ID Q7PXM3_ANOGA Unreviewed; 966 AA.
AC Q7PXM3;
DT 15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT 23-OCT-2007, sequence version 3.
DT 27-MAR-2024, entry version 143.
DE RecName: Full=Glutamate [NMDA] receptor subunit 1 {ECO:0000256|ARBA:ARBA00015895};
GN Name=1281696 {ECO:0000313|EnsemblMetazoa:AGAP001478-PA};
GN ORFNames=AgaP_AGAP001478 {ECO:0000313|EMBL:EAA00817.3};
OS Anopheles gambiae (African malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7165 {ECO:0000313|EMBL:EAA00817.3};
RN [1] {ECO:0000313|EMBL:EAA00817.3, ECO:0000313|Proteomes:UP000007062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PEST {ECO:0000313|EMBL:EAA00817.3,
RC ECO:0000313|Proteomes:UP000007062};
RX PubMed=12364791; DOI=10.1126/science.1076181;
RA Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R.,
RA Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R.,
RA Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z.,
RA Kraft C.L., Abril J.F., Anthouard V., Arensburger P., Atkinson P.W.,
RA Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C.,
RA Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K.,
RA Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V.,
RA Dana A., Delcher A., Dew I., Evans C.A., Flanigan M.,
RA Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R.,
RA Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J.,
RA Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I.,
RA Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A.,
RA McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D.,
RA O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H.,
RA Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J.,
RA Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B.,
RA Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M.,
RA Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I.,
RA Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J.,
RA Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M.,
RA Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C.,
RA Collins F.H., Hoffman S.L.;
RT "The genome sequence of the malaria mosquito Anopheles gambiae.";
RL Science 298:129-149(2002).
RN [2] {ECO:0000313|EMBL:EAA00817.3}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PEST {ECO:0000313|EMBL:EAA00817.3};
RG The Anopheles Genome Sequencing Consortium;
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:EAA00817.3}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PEST {ECO:0000313|EMBL:EAA00817.3};
RX PubMed=14747013; DOI=10.1016/j.pt.2003.11.003;
RA Mongin E., Louis C., Holt R.A., Birney E., Collins F.H.;
RT "The Anopheles gambiae genome: an update.";
RL Trends Parasitol. 20:49-52(2004).
RN [4] {ECO:0000313|EMBL:EAA00817.3}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PEST {ECO:0000313|EMBL:EAA00817.3};
RX PubMed=17210077; DOI=10.1186/gb-2007-8-1-r5;
RA Sharakhova M.V., Hammond M.P., Lobo N.F., Krzywinski J., Unger M.F.,
RA Hillenmeyer M.E., Bruggner R.V., Birney E., Collins F.H.;
RT "Update of the Anopheles gambiae PEST genome assembly.";
RL Genome Biol. 8:R5.1-R5.13(2007).
RN [5] {ECO:0000313|EMBL:EAA00817.3}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PEST {ECO:0000313|EMBL:EAA00817.3};
RG VectorBase;
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000313|EnsemblMetazoa:AGAP001478-PA}
RP IDENTIFICATION.
RC STRAIN=PEST {ECO:0000313|EnsemblMetazoa:AGAP001478-PA};
RG EnsemblMetazoa;
RL Submitted (JAN-2021) 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 EMBL; AAAB01008987; EAA00817.3; -; Genomic_DNA.
DR RefSeq; XP_321646.3; XM_321646.3.
DR AlphaFoldDB; Q7PXM3; -.
DR STRING; 7165.Q7PXM3; -.
DR PaxDb; 7165-AGAP001478-PA; -.
DR EnsemblMetazoa; AGAP001478-RA; AGAP001478-PA; AGAP001478.
DR GeneID; 1281696; -.
DR KEGG; aga:AgaP_AGAP001478; -.
DR VEuPathDB; VectorBase:AGAP001478; -.
DR eggNOG; KOG4440; Eukaryota.
DR HOGENOM; CLU_007257_2_0_1; -.
DR InParanoid; Q7PXM3; -.
DR OMA; AYKKHQI; -.
DR OrthoDB; 1034721at2759; -.
DR Proteomes; UP000007062; Chromosome 2R.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0017146; C:NMDA selective glutamate receptor complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0015276; F:ligand-gated monoatomic ion channel activity; IBA:GO_Central.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0035235; P:ionotropic glutamate receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central.
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:UP000007062};
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..966
FT /note="Glutamate [NMDA] receptor subunit 1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014587970"
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"
SQ SEQUENCE 966 AA; 108433 MW; 2A50D983D30D4245 CRC64;
MKLTRMLPAS CMLLSLMIPQ ALLAQKPTGS ESPSYYNIGG VLSNNESESH FATVIAHLNF
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
EYDVINVHEK HSFVKVGSFH YDSEKRKMRL KINDSSITWP GNTGKKPEGI MIPTHLKVLT
IEEKPFVYAR KLLDDEIDCA DDEVVCPHFN ITNGNEQEYC CKGYCIDLLK ALAQRINFTY
DLALSPDGQF GHYQLKNHTT GIGTTVKKEW NGLIGELVAE RADLIVAPLT INPERAEFIE
FSKPFKYQGI TILEKKPSRS STLVSFLQPF SNTLWILVMV SVHVVALVLY LLDRFSPFGR
FKLSTTDGTE EDALNLSSAI WFAWGVLLNS GIGEGTPRSF SARVLGMVWA GFAMIIVASY
TANLAAFLVL ERPKTKLTGI NDARLRNTME NLTCATVKGS SVDMYFRRQV ELSNMYRTME
ANNYDTAEQA IQDVKDGKLM AFIWDSSRLE YEASKDCELV TAGELFGRSG YGVGLQKGSP
WTDAVTLAIL DFHESGFMES LDKEWIFHGN VQQCEQFEKT PNTLGLKNMA GVFILVGAGI
VGGIGLIIIE VVYKKHQIKK QKKMEIARHA ADKWRGTIEK RKTLRASLAM QRQYNVGLNS
VSKSVQSQNA EKSRYPILPP LPRTPERAWP KDKEYIVNRK NNSSGAGKPP PRYMPTYATD
VSHLIV
//
