ID F6X9P6_XENTR Unreviewed; 1450 AA.
AC F6X9P6;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 4.
DT 24-JAN-2024, entry version 81.
DE RecName: Full=Glutamate receptor {ECO:0000256|RuleBase:RU367118};
GN Name=grin2a {ECO:0000313|Ensembl:ENSXETP00000017540,
GN ECO:0000313|RefSeq:XP_031749422.1,
GN ECO:0000313|Xenbase:XB-GENE-992741};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364 {ECO:0000313|Ensembl:ENSXETP00000017540};
RN [1] {ECO:0000313|Ensembl:ENSXETP00000017540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nigerian {ECO:0000313|Ensembl:ENSXETP00000017540};
RX PubMed=20431018; DOI=10.1126/science.1183670;
RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT "The genome of the Western clawed frog Xenopus tropicalis.";
RL Science 328:633-636(2010).
RN [2] {ECO:0000313|Ensembl:ENSXETP00000017540}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUN-2011) to UniProtKB.
RN [3] {ECO:0000313|RefSeq:XP_031749422.1}
RP IDENTIFICATION.
RC STRAIN=Nigerian {ECO:0000313|RefSeq:XP_031749422.1};
RC TISSUE=Liver and blood {ECO:0000313|RefSeq:XP_031749422.1};
RG RefSeq;
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_031749422.1; XM_031893562.1.
DR STRING; 8364.ENSXETP00000017540; -.
DR PaxDb; 8364-ENSXETP00000016336; -.
DR Ensembl; ENSXETT00000017540; ENSXETP00000017540; ENSXETG00000008002.
DR KEGG; xtr:100489006; -.
DR Xenbase; XB-GENE-992741; grin2a.
DR eggNOG; KOG1053; Eukaryota.
DR HOGENOM; CLU_002598_1_0_1; -.
DR OMA; CDDCLHI; -.
DR TreeFam; TF314731; -.
DR Proteomes; UP000008143; Chromosome 9.
DR Bgee; ENSXETG00000008002; Expressed in brain and 1 other cell type or tissue.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0022890; F:inorganic cation transmembrane transporter activity; IEA:UniProt.
DR GO; GO:0004970; F:ionotropic glutamate receptor activity; IEA:InterPro.
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:SF407; GLUTAMATE RECEPTOR IONOTROPIC, NMDA 2A; 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 Calcium {ECO:0000256|ARBA:ARBA00022837};
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}; Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU367118};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
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:UP000008143};
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};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT CHAIN 21..1450
FT /note="Glutamate receptor"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT /id="PRO_5041007684"
FT TRANSMEM 549..571
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT TRANSMEM 621..643
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT TRANSMEM 812..835
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT DOMAIN 423..790
FT /note="Ionotropic glutamate receptor C-terminal"
FT /evidence="ECO:0000259|SMART:SM00079"
FT DOMAIN 431..494
FT /note="Ionotropic glutamate receptor L-glutamate and
FT glycine-binding"
FT /evidence="ECO:0000259|SMART:SM00918"
FT REGION 1012..1081
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1103..1139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1179..1198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1012..1031
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1032..1046
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1103..1117
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1124..1139
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1450 AA; 164262 MW; 224AA87059F42A28 CRC64;
MGIFALLLYT LLYAGDLGQG AEKSFPVLNI AVILGRTRYI TERDIRSLWT RDMSLDFDVN
VVTLLVNQTD PKSIITHVCD LMSGTKIHGV VFGDDTDQEA IAQILDFVSS QTFIPILGIH
GGSSMIMADK DEMSTFFQFG ASIKQQAIVM LNIMEEYDWH VFSIITSTFP GYRDFISFIK
TTVDNSFVGW EVQNVITLDT SYTDARTLTQ LKKIHSSVIL LYCSKDEANY IFVEARSLGL
MGYGFVWIVP SLVTGNTDII PYEFPSGLVS VSYDDWDYNI EARVRDGLGI ITTAASAMLE
KHSVIPEAKT SCYAQNERNE PPLHTLHKFM INVTWDGKDL SFTEDGYQAN PKLVVLLLNM
DREWEKVGKW ENKSLNMKYP VWPRITASLD SDPDDNHLSI VTLEEAPFVI VENVDYLTGT
CVRNTVPCRK YFRLNNSTTE GTSVKKCCKG FCIDILKKLS KTVKFTYDLY LVTNGKHGKK
IKNVWNGMIG EVVYKRAVMA VGSLTINEER SEAVDFSVPF VETGISVMVS RSNGTVSPSA
FLEPFSASVW VMMFVMLLLV SAVAVFVFEY FSPVGYNRNL ADGKAPHGPS FTIGKAVWLL
WGLVFNNSVP VQNPKGTTSK IIVSIWAFFA VIFLASYTAN LAAFMIQEEF VDQVTGLSDK
KFQRPHDYSP PFRFGTVPNG STERNIRNNY PDMHQYMVKF HQKGVQDALV SLKTGKLDAF
IYDAAVLNYM AGRDEGCKLV TIGSGYIFAT TGYGIALQKG SRWKRPIDLA LLQFVGDGEM
EELEKLWLTG ICHTEKNEVM SSQLDIDNMA GVFYMLAAAM ALSLITFVWE HLFYWKLRYC
FTGVCTGTPG LLFSISRGIY SCIHGVHIEE KKKSPDFSFT ASQTNMLKLL RASKNIANLS
NLNQSQCNSP KRTSDYIQRN SLLMDMVLDK GNLSYSDNRP FQQKDVYSEN TYDLAMLSGN
HPKDNLNNYV FQGQHPLTLN ESNPNTVEVA VSAEPKLNSR PRQLWKKSVE TLRQNQGSVN
ENGTEESKPS TKNQRFLPED GHFSDVSEAS SRATCHIDSE NNNKHHKSKD NLKKRSVSSK
YPRDCSEVEL SYLKLKHGSN RDKVYTIDGD KEPSFIMDQP KYSENSPDQD DDYPDVYQDH
NDNYRKAEAL QPDRTPLHSE GRLPNNDIQY KLFSKHYSSK EKNTSMSESN DRHRQNSTHC
RSCLSNMPNY TGHYTARSPY KCDDCLHIGK LYDIDEDQML HEAANSMHSE DFYEHNWLEN
NALHFQKKNK LRINRQHSCD NINKPREQDL GRPPRSVSLK EKERYIQDSP FAKFLIVPPE
KLLGNNTALF TDSLKESKRS KSLYPDNSSD NPFLHSYQET QKLSHGRSSS DIYKQSSLTK
ARNDNYLRSS IKSTSSYSSR DGRVPNDMCA SEYALPYVTS NNSVYSAPRV VNSCSNRRVF
KKMPSIESDV
//