ID G1KKS8_ANOCA Unreviewed; 1092 AA.
AC G1KKS8;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 2.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=Glutamate receptor {ECO:0000256|RuleBase:RU367118};
GN Name=grin3a {ECO:0000313|Ensembl:ENSACAP00000010837.3};
OS Anolis carolinensis (Green anole) (American chameleon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Iguania; Dactyloidae; Anolis.
OX NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000010837.3, ECO:0000313|Proteomes:UP000001646};
RN [1] {ECO:0000313|Ensembl:ENSACAP00000010837.3, ECO:0000313|Proteomes:UP000001646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000010837.3,
RC ECO:0000313|Proteomes:UP000001646};
RG The Genome Sequencing Platform;
RA Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACAP00000010837.3}
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 RefSeq; XP_003216676.1; XM_003216628.3.
DR AlphaFoldDB; G1KKS8; -.
DR STRING; 28377.ENSACAP00000010837; -.
DR Ensembl; ENSACAT00000011061.4; ENSACAP00000010837.3; ENSACAG00000011011.4.
DR GeneID; 100565030; -.
DR KEGG; acs:100565030; -.
DR CTD; 116443; -.
DR eggNOG; KOG1053; Eukaryota.
DR GeneTree; ENSGT00940000158571; -.
DR HOGENOM; CLU_002039_0_0_1; -.
DR InParanoid; G1KKS8; -.
DR OrthoDB; 1034721at2759; -.
DR TreeFam; TF314731; -.
DR Proteomes; UP000001646; Chromosome 2.
DR Bgee; ENSACAG00000011011; Expressed in brain and 4 other cell types or tissues.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098839; C:postsynaptic density membrane; IBA:GO_Central.
DR GO; GO:0008066; F:glutamate receptor activity; IBA:GO_Central.
DR GO; GO:1904315; F:transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential; IBA:GO_Central.
DR GO; GO:0035235; P:ionotropic glutamate receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0035249; P:synaptic transmission, glutamatergic; IBA:GO_Central.
DR CDD; cd06377; PBP1_iGluR_NMDA_NR3; 1.
DR CDD; cd13720; PBP2_iGluR_NMDA_Nr3; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
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:SF397; GLUTAMATE RECEPTOR IONOTROPIC, NMDA 3A; 1.
DR PANTHER; PTHR18966; IONOTROPIC GLUTAMATE RECEPTOR; 1.
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.
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:UP000001646};
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..26
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT CHAIN 27..1092
FT /note="Glutamate receptor"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT /id="PRO_5027156083"
FT TRANSMEM 649..669
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT TRANSMEM 690..708
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT TRANSMEM 720..743
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT TRANSMEM 908..930
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT DOMAIN 539..884
FT /note="Ionotropic glutamate receptor C-terminal"
FT /evidence="ECO:0000259|SMART:SM00079"
FT DOMAIN 543..596
FT /note="Ionotropic glutamate receptor L-glutamate and
FT glycine-binding"
FT /evidence="ECO:0000259|SMART:SM00918"
FT REGION 57..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1012..1040
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1049..1076
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1092 AA; 122401 MW; 56FEEE9B32D66E5A CRC64;
MWRLSLWWLL SRVALPLLPP CALVLARVPA SSCHPQPCQI LKRIGHTVRL GAAHLQPWLP
DDEEGPERAP GAGSLRSRGS AERDGTPFLP REALLLAAER LNGLKNLLPY NLSLEVVMAI
EAGLGDLPLF PFSSPGAAQP SSPGGGSSND PASFLQSVCH TVVVQGVSAL LAFPRSRREM
LEVDFLAGAL RLTALSIVRE EFPTKSQNPL HLQLSLERSL SFDADVTFSI LALNNWYNFS
LMVCQEEWNI TDFLFLTQQS SKFHLGSIIN ITGNLTSTDD LLTYLQVHLE NIKDTTSTVV
MFGCDMESTR RIFEITTQFG VMPPELHWIL GDSHNVEELR TEGLPLGLIA HGKTTQSFFE
DYVQDAMELV ARAVASATMI QPELALIPST TNCLNTEEKN LTSGQYLSKF LANTTFHGLS
GHIKVKDSSI ISSENNFFIW NLQHDPVGNP MWTRLGSWQE GKIIMDYGIW PEQAQRHKNH
NQHPTRLHLR VVTLIEHPFV FTRAVDDEGL CPAGQLCLDP LTNDSAVLDT LFENLQGGND
TVPTKFKQCC YGYCIDLLEK LAEDMNFDFD LYIVGDGKYG ALKNGQWTGL VGDLLAGTAH
MAVTSFSINT ARSQVVDFTS PFFSTSLGIL VRTKDTAAPI GAFMWPLHWT MWLGIFVALH
ITAIFLTLYE WTSPFGMTPK GRNRDKVFSF SSALNVCYAI LFGRTAAIKP PKCWTGRFLM
NLWAIFCLFC LSTYTANLAA VMVGEKIYEE LSGIHDPKLN HPSQGFRFGT VRESSAEDYF
KQSFPDMHEY MKRFNVPATP DGIDYLKQDP EKLDAFIMDK ALLDYEVSID ADCKLLTVGK
PFAIEGYGIG LPPNSPLTSN ISELISQYKS HGFMDVLHDK WYKVVPCGKR SFAVTETLQM
GIKHFSGLFV MLCIGFGMSI LTTIGEHIVY RLVIPRVKKK SKMKYWLHTS QRLHRALNSS
FIEDKHQPKA KRVEKRSHTG NSEHAVWNTA SPGNCHRRKY ICTEERQNEV VLKQQQEQQE
QEIPLPPVKR DSPASLATNG KADSVNIART SVIQELSELE KQIQVIKQEL QLAMSRKLEL
EEFQRTNRTA ES
//
