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Database: UniProt
Entry: F6X9P6_XENTR
LinkDB: F6X9P6_XENTR
Original site: F6X9P6_XENTR 
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
//
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