ID A0A3B0K550_DROGU Unreviewed; 782 AA.
AC A0A3B0K550;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Blast:Glutamate receptor ionotropic, kainate 2 {ECO:0000313|EMBL:SPP87822.1};
GN ORFNames=DGUA_6G015587 {ECO:0000313|EMBL:SPP87822.1};
OS Drosophila guanche (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7266 {ECO:0000313|EMBL:SPP87822.1, ECO:0000313|Proteomes:UP000268350};
RN [1] {ECO:0000313|Proteomes:UP000268350}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Alioto T., Alioto T.;
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. 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|ARBA:ARBA00008685}.
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DR EMBL; OUUW01000013; SPP87822.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B0K550; -.
DR OMA; AQYENFG; -.
DR Proteomes; UP000268350; Unassembled WGS sequence.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
DR GO; GO:0015276; F:ligand-gated monoatomic ion channel activity; IEA:InterPro.
DR GO; GO:0038023; F:signaling receptor activity; IEA:InterPro.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:UniProt.
DR CDD; cd13714; PBP2_iGluR_Kainate; 1.
DR Gene3D; 1.10.287.70; -; 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; IPR028082; Peripla_BP_I.
DR InterPro; IPR001638; Solute-binding_3/MltF_N.
DR PANTHER; PTHR18966:SF349; FI04462P-RELATED; 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; 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 Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Ion channel {ECO:0000256|ARBA:ARBA00023303};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Ligand-gated ion channel {ECO:0000256|ARBA:ARBA00023286};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00023257};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000313|EMBL:SPP87822.1};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Synapse {ECO:0000256|ARBA:ARBA00023018};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 439..457
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 515..537
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 704..726
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 308..678
FT /note="Ionotropic glutamate receptor C-terminal"
FT /evidence="ECO:0000259|SMART:SM00079"
FT DOMAIN 319..383
FT /note="Ionotropic glutamate receptor L-glutamate and
FT glycine-binding"
FT /evidence="ECO:0000259|SMART:SM00918"
SQ SEQUENCE 782 AA; 89179 MW; 945DB18288E443B6 CRC64;
MSICDAMDIP HIYSYMSEYA EGFNLHPHPA DLAKALYSLI TEFNWTRFIF LYESADYLNI
LNELTTLFGM NGPVVTVLRY DMHLNGNYKQ VLRRVRKSVD NRIVVVGSSE TMPEFLNQAQ
QVGIINEDYK YIIGNLDFHS FDLEEYKYSE ANITGLRLFS PEKMAVKELL LKMGYPSDQD
EFRNGSCPIT VEMALTYDAV QLFAETLKNL PFKPVPQNCS QRTESVRDDG SSFKNYMRTL
RLTDRLLTGP IFFEGNVRKG YHLDVIELQP SGIVKVGTWD AQREYRAQRL AATTAQFDNI
DNSLANKTFI VLLSVPNKPY AQLVETFKQL EGNSQYEGYG VDLIKELADK LGFNFTFVNG
GNDYGSYNKT SNESTGMLRE IMMGRADLAI TDLTITSERE EAIDFTIPFM NLGIAILYLK
PQKATPELFT FMDPFSEEVW WFLGFSFLAV ALSFFILGRL SPSEWDNPYP CIEEPEELEN
QFTIGNSIWF TTGALLQQGS EIGPKALSTR TVATFWLFFT LIVVSSYTAN LAAFLTIEKP
QSLINSVDDL ADNKDGVVYG AKRTGSTRNF FLTSEDDRYK KMNKFMTEHP EHLTEDNQEG
VRRVKTSTHY AFLMESTSIE YNTKRECNLK KIGDALDEKG YGIAMRKNWP HRDKFNNALL
ELQEQGVLEK MKNKWWNEVG TGICATKEDA PDATPLDMNN LEGVFFVLLV GSCCALLYGI
ISWVLFVMKK AHHYRVPLRE ALKEEFQFVV DFNNYVRVLK SSASIYSRSR QSSMSVASMA
DS
//