ID H3AUN9_LATCH Unreviewed; 1375 AA.
AC H3AUN9;
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=GRIN2C {ECO:0000313|Ensembl:ENSLACP00000013360.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000013360.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000013360.1}
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|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 EMBL; AFYH01091807; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01091808; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01091809; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01091810; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01091811; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01091812; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01091813; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01091814; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 7897.ENSLACP00000013360; -.
DR Ensembl; ENSLACT00000013456.1; ENSLACP00000013360.1; ENSLACG00000011764.1.
DR eggNOG; KOG1053; Eukaryota.
DR GeneTree; ENSGT00940000156964; -.
DR HOGENOM; CLU_002039_1_1_1; -.
DR InParanoid; H3AUN9; -.
DR OMA; FPIHYGD; -.
DR TreeFam; TF314731; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
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:SF361; GLUTAMATE RECEPTOR IONOTROPIC, NMDA 2C; 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}; Coiled coil {ECO:0000256|SAM:Coils};
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:UP000008672};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
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 525..548
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT TRANSMEM 569..586
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT TRANSMEM 598..623
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT TRANSMEM 789..812
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT DOMAIN 409..767
FT /note="Ionotropic glutamate receptor C-terminal"
FT /evidence="ECO:0000259|SMART:SM00079"
FT DOMAIN 419..471
FT /note="Ionotropic glutamate receptor L-glutamate and
FT glycine-binding"
FT /evidence="ECO:0000259|SMART:SM00918"
FT COILED 877..904
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1375 AA; 155927 MW; A2A2A080FB991C34 CRC64;
PILNVAIVFG GSNYQMEMKS KLTRDSFHGL PLEINPVLVI INNTNPSALL TQICDVLSNS
RIHGVIFEDN IGTEAVAQIL DFISSQTSVP IISISGGSAV VLIPKEQGST FLQLGASMEQ
QISVIFKVLE EYDWSSFAVI TSLYPGYDDF IDYIKIFTDT SYFGWELENI LTFEMTQEWS
NSKTQRLLKQ IDSQVIIVYC SHEEAEYLFE VAAESGLIGP GNIWIVPSLT VGNMERPPQR
FPIGLISVMT DRWKVNLRQR IRDGVAVIAK GAASFLKQNK LLPNLTINCQ APANPTMINA
FYRHILNVTW ERKDFSFNEN GYLVRPSMVV ITLTRDKLWD TVGKWENGLI QMKYPVWPRY
GSFLQPMSDN RHLTVATLEE RPFVIVENVD PVTGGCVRNT VPCRKQTNRT GSGVNVADPY
VKLCCKGFCI DILKKLAKTV KFSYDLYLVT NGKHGKKVRG VWNGMIGEVY YKRADVAIGS
LTINEERSEI IDFSVPFVET GISVMVARSN GTVSPSAFLE PYSPAVWVMM FVMCLTVVAI
TVFIFEFFSP VGYNKTLTNG KKPGGPTFTI GKSIWLLWAL VFNNSVPIEN PKGTTSKIMV
LIWAFFAVIF LASYTANLAA FMIQEQYIDT VSGLSDKKFQ KPQEQYPPFR FGTVPNGSTE
RNIKNNYKDM HTHMVKYNQR SVEDALTSLK TGKLDAFIYD AAVLNYMAGK DEGCKLVTIG
SGKVFATTGY GIALQKESKW KRPVDLALLQ FLGDGETQKL ETVWLSGICQ NEKNEVMSSK
LDIDNMAGVF YMLLVAMGLS LLTFAWEHLL FWKLRHTIKK SDKLDFLLAI SRGIYSCFNG
VQDIDSPIHV HTPDVTANYA QANMLKMLQT AKDIVSSTNV EDSLENATRT IENWTRRSEN
VQGSFPLRSP KLVINNSNVC SSKQPYLSDL KDNSITYIPR PVTSIHTPTT YRYGDMKPQM
LEKQRTVRHH LPFKSPMYMG GSYVDDQNLP ISTITNSPQL VDRNPDFLNP HQTGHIYVRN
PHREPNSIFV PYRDLQLPDL YREYKNPIPS KLYSPEIVRK GKSHHQYLVE TSDMMLGAAA
INADRPFSQR NENQYIESHI PTLSCMNNHV TRASVNCNSC IKAYGEPEPD EMLLLEKEKF
NRRASLIRAA WEHNEKLKAL GLANPPKSSS FHRETPNLFP KPRLVLKQSP TLHSTMENDL
HYPTHIVKAN YAYNNKYEDP IARHPFKQQR LKHSQSTRLP SYSEACLQNA AALRRSSTVV
HRHYSYVDSY AHLPMCLGQL NQVPSHFYEP TEKMGNRFTY ADQYPDDDTF IAKGSDGRLS
YENGVYRTYR HVSGMDSEHH QVPSKDKRQY LAARRMNRSY AAKPWRRVSS LESEV
//
