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Database: UniProt
Entry: H3CIB5_TETNG
LinkDB: H3CIB5_TETNG
Original site: H3CIB5_TETNG 
ID   H3CIB5_TETNG            Unreviewed;       945 AA.
AC   H3CIB5;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   RecName: Full=Glutamate receptor {ECO:0000256|RuleBase:RU367118};
GN   Name=GRIK5 {ECO:0000313|Ensembl:ENSTNIP00000007993.1};
OS   Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS   nigroviridis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX   NCBI_TaxID=99883 {ECO:0000313|Ensembl:ENSTNIP00000007993.1, ECO:0000313|Proteomes:UP000007303};
RN   [1] {ECO:0000313|Proteomes:UP000007303}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15496914; DOI=10.1038/nature03025;
RA   Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA   Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA   Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA   Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA   Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA   Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA   Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA   McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA   Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA   Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA   Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT   "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT   early vertebrate proto-karyotype.";
RL   Nature 431:946-957(2004).
RN   [2] {ECO:0000313|Ensembl:ENSTNIP00000007993.1}
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   AlphaFoldDB; H3CIB5; -.
DR   Ensembl; ENSTNIT00000008154.1; ENSTNIP00000007993.1; ENSTNIG00000005311.1.
DR   GeneTree; ENSGT00940000158852; -.
DR   HOGENOM; CLU_007257_1_0_1; -.
DR   Proteomes; UP000007303; Unassembled WGS sequence.
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; cd06394; PBP1_iGluR_Kainate_KA1_2; 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; 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   PANTHER; PTHR18966:SF351; GLUTAMATE RECEPTOR IONOTROPIC, KAINATE 5; 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:UP000007303};
KW   Signal {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..19
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT   CHAIN           20..945
FT                   /note="Glutamate receptor"
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT                   /id="PRO_5027146040"
FT   TRANSMEM        546..566
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT   TRANSMEM        625..646
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT   TRANSMEM        805..829
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT   DOMAIN          417..786
FT                   /note="Ionotropic glutamate receptor C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00079"
FT   DOMAIN          427..491
FT                   /note="Ionotropic glutamate receptor L-glutamate and
FT                   glycine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00918"
SQ   SEQUENCE   945 AA;  105914 MW;  829C4E30690CF876 CRC64;
     MPALPALLLS LLFLSFLLAT MPPRSLNLAA ILDDQSVCGR GERLALALAR ENINSVMEGP
     ARARVEVDIY ELQKDSQYDT TDTMCQILPK GVVSVIGPAS SPASGSTVSH ICGEKEIPHI
     KIGPEETPRL PYLRFASVTL YPSNEDLSLA IGAILRSFSY PSASLVCAKA ECLLRLEELV
     RRFLISRETL SVRMLDDNLD PTPLLKEIRD DKVATIIIDA NASVSYLILK KASELGMTSA
     FYKYILTTMD FPLLRLEDIV DEQSNIVGFS MFNTTHPFYL EFIRSLNLSW REGCDLTYPG
     PALSSALMFD AVHVVVGAVR ELNRSQEIGV KPLSCTSPQI WQHGTSLMNY LRMVEYDGLT
     GRVEFNSKGQ RTNYTLRILE KHRGGHKEIG IWYSNNTLAM NSTSLDINVS ETLANKTLIV
     TTILENPYVM RKDNYQDFQG NDQYEGFCVD MLREVADILK FSFKIKLVDD GLYGAPEPNG
     SWTGMVGELI NRKADLAVAA FTITSEREKV IDFSKPFMTL GISILYRVQL GRKPGYFSFL
     DPFSPAVWLF MLLAYLAVSC VLFLAARLSP YEWYNPHPCL RENRDMLENQ YTLGNSLWFP
     VGGFMQQGSE IMPRALSTRC VSGVWWAFTL IIISSYTANL AAFLTVQRME VPIESPDDLA
     DQTNIEYGTI HGGSTMTFFM NSRYQTYQRM WNYMKSKQPG VFVKSTEEGI ARVVNSKYAF
     LMESTMNEYH RGLNCNLTQI GGLLDTKGYG IGMPLGSPFR DEITLAILQL QENNRLEILK
     RRWWEGGQCP KEEDHRAKGL GMENIGGIFV VLICGLIIAV FVAIMEFVWS TRRSAETDEA
     SVCQEMITEF RNAVSCKKSS RIRRRRPLGG SAALRHPARI ALGAPRPLRL VREMRLSNGK
     LYSGSGPLTP PPPAPTPVML PARGCTHVRI CQECRRIQNL KTASS
//
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