ID G3TLE2_LOXAF Unreviewed; 1304 AA.
AC G3TLE2;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Glutamate receptor {ECO:0000256|RuleBase:RU367118};
GN Name=GRIN2B {ECO:0000313|Ensembl:ENSLAFP00000015704.2};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000015704.2, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000015704.2, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000015704.2,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000015704.2}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000015704.2};
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. NR2B/GRIN2B subfamily. {ECO:0000256|ARBA:ARBA00038189}.
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DR Ensembl; ENSLAFT00000018733.2; ENSLAFP00000015704.2; ENSLAFG00000018733.2.
DR GeneTree; ENSGT00940000155964; -.
DR HOGENOM; CLU_002598_1_0_1; -.
DR Proteomes; UP000007646; 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 GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 2.
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:SF382; GLUTAMATE RECEPTOR IONOTROPIC, NMDA 2B; 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; 2.
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 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:UP000007646};
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 492..513
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT TRANSMEM 679..702
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT DOMAIN 294..657
FT /note="Ionotropic glutamate receptor C-terminal"
FT /evidence="ECO:0000259|SMART:SM00079"
FT DOMAIN 303..366
FT /note="Ionotropic glutamate receptor L-glutamate and
FT glycine-binding"
FT /evidence="ECO:0000259|SMART:SM00918"
FT REGION 988..1013
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1091..1119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1091..1111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1304 AA; 147034 MW; 5C1C6152B78F8AC2 CRC64;
DESSMFFQFG PSIEQQASVM LNIMEEYDWY IFSIVTTYFP GYQDFVNKIR STIENSFVGW
ELEEVLLLDM SLDDGDSKIQ NQLKKLQSPI ILLYCTKEEA TYIFEVANSV GLTGYGYTWI
VPSLVAGDTD TVPSEFPTGL ISVSYDEWDY GLPARVRDGI AIITTAASDM LSEHSFIPEP
KSSCYNTHEK RIYQSNMLNR YLINVTFEGR NLSFSEDGYQ MHPKLVIILL NKERKWERVG
KWKDKSLQMK YYVWPRMCPE TEEQEDDHLS IVTLEEAPFV IVESVDPLSG TCMRNTVPCQ
KRIISENKTD EEPGYIKKCC KGFCIDILKK ISKSVKFTYD LYLVTNGKHG KKINGTWNGM
IGEVVMKRAY MAVGSLTINE ERSEVVDFSV PFIETGISVM VSRSNGTVSP SAFLGKRLGL
SWRIFYSGQK LTSSVYLHPM LTFCPCLLVM PEPGGPSFTI GKAIWLLWGL VFNNSVPVQN
PKGTTSKIMV SVWAFFAVIF LASYTANLAA FMIQEEYVDQ VSGLSDKKFQ RPNDFSPPFR
FGTVPNGSTE RNIRNNYAEM HAYMGKFNQR GVDDALLSLK TGKLDAFIYD AAVLNYMAGR
DEGCKLVTIG SGKVFASTGY GIAIQKDSGW KRQVDLAILQ LFGDGEMEEL EALWLTGICH
NEKNEVMSSQ LDIDNMAGVF YMLGAAMALS LITFICEHLF YWQFRHCFMG VCSGKPGMVF
SISRGIYSCI HGVAIEERQS VMNSPTATMN NTHSNILRLL RTAKNMANLS GVNGSPQSAL
DFIRRESSVY DISEHRRSFT HSDCKSYNNP PCEENLFSDY ISEVERTFGN LQLKDSNVYQ
DHYHHHRPHS IGPSSKHSQL SDLYGKFSFK SDRYSGHDDL IRDVSDISTH TVYGNIEGNA
AKRRKQQYKD SLKKRPASAK SRREFDEIEL AYRRRPPRSP DHKRYFRDKE GLRDFYLDQF
RTKENSPHWE HVDLTDIYKE RGDDFKRDSV SGGGPCTNRS HLKGDKHSVV SGVPAPWEKN
LTNMDWEDRS GGNFCRSCPS KLHNYSTTVA GQNSGRQACI RCEACKKAGN LYDISEDNSL
QELDQPAAPV AVTSNASTTK YPQSPTNSKA QKKTRNKLRR QHSYDTFVDL QKEEAALAPR
SVSLKDKGRF LDGSPYAHMF EMPAGESTFA NNKSSVPTAG HHHHNNPGSS YMLSKSLYPD
RVTQNPFIPT FGDDQCLLHG SKSYFFRQPT VAGAPKARPD FRALVTNKPV VSALHGAVPG
RFQKDICIGN QSNPCVPNNK NPRAFNGSSN GHVYEKLSSI ESDV
//
