ID A0A091XCK4_OPIHO Unreviewed; 1365 AA.
AC A0A091XCK4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Glutamate receptor {ECO:0000256|RuleBase:RU367118};
DE Flags: Fragment;
GN ORFNames=N306_07415 {ECO:0000313|EMBL:KFR11056.1};
OS Opisthocomus hoazin (Hoatzin) (Phasianus hoazin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Opisthocomiformes; Opisthocomidae;
OC Opisthocomus.
OX NCBI_TaxID=30419 {ECO:0000313|EMBL:KFR11056.1, ECO:0000313|Proteomes:UP000053605};
RN [1] {ECO:0000313|EMBL:KFR11056.1, ECO:0000313|Proteomes:UP000053605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N306 {ECO:0000313|EMBL:KFR11056.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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 EMBL; KK734814; KFR11056.1; -; Genomic_DNA.
DR STRING; 30419.A0A091XCK4; -.
DR PhylomeDB; A0A091XCK4; -.
DR Proteomes; UP000053605; 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; 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: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; 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};
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:UP000053605};
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 422..444
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT TRANSMEM 465..482
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT TRANSMEM 494..519
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT TRANSMEM 685..708
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT DOMAIN 302..663
FT /note="Ionotropic glutamate receptor C-terminal"
FT /evidence="ECO:0000259|SMART:SM00079"
FT DOMAIN 304..367
FT /note="Ionotropic glutamate receptor L-glutamate and
FT glycine-binding"
FT /evidence="ECO:0000259|SMART:SM00918"
FT REGION 1031..1063
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1149..1180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1149..1169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFR11056.1"
FT NON_TER 1365
FT /evidence="ECO:0000313|EMBL:KFR11056.1"
SQ SEQUENCE 1365 AA; 153350 MW; 0A7033B418F554AC CRC64;
ESSMFFQFGP SIEQQASVML NIMEEYDWYI FSIVTTYFPG YQDFVNKIRS TIEHSFVGWE
LEEVLLLDMS LDDGDSKIQN QLKKLQSPVI LLYCTKEEAT YIFEVANSVG LTGYGYTWIV
PSLVAGDTDT VPSEFPTGLI SVSYDEWDYG LPARVRDGIA IITTAASDML SEHSFIPEPK
SSCYNTQEKR IYQSNMLNRY LINVTFEGRN LSFSEDGYQM HPKLVIILLT KERKWERVGK
WKEKKLQMKY YVWPRFELYP DSEEREDDHL SIVTLEEAPF VIVENVDPLS GTCMRNTVPC
QKRIVTENKT DEEPDYMKKC CKGFCIDILK KISKSVKFTY DLYLVTNGKH GKKINGTWNG
MIGEVVTKRA YMAVGSLTIN EERSEVVDFS VPFIETGISV MVSRSNGTVS PSAFLEPFSA
DVWVMMFVML LIISAVAVFV FEYFSPVGYN RCLADGREPG GPSFTIGKAI WLLWGLVFNN
SVPVQNPKGT TSKIMVSVWA FFAVIFLASY TANLAAFMIQ EEYVDQVSGL SDKKFQKPND
FSPPFRFGTV PNGSTERNIR NNYPEMHSYM VKFNQRGVDD ALFSLKTGKL DAFIYDAAVL
NYMAGRDEGC KLVTIGSGKV FASTGYGIAI QKDSGWKRQV DLAILQLFGD GEMEELEALW
LTGICHNEKN EVMSSQLDID NMAGVFYMLG AAMALSLITF ICEHLFYWQF RHCFMGVCSG
KPGVVFSISR GIYSCIHGVA IEERQSAMNS PTATMNNTHS NILRLLRTAK NMANLSGVNG
SPQSALDFIR RESSVYDISE HRRSFTHSDC KSYNNPPCEE NLFSDYISEV ERTFGNLQLK
DSNVYQDHYH HHHRPHSIGS TSSIDGLYDC DNPPFNAQSR SIGKKPLDLG LPPAKHSQLG
DLYGKFSFKS DRYGGSGAHD DLIRSDVSDI STHTVTYGNI EGNAAKRRKQ QYKDSLKKRP
ASAKSRREFD EIELAYRRRP PRSPDHKRYF RDKEGLRDFY LDQFRAKENS PHWEHVDLTD
IYKERGDEFK RDTGGGGGGS CTNRAHHKHG SGEFGGSNEH KHGVVSGVPA PWEKNLTNLD
WEDRSGANFC RGCPSKVHNY TPSVVGQNST RQACIRCEAC KKAGNLYDIS EDNSLQELDQ
PPACVPVAAS ATSSSKYPQS PSNSASKVQK KNRNKLRRQH SYDTFVDLQK DDSALAPRSV
SLKDKGRFLE GSPYAHMFEM PASETTFANN KSSVPATSYH HHNNPGSSGG YMLSKSLYPD
RVTQNPFIPT FGDDQCLLHG SKSYFFRQPV VAGGPKARPD FRAIVTTNKP VVSALHGAVP
ARFQKDICIG NQSNPCVPNN KNPRAFNGSS NGHVYEKLSS IESDV
//
