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Database: UniProt
Entry: A0A3B4D4W0_PYGNA
LinkDB: A0A3B4D4W0_PYGNA
Original site: A0A3B4D4W0_PYGNA 
ID   A0A3B4D4W0_PYGNA        Unreviewed;      1415 AA.
AC   A0A3B4D4W0;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Glutamate receptor {ECO:0000256|RuleBase:RU367118};
GN   Name=GRIN2C {ECO:0000313|Ensembl:ENSPNAP00000017939.1};
OS   Pygocentrus nattereri (Red-bellied piranha).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC   Characoidei; Pygocentrus.
OX   NCBI_TaxID=42514 {ECO:0000313|Ensembl:ENSPNAP00000017939.1, ECO:0000313|Proteomes:UP000261440};
RN   [1] {ECO:0000313|Ensembl:ENSPNAP00000017939.1}
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|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. {ECO:0000256|RuleBase:RU367118}.
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DR   RefSeq; XP_017561386.1; XM_017705897.1.
DR   STRING; 42514.ENSPNAP00000017939; -.
DR   Ensembl; ENSPNAT00000026936.1; ENSPNAP00000017939.1; ENSPNAG00000005556.1.
DR   GeneID; 108432208; -.
DR   CTD; 100003342; -.
DR   GeneTree; ENSGT00940000156964; -.
DR   OMA; FPIHYGD; -.
DR   OrthoDB; 1034721at2759; -.
DR   Proteomes; UP000261440; Unplaced.
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   CDD; cd06378; PBP1_iGluR_NMDA_NR2; 1.
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; 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; IPR018884; NMDAR2_C.
DR   InterPro; IPR028082; Peripla_BP_I.
DR   InterPro; IPR001638; Solute-binding_3/MltF_N.
DR   PANTHER; PTHR18966:SF405; GLUTAMATE RECEPTOR; 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; 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.
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   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..30
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT   CHAIN           31..1415
FT                   /note="Glutamate receptor"
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT                   /id="PRO_5027148724"
FT   TRANSMEM        564..587
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT   TRANSMEM        639..662
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT   TRANSMEM        828..850
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT   DOMAIN          451..806
FT                   /note="Ionotropic glutamate receptor C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00079"
FT   DOMAIN          458..510
FT                   /note="Ionotropic glutamate receptor L-glutamate and
FT                   glycine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00918"
FT   REGION          1090..1116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1361..1387
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1415 AA;  158536 MW;  9A59324E248B62F7 CRC64;
     MGVRLGRLSD TLWPPLLLLL LLCALPSCQG RPFTMVEPTV NVAVVFSGSA YQLEIKGRLS
     RENFLDLPME VNPITVLVNN TNPRALLTRI CDTLAANRVH GVVFEDNIGS EAVAQILDFI
     STQTAVPIVG ISGGSAVVLP HKGDGSTFLQ LGSSIEQQIN GMFKVMEEYN WDSFVVVTSQ
     YPGYEAFVDY IRSFTDTSYF LWELQDVLTF DMSADGMNDL RARRLLQQID AQVLLVYCSH
     DEAQYLFSMA KEVGLLGPGY IWIIPSLAVG NPNIPPPDSF PVGLISIITD RWKMSLRNRV
     RDGVAIVVKG VESFRKHRGF IPDGHTDCQT PLRPDTNDTL FKHMLNVSWE HTDFSFNSDG
     YLVNPSMIII TLDRERQWDK VGSYESGILQ MRYPVWPRYG TYMEPVSDNR HLTVATLEER
     PFVIVEAVDP ITGTCLSNTV PCRRQSNKTE TIIGHTEPYT KLCCKGFCID ILKKLSRNIK
     FSYDLYLVTN GKHGKLVRGV WNGMIGEVVY KRADMAIGSL TINEERSEII DFSVPFVETG
     ISVMVARSNG TVSPSAFLEP YSPAVWVMMF VMCLTVVAVT VFVFEYFSPV GYNRSLVSAK
     DPGGPTFTIG KSVWLLWGIV FNNSVPIENP KGTTSKIMVL VWAFFAVIFL ASYTANLAAF
     MIQEQYIDTV SGLSDKKFQK PQEQYPPFRF GTVPNGSTER NIRSNYPEMH SHMVKYNQKG
     VEDALNSLKT GKLDAFIYDA AVLNYMAGKD EGCKLVTIGS GKVFATTGYG IALQKGSRWK
     RPIDLALLQF LADGDTAKLQ TVWLTGICRN EKKEVMSSKL DIDNMAGVFY MLLVAMGLSL
     LVFAWEHLLY WKLRHSVRKS ERLDFLLAIS RGIYSCFNGV EDTDRNGSMQ SPDVTTNYTQ
     ANMLKMLKTA KDIVSSARVE NSLDNATKTI ENLSRRGPDA TKPCLPTRLI STDSSHGRLP
     YISSVTDNHA PYPHTPTFPL HYGDSGTQPL LEKPRVVTRP TPLRYTLPAR TSHHHIYERT
     LPISSLSSPH IAMRDPPPPT APKPHHSGRF YMDSQACHQT SPFLPYREFH VPDIYVEHQE
     PSGSRKLYAE GLGRKKRSHS YVAPSPETRR RNDYDEPTSC LAELRANHLL DNHAHTTPCM
     GSHYQRPSGS CNSCMKPYLE PEMDDVPLLG KEKLNRRASF LRATWGGDRI RHLDEKPSTS
     ASSSSRINMP DLFPRVVVAN PKPSKMYSSA GNNLCYNMAV EPAYLDPAHM GSYPYKPQKL
     KYSQSTRLPS YREAILQNAA ALRRSSSTVV HRHYSTYLNS YTDLPVYVGP LAQGPAHFYD
     HSKDMCHLFP CVNHCPDDAA LLPRLSGRPV MYQNTAFGGY EGAGRSRDEP PLQPLHTLPA
     SSGNRDRRQV LVARRVNSPY VPKPWGRVSS LESEV
//
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