ID G3PWH0_GASAC Unreviewed; 1466 AA.
AC G3PWH0;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=Glutamate receptor {ECO:0000256|RuleBase:RU367118};
OS Gasterosteus aculeatus (Three-spined stickleback).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC Gasterosteus.
OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000021959.1, ECO:0000313|Proteomes:UP000007635};
RN [1] {ECO:0000313|Ensembl:ENSGACP00000021959.1, ECO:0000313|Proteomes:UP000007635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGACP00000021959.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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|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 STRING; 69293.ENSGACP00000021959; -.
DR Ensembl; ENSGACT00000022000.1; ENSGACP00000021959.1; ENSGACG00000016632.1.
DR eggNOG; KOG1053; Eukaryota.
DR GeneTree; ENSGT00940000156222; -.
DR InParanoid; G3PWH0; -.
DR OMA; FTHYHPQ; -.
DR TreeFam; TF314731; -.
DR Proteomes; UP000007635; Unassembled WGS sequence.
DR Bgee; ENSGACG00000016632; Expressed in telencephalon and 2 other cell types or tissues.
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 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; IPR018884; NMDAR2_C.
DR InterPro; IPR028082; Peripla_BP_I.
DR PANTHER; PTHR18966:SF407; GLUTAMATE RECEPTOR IONOTROPIC, NMDA 2A; 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; PF10565; NMDAR2_C; 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 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:UP000007635};
KW Signal {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 Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT CHAIN 21..1466
FT /note="Glutamate receptor"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT /id="PRO_5027151954"
FT TRANSMEM 620..642
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT TRANSMEM 810..833
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT DOMAIN 422..788
FT /note="Ionotropic glutamate receptor C-terminal"
FT /evidence="ECO:0000259|SMART:SM00079"
FT DOMAIN 430..493
FT /note="Ionotropic glutamate receptor L-glutamate and
FT glycine-binding"
FT /evidence="ECO:0000259|SMART:SM00918"
FT REGION 951..1126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1150..1184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1270..1294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1307..1382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 964..985
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1030..1047
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1084..1100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1150..1166
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1312..1328
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1356..1376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1466 AA; 161084 MW; BADF49B5C37EE49D CRC64;
MGAVGWTLLL LSQMMVPAAS QKPPGLSVGV IMGQTRHISD QDLRPARRPD DALDVSVVIL
RINQTDPKSV ITQVCELLTR TRLHGLVFAD GTDQEAISQI LDFLSVQTQL PVLGVYGGSS
MIMADKDESP RSSSSVRRLQ QEALLMLSIM EEYDWHVFSI VTSKFPGYQD FIGTLKITVD
HSFVRWDLQS VVTLDAVDGD PNSKSHIALK RIQSPVILLY CSKDEAVYIL EEARSLGLIG
AGYIWIVSSL TTGNPDFTPE VFPLGMISVS YDDWDYPLDT RVRDGVGIIS YAATAMLREK
GELPEAQSSC YSTPSDRSPG KLPPSALHMM HVWNEGRDLS FTPDGYQANP KLVVIVLNSE
RNWEKMGRWE NGTLSLMFPV WPRYNSHGDE DADENHLSIV TLEEKPFVIV DNVDILTGTC
VRNSVPCRKH VKDSNSTAGG SYIKQCCKGF CIDILKKIAR NVKFTYDLYL VTNGKHGKKI
NNMWNGMVGE VVYKKAVMAV GSLTINEERS EAIDFSVPFV ETGISVMVSR SNGTVSPSAF
LGKISSNTLM LVFKFELILT TSRRLIGGCF AGAGQNMKNL KGKHPHGPSF TIGKAVWLLW
GLVFNNSVPV QNPKGTTSKF IVSVWAFFAV IFLASYTANL AAFMIQEEFV DQVTGLSDKK
FQSPYSYSPP FRFGTVPNGS TERNIRKNYP DMHQYMTKYH QTGVTDALVT LKTGPLSKHF
IDKGILNILR AGRKNLISSS FAIKTNPKLL VCLQHYTPPP AGAETCRVLW IGLKQCEMEE
LEAQWLTGIC HSEKNEVMSS QLDVDNMAGV FYMLATAMGL SILTFISEHL FYWRLRYCFT
GVCTGRPGLL FTISRGIWSC IHGVHIDMKK KNPELDFSPQ ANMLHLLKSA KSMALSSPKR
NTVLLQPNIL DVMSGKGNSL HSLAPKGPGL YSNAAGPHSF LSLSGRHKNL LNNAAPFPGQ
KKAPPLQTSP NKPQLSITND NGPQGSKPRA LWKKSVETLK TQPAAASPGP SPVPSSGPGP
ATMKSQRYLP EEPPHSDMSE CSSRPPSHKD SDSVAAARAG GFKPINQLRK RGGAGGGGGS
KIYSIDSDQA SLQSAPPYQR DSQGGGDDHS YPPDLFPPDN TYSHTHTLSH QADAPILQLS
ASLLHHSHSA EADLHSLKDK NSKDKSAGSF DTPGAGQGTQ SVRPGHCRSC LTKLSGYSGL
YTVRSPGARC DACAHLGNLY DIREDHLHSH YSHPHAHPHG GDMFTHYLPQ SELGLHLQLS
RQHSYENVLP DGVPDRQSQL HSHLRGLSLP DRDRERELTL DEGAYANVLT MRSDRPFSSR
SPPSPSPSHH HSLDAPMALP RRSKSLFPDR PSHNPFLQSA PGTTQRDPSP QAVARMPQRS
SAHELYKQRM PLSLTLGNHG SHHNSQHGGL VDQQVFYPQQ EPPVVAYMVP PAASQPMSYV
TAPRASSAGG NRPRLYRRMP SIESDV
//
