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Database: UniProt
Entry: A0A3P9DDF8_9CICH
LinkDB: A0A3P9DDF8_9CICH
Original site: A0A3P9DDF8_9CICH 
ID   A0A3P9DDF8_9CICH        Unreviewed;       840 AA.
AC   A0A3P9DDF8;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Glutamate receptor {ECO:0000256|RuleBase:RU367118};
GN   Name=GRIK1 {ECO:0000313|Ensembl:ENSMZEP00005032192.1};
OS   Maylandia zebra (zebra mbuna).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Maylandia; Maylandia zebra complex.
OX   NCBI_TaxID=106582 {ECO:0000313|Ensembl:ENSMZEP00005032192.1, ECO:0000313|Proteomes:UP000265160};
RN   [1] {ECO:0000313|Ensembl:ENSMZEP00005032192.1, ECO:0000313|Proteomes:UP000265160}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=25186727; DOI=10.1038/nature13726;
RA   Brawand D., Wagner C.E., Li Y.I., Malinsky M., Keller I., Fan S.,
RA   Simakov O., Ng A.Y., Lim Z.W., Bezault E., Turner-Maier J., Johnson J.,
RA   Alcazar R., Noh H.J., Russell P., Aken B., Alfoldi J., Amemiya C.,
RA   Azzouzi N., Baroiller J.F., Barloy-Hubler F., Berlin A., Bloomquist R.,
RA   Carleton K.L., Conte M.A., D'Cotta H., Eshel O., Gaffney L., Galibert F.,
RA   Gante H.F., Gnerre S., Greuter L., Guyon R., Haddad N.S., Haerty W.,
RA   Harris R.M., Hofmann H.A., Hourlier T., Hulata G., Jaffe D.B., Lara M.,
RA   Lee A.P., MacCallum I., Mwaiko S., Nikaido M., Nishihara H.,
RA   Ozouf-Costaz C., Penman D.J., Przybylski D., Rakotomanga M., Renn S.C.P.,
RA   Ribeiro F.J., Ron M., Salzburger W., Sanchez-Pulido L., Santos M.E.,
RA   Searle S., Sharpe T., Swofford R., Tan F.J., Williams L., Young S., Yin S.,
RA   Okada N., Kocher T.D., Miska E.A., Lander E.S., Venkatesh B., Fernald R.D.,
RA   Meyer A., Ponting C.P., Streelman J.T., Lindblad-Toh K., Seehausen O.,
RA   Di Palma F.;
RT   "The genomic substrate for adaptive radiation in African cichlid fish.";
RL   Nature 513:375-381(2014).
RN   [2] {ECO:0000313|Ensembl:ENSMZEP00005032192.1}
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|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   AlphaFoldDB; A0A3P9DDF8; -.
DR   Ensembl; ENSMZET00005033233.1; ENSMZEP00005032192.1; ENSMZEG00005012154.1.
DR   GeneTree; ENSGT00940000156253; -.
DR   Proteomes; UP000265160; LG14.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015276; F:ligand-gated monoatomic ion channel activity; IEA:InterPro.
DR   GO; GO:0038023; F:signaling receptor activity; IEA:InterPro.
DR   CDD; cd06382; PBP1_iGluR_Kainate; 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; 1.
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   PANTHER; PTHR18966:SF36; GLUTAMATE RECEPTOR IONOTROPIC, KAINATE 1; 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   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:UP000265160};
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        522..539
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT   TRANSMEM        596..618
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT   TRANSMEM        777..801
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT   DOMAIN          392..758
FT                   /note="Ionotropic glutamate receptor C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00079"
FT   DOMAIN          402..466
FT                   /note="Ionotropic glutamate receptor L-glutamate and
FT                   glycine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00918"
SQ   SEQUENCE   840 AA;  94925 MW;  C2AD293FB85EC6B5 CRC64;
     SQKTLENEPI SVEELAFKFA VTNINRNRTL MPNTTLTYDI QRINLFDSFE ASRRACDQLA
     LGVGAVFGPS HSSSVSAVQS ICNALEVPHI QTRWKHPSVD NKDSFYINLY PEYASISRAV
     LDIVQFYKWK TVTVVYEDAT GLIRLQELIK APSRYSIKIK IRQLPTGSKD ARPLLKEMKK
     GKEFYVIFDC SYQTSADVLK QILSMGMMTE YYHFFFTTLD LFALDLEPYR YSGVNMTGFR
     LLNIDNPHVA SVVERWAMER LQAPSKAETG MMEGMMTTEA ALMYDAVYMV AAASQRTSQI
     TVSSLQCHRH KPWRFGSRFM SMLKDAQWNG LTGQIIINKT DGLRKEFDLD VISLKEDGLE
     KIGVWNSQTG LNLSEINKDS STNVTDSMAN RTLIVTTILE NPYVMYKKSD KPLYGNDRFE
     GYCLDLLKEL SNILGFSYEV KLVSDGKYGA QNDKGEWNGM VRELIDHVAD LAVAPLTITY
     VREKVIDFSK PFMTLGISIL YHKPNGTNPG VFSFLNPLSP DIWMYVLLAC LGVSFAFTFK
     FTPYEWYNPH PCNPDSDVVE NNFTLINSVW FGVGALMQQG SELMPKALST RIVGGIWWFF
     TLIIISSYTA NLAAFLTVER MDSPIDSADD LAKQTKIEYG AVRDGSTMTF FKKSKISTYE
     KMWAFMSSRK NTALVKNNRE GIQRVLTTDY ALLMESTSIE YISQRNCNLT QIGGLIDSKG
     YGVGTPIGSP YRDKVTIAIL QLQEEGKLHM MKEKWWRGNG CPEEDSKEAS ALGVENIGGI
     FIVLAAGLVL SVFVAIGEFI YKSRKNLDID EVSSAMKEEH SDQCRIRLLL CFVKPLKFKP
//
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