GenomeNet

Database: UniProt
Entry: A0A3B1IE89_ASTMX
LinkDB: A0A3B1IE89_ASTMX
Original site: A0A3B1IE89_ASTMX 
ID   A0A3B1IE89_ASTMX        Unreviewed;       943 AA.
AC   A0A3B1IE89;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 31.
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:ENSAMXP00000027996.1, 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:ENSAMXP00000027996.1}
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; A0A3B1IE89; -.
DR   Ensembl; ENSAMXT00000032445.1; ENSAMXP00000027996.1; ENSAMXG00000030727.1.
DR   GeneTree; ENSGT00940000158016; -.
DR   Proteomes; UP000018467; Unassembled WGS sequence.
DR   Bgee; ENSAMXG00000030727; Expressed in brain and 3 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; cd06379; PBP1_iGluR_NMDA_NR1; 1.
DR   CDD; cd13719; PBP2_iGluR_NMDA_Nr1; 1.
DR   Gene3D; 1.10.287.70; -; 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; 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:SF570; GLUTAMATE RECEPTOR; 1.
DR   PANTHER; PTHR18966; IONOTROPIC GLUTAMATE RECEPTOR; 1.
DR   Pfam; PF01094; ANF_receptor; 2.
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:UP000018467};
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..17
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT   CHAIN           18..943
FT                   /note="Glutamate receptor"
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT                   /id="PRO_5027151836"
FT   TRANSMEM        578..596
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT   TRANSMEM        651..673
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT   TRANSMEM        829..853
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT   DOMAIN          451..811
FT                   /note="Ionotropic glutamate receptor C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00079"
FT   DOMAIN          457..523
FT                   /note="Ionotropic glutamate receptor L-glutamate and
FT                   glycine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00918"
FT   REGION          881..908
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        887..903
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   943 AA;  106552 MW;  2A7FCCA27045ECD3 CRC64;
     MRLLLLAALF SCSCVRGGCE PKVVNIGAVL SQKRYEQVFK DAVAQANVVY GRDKFKLTAI
     SVTHKANAIQ MALSVCEDLI SSQVYAILVS HPPQSSDHLT PTPVSYTAGF YRIPVVGLTT
     RMSIYSDKSI HLSFLRTVPP YSHQAHVWFD MMREFRWNHI ILIVSDDHEG RAAQKRLETL
     LEERETKNKK RNYENLDQLS YDNKRGPKAE KVLQFNQETN LTALLLEAKE LEARVIILSA
     SEEDAAAVYK TARFLNMTGS GYVWLVGERE MSGKALSEAP DGLIGLQLIN GKNESAHISD
     AVAVVAQSIQ ELFEKENITE PPRGCVGNTN IWKTGPLFKR VLMSSKYPEG LTGRVEFNDD
     GDRKYAHYSI LNYQKSRLIQ VGIYNGTQVV LNKQRKIIWP GGETERPRGF QMSTRLKIVT
     IHQEPFVYVK PTMQDGTCRE EYTPNGVLIK KVICTGPNET IPGRPIVPQC CYGFCVDLLI
     KLAMTMNFTY EVHLVADGKF GTQERVNNSN KKEWNGMMGE LLSGLADMIV APLTINNERA
     QYIEFSKPFK YQGLTILVKK EIPRSTLDSF MQPFQSTLWL LVGLSVHVVA VMLYLLDRFS
     PFGRFKVNSE EEEEDALTLS SAMWFSWGVL LNSGIGEGAP RSFSARILGM VWAGFAMIIV
     ASYTANLAAF LVLDRPEERI TGINDPRLRN PSDKFIYATV KQSSVDIYFR RQVELSTMYR
     HMEKHNYESA AEAIQAVRDN KLHAFIWDSA VLEFEASQKC DLVTTGELFF RSGFGIGMRK
     DSPWKQNVSL AILSSHENGF MEDLDKTWVR YQECDSRSNA PATLTFENMA GVFMLVAGGI
     AAGIFLIFIE IAYKRHKDAR RKQMQLAFAA VNVWRKNLQP SSSVETQDDR KSGRAESDPK
     KKPSFRSIST TLASSIKRRR SSKDTVRKIK EWHLLLLVYQ SVV
//
DBGET integrated database retrieval system