ID A0A3B3U5Y4_9TELE Unreviewed; 1596 AA.
AC A0A3B3U5Y4;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Glutamate receptor {ECO:0000256|RuleBase:RU367118};
OS Poecilia latipinna (sailfin molly).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48699 {ECO:0000313|Ensembl:ENSPLAP00000008057.1, ECO:0000313|Proteomes:UP000261500};
RN [1] {ECO:0000313|Ensembl:ENSPLAP00000008057.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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. NR2B/GRIN2B subfamily. {ECO:0000256|ARBA:ARBA00038189}.
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DR Ensembl; ENSPLAT00000003526.1; ENSPLAP00000008057.1; ENSPLAG00000010849.1.
DR GeneTree; ENSGT00940000155964; -.
DR Proteomes; UP000261500; Unplaced.
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 GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd06378; PBP1_iGluR_NMDA_NR2; 1.
DR CDD; cd13718; PBP2_iGluR_NMDA_Nr2; 1.
DR Gene3D; 3.40.50.2300; -; 4.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 3.
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 InterPro; IPR001638; Solute-binding_3/MltF_N.
DR PANTHER; PTHR18966:SF382; GLUTAMATE RECEPTOR IONOTROPIC, NMDA 2B; 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 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 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00023257,
KW ECO:0000256|RuleBase:RU367118};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU367118};
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}.
FT TRANSMEM 498..520
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT TRANSMEM 570..595
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT TRANSMEM 758..781
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT DOMAIN 371..736
FT /note="Ionotropic glutamate receptor C-terminal"
FT /evidence="ECO:0000259|SMART:SM00079"
FT DOMAIN 389..443
FT /note="Ionotropic glutamate receptor L-glutamate and
FT glycine-binding"
FT /evidence="ECO:0000259|SMART:SM00918"
FT REGION 934..960
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1061..1145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1163..1186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1308..1327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1556..1582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1071..1104
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1105..1119
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1308..1323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1596 AA; 173741 MW; BEBCFDEA59956FA3 CRC64;
SPGVNNPLLT LSLPPNAPKL ISSLSIAVIL VGNSSEVTLG AGLEKEDFLH IPYPPKVEVV
TMNETDPKSI INRICAQMMR NSLQGVVFGD DTDQEAIAQI LDFISAQTHI PILGIRGGSS
MVMAAKDDHS MFFQFGPSIE QQASVMLNIM EEYDWYIFSI VTTYYPGYQD FINKVNAQKD
ALNSFVGWEL EEVIILDMSV DDGDSKIQNQ MKKLQSPVIL LYCTKEEATT IFEVAHSVGL
TGYGYTWIVP SLVAGDADHV PSVFPIGMQR TINSYQYVMN VTFEGRNLSF SEKGHQMFPK
LVIILLDKDR QWDRVGKWER GSLTMRYHVW PRFELYSDVE EREDHLSIVT LEEAPFVIVE
DVDPLSGTCM RNTVPCRKQL KLSNHTGDSG IYIKRCCKGF CIDILKKIAK TVKFTYDLYL
VTNGKHGKKV NGTWNGMVGE VVAKNAHMAV GSLTINEERS EVIDFSVPFI ETGISVMVSR
SNGTVSPSAF LEPFSADVWV MMFVMLLIVS AVAVFVFEYF SPVGYNRCLA DGREPGGPSF
TIGKAIWLLW GLVFNNSVPV QNPKGTTSKI MVSVWAFFAV IFLASYTANL AAFMIQEEYV
DQVSGLSDKK FQKPNEFSPP FRFGTVPNGS TERNIRNNYR DMHAYMTSFH QKNVDEALHS
LKTGKLDAFI YDAAVLNYMA GRDEGCKLVT IGSGKVFAST GYGIAIQKDS GWKRAVDLAI
LMLFGDGKFE ALWLTGICHN EKNEVMSSQL DVDNMAGVFY MLGAAMVLSL ITFICEHLFY
WQLRFCFMGV CSGKPGVTFS ISRGIYSCIH GVQIEENKST IDSPSSTIKK NMNNTHSNIL
RLLRTAKDMT AVPGVNGSPH AALEYSHSSR EAAIYDIQKH RHSLVGHPAD CKSAPPYLPE
DPMFSDYISE VERTFGNLPL KDSNLYQDHY RHHHPASALG MSGPPPNRPR SLGSASSLEG
GMFDADSLGG GVAPIFTTQP RPSMTHRNTS KFDLIAGHTA ADTNQGGFKG SNVYGRFSFK
GGASSTGLIG GHDRYCGGGG GGSGGDDGNI RSDVSDISTH TVTYGNLEGS TKRRKQYRDS
LKKRPASAKV RREQDEIELN AFRKRPHHHT VHHHFPHGPL AHRPVSPPLE RKRGGGTGNS
SPYIFRKDKD NLRDFYADQF RSKEGKAKWE QEGGSGGSGA GGGSGGGICK SLVPVEDFLK
GKGKKTECKG GIGGMSAGQQ AHTCWEKGVS GLGGGGIAGG DWECRNCHTV CHHSGGGGST
CSASGVGGSG SRPSSATLCK RCDSCKIQPS NLYNISEDNN MIFSGVKSSI GPSQTQTQTQ
RRKLGPGGKV LRRQHSYDTF VDLQREGAGR MGGVGGGIGG QFVQPRSVSL KEKDRYMEGP
SPYAHMFERY LGERESPMFG GIGGDRAAGG SSFSLYRGGE GGLHRRSVGE RDLRDRDRNM
MGGGGCGGGG GNRGAGTYSL SKSLYPDKVN QNPFIPTFGD DQCLLHGAKP YYIKKPQTQQ
QQLLNNSRGG GDFRGSMGAT SYLPASATAG VMSNVATRYP KELCLGGVGG PMGNHHGANK
LLPGGRDTLG LGQGQRPFNG ANGHVYEKLS SIESDV
//
