ANNYDTAEQA IQDVKDGKLM AFIWDSSRLE YEASKDCELV TAGELFGRSG YGVGLQKASP
WTDAVTLAIL DFHESGFMES LDKEWIFHGN VQQCEQFEKT PNTLGLKNMA GVFILVGAGI
VGGIGLIIIE VVYKKHQIKK QKKMEIARHA ADKWRGTIEK RKTLRASLAM QRQYNVGLNS
VSKSVSQNSE KTRYPILPPL PRTPERAWPK DKEYIVSRKS TSAGKPPPRY MPTYATDVSH
LIV
//
