ID W5MJC3_LEPOC Unreviewed; 903 AA.
AC W5MJC3;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Glutamate receptor {ECO:0000256|RuleBase:RU367118};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000008482.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000008482.1}
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|RuleBase:RU367118}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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 EMBL; AHAT01003060; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01003061; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015197117.1; XM_015341631.1.
DR AlphaFoldDB; W5MJC3; -.
DR Ensembl; ENSLOCT00000008492.1; ENSLOCP00000008482.1; ENSLOCG00000006993.1.
DR GeneID; 102694201; -.
DR CTD; 2893; -.
DR GeneTree; ENSGT00940000155677; -.
DR HOGENOM; CLU_007257_1_2_1; -.
DR OrthoDB; 511851at2759; -.
DR Proteomes; UP000018468; Linkage group LG3.
DR Bgee; ENSLOCG00000006993; Expressed in brain and 6 other cell types or tissues.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0022824; F:transmitter-gated monoatomic ion channel activity; IEA:UniProt.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:UniProt.
DR CDD; cd06388; PBP1_iGluR_AMPA_GluR4; 1.
DR CDD; cd13727; PBP2_iGluR_AMPA_GluR4; 1.
DR Gene3D; 1.10.287.70; -; 2.
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; IPR028082; Peripla_BP_I.
DR InterPro; IPR001638; Solute-binding_3/MltF_N.
DR PANTHER; PTHR18966:SF100; GLUTAMATE RECEPTOR 4; 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; 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 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:UP000018468};
KW Signal {ECO:0000256|ARBA:ARBA00022729, 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}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT CHAIN 22..903
FT /note="Glutamate receptor"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT /id="PRO_5027166051"
FT TRANSMEM 543..565
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT TRANSMEM 627..649
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT TRANSMEM 817..839
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT DOMAIN 416..792
FT /note="Ionotropic glutamate receptor C-terminal"
FT /evidence="ECO:0000259|SMART:SM00079"
FT DOMAIN 426..491
FT /note="Ionotropic glutamate receptor L-glutamate and
FT glycine-binding"
FT /evidence="ECO:0000259|SMART:SM00918"
FT REGION 882..903
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 885..903
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 903 AA; 101388 MW; BC646D0212FAF9FC CRC64;
MRITCRQLLL LFSSFWGLTM GAFPSSVQIG GLFIRNTDQE YTAFRLAIFL HNTSPNATEA
PFNLVPHVDN IETANSFAVT NAFCSQYSRG VFAIFGLYDK RSVHTLTSFC SALHISLITP
SFPTEGESQF VLQLRPSLRG ALLSLLDHYD WNRFVFLYDT DRGYSILQAI MEKAGQNGWQ
VSAICVENFN DASYRRLLED LDRRQEKKFV IDCEAERLQN ILEQIVSVGK HVKGYHYIMA
NLGFKDISLE RFMHGGANVT GFQLVDFNTP MVIKLMQRWN KLDQREYPGS ESPPKYTSAL
TYDGVLVMAE AFRNLRRQKI DISRRGNAGD CLANPAAPWN QGIDMERTLK QVRIQGLTGN
VQFDHYGRRV NYTMDVFELK SNGPRRIGYW NDNDKLVLIQ NEILLPNETA AMENRTVVVT
TIMEGPYVML KKNWEMFEGN DQYEGYCVDL ASEIAKHIGI KYKISIVPDG KYGARDPETK
IWNGMVGELV YGKAEIAVAP LTITLVREEV IDFSKPFMSL GISIMIKKPQ KSKPGVFSFL
DPLAYEIWMC IVFAYIGVSV VLFLVSRFSP YEWHTEEPED GNEGPPSDQP PNEFGIFNSL
WFSLGAFMQQ GCDISPRSLS GRIVGGVWWF FTLIIISSYT ANLAAFLTVE RMVSPIESAE
DLAKQTEIAY GTLDSGSTKE FFRRSKIAVY EKMWTYMKSA EPSVFTKTTA EGVARVRKSK
GKFAFLLEST MNEYIEQRKP CDTMKVGGNL DSKGYGVATP KGSQLRNAVN LAVLKLNEQG
LLDKLKNKWW YDKGECGSGG GDSKDKTSAL SLSNVAGVFY ILVGGLGLAM LVALIEFCYK
SRAEAKRMKL TFTEAMRNKA RLSITGSVGE NGRVLTPDCP KAVHTGPSQR QSSGLAVVSS
EYQ
//
