ID W5LHC5_ASTMX Unreviewed; 1511 AA.
AC W5LHC5;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Glutamate receptor {ECO:0000256|RuleBase:RU367118};
OS Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Characidae; Astyanax.
OX NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000019237.2, ECO:0000313|Proteomes:UP000018467};
RN [1] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA Jeffery W., Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX PubMed=25329095; DOI=10.1038/ncomms6307;
RA McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA Yoshizawa M., Warren W.C.;
RT "The cavefish genome reveals candidate genes for eye loss.";
RL Nat. Commun. 5:5307-5307(2014).
RN [3] {ECO:0000313|Ensembl:ENSAMXP00000019237.2}
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. NR2B/GRIN2B subfamily. {ECO:0000256|ARBA:ARBA00038189}.
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DR STRING; 7994.ENSAMXP00000019237; -.
DR Ensembl; ENSAMXT00000019237.2; ENSAMXP00000019237.2; ENSAMXG00000018685.2.
DR eggNOG; KOG1053; Eukaryota.
DR GeneTree; ENSGT00940000155964; -.
DR HOGENOM; CLU_002039_3_2_1; -.
DR InParanoid; W5LHC5; -.
DR Proteomes; UP000018467; Unassembled WGS sequence.
DR Bgee; ENSAMXG00000018685; Expressed in brain.
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; cd13718; PBP2_iGluR_NMDA_Nr2; 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; 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; 3.
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 Reference proteome {ECO:0000313|Proteomes:UP000018467};
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 513..535
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT TRANSMEM 585..607
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT TRANSMEM 776..799
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT DOMAIN 401..754
FT /note="Ionotropic glutamate receptor C-terminal"
FT /evidence="ECO:0000259|SMART:SM00079"
FT DOMAIN 404..458
FT /note="Ionotropic glutamate receptor L-glutamate and
FT glycine-binding"
FT /evidence="ECO:0000259|SMART:SM00918"
FT REGION 1082..1113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1126..1157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1231..1251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1284..1311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1088..1113
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1236..1250
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1511 AA; 164851 MW; 48EFC18CEA6DDC83 CRC64;
TPAENSCGKS VGSLDMSVLK APPLPPPTPL LPGRVSAVTS LKPNQGNGSV HFGPPGGVDS
RVAGFDVEPT PFIFMYSYSY CGLCVLQDDH SMFFQFGPSI EQQASVMLNI MEEYDWYIFS
IVTTYYPGYQ DFVNRIRSTI ENSFVGWELE EVILLDMSVD DGDSKIQNQL KKLQSPVILL
YCTKEEAATI FEVAHSVGLT GYGYTWIVPA LVAGDADNVP NVFPTGLISV SYDEWDYGLE
ARVRDAVAII AMATSTMMLD RGPHTLLKSG CLGAPDKKGT KGGNPNEVLR YLMNVTFEGR
NLSFSEDGYQ MHPKLVIILL DKERQWDRVG KWENGSLTMK YHVWPRFELY SDAEEREDDH
LSIVTLEEAP FVIVEDVDPL SGTCMRNTVP CRKQLKTQNQ TGDSGIYIKR CCKGFCIDIL
KKIAKTVKFT YDLYLVTNGK HGKKINGTWN GMVGEVVFKN AHMAVGSLTI NEERSEVIDF
SVPFIETGIS VMVSRSNGTV SPSAFLEPFS ADVWVMMFVM LLIVSAVAVF VFEYFSPVGY
NRCLADGREP GGPSFTIGKA IWLLWGLVFN NSVPVQNPKG TTSKIMVSVW AFFAVIFLAS
YTANLAAFMI QEEYVDQVTG LSDKKFQRPN DFSPPFRFGT VPNGSTERNI RNNYKEMHSY
MTSFHQKNVN EALHSLKTGK LDAFIYDAAV LNYMAGRDEG CKLVTIGSGY IFATTGYGIA
IQKDSGWKRA VDLAILQLFG DGEMEELEAL WLTGICHNEK NEVMSSQLDV DNMAGVFYML
GAAMALSLIT FIAEHLFYWQ LRFCFMGVCS GKPGVTFSIS RGIYSCIHGV QIEENKSGLN
SPSATMNMNM NNTHSNILRL LRTAKNMTSV PGVNGSPHSA LDYGHRESAV YDISEHRRSL
VGHTDCKPPP PYLPEDNMFS DYVSDVERTF GNMHLKDSNL YQDHYLHHHG GTGSALALGM
SGPLPNRPRS LGSASSLEGG MYDCDSLGGG VAPIFTTQPR QSLTHRNREK FDLIAGHPTQ
SSFKSGLPDL YGKFSFKGGA SSSGFIAGHD RYCGGGGAGS GGDDGNIRSD VSDISTHTVT
YGNLEGNAKR RKQYRDSLKK RPASAKSRRE QDEIELGFRR RTHHTIHHHH HHNHPVTQGH
RSATPPVERK SQRGANSSSY VFRDKENLRD FYMDQFRSKE GASPWEHLDL SDAPGMVGGG
GSPGQQGHAC WEKSIGGVGG LAAAGGVGGS GGGGGGGSGQ VSSRPSSATC KRCDSCKKPG
NLYDISEDNH LLLDQLGGKF VLEGGKGGGG GGGGGGGGAQ TQAQRRKFGP GGRVLRRQHS
YDTFVDLQKE GAGRMGGSGF GGGGASMLPP PRSVSLKDKD RYMEGASPYA QMFERYAGGE
RETGFFAGGD RGKGGGSSFS LFRGGEGGLH RRSVGERDMR DRDRGVGTYS LSKSLYPDKV
NQNPFIPTFG DDQCLLHGAK SYYLLNNNRA DFRGSMGVTS YLPASASAGR PFNGSSNGHV
YEKLSSIESD V
//
