ID   F4WBH7_ACREC            Unreviewed;       536 AA.
AC   F4WBH7;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   SubName: Full=Glutamate [NMDA] receptor subunit epsilon-2 {ECO:0000313|EMBL:EGI68456.1};
DE   Flags: Fragment;
GN   ORFNames=G5I_02889 {ECO:0000313|EMBL:EGI68456.1};
OS   Acromyrmex echinatior (Panamanian leafcutter ant) (Acromyrmex octospinosus
OS   echinatior).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Acromyrmex.
OX   NCBI_TaxID=103372 {ECO:0000313|Proteomes:UP000007755};
RN   [1] {ECO:0000313|EMBL:EGI68456.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Nygaard S., Zhang G.;
RT   "The genome of the leaf-cutting ant Acromyrmex echinatior suggests key
RT   adaptations to social evolution and fungus farming.";
RL   Submitted (FEB-2011) 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; GL888063; EGI68456.1; -; Genomic_DNA.
DR   AlphaFoldDB; F4WBH7; -.
DR   STRING; 103372.F4WBH7; -.
DR   eggNOG; KOG1053; Eukaryota.
DR   InParanoid; F4WBH7; -.
DR   Proteomes; UP000007755; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015276; F:ligand-gated monoatomic ion channel activity; IEA:InterPro.
DR   GO; GO:0038023; F:signaling receptor activity; IEA:InterPro.
DR   Gene3D; 1.10.287.70; -; 1.
DR   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 3.
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; IPR001638; Solute-binding_3/MltF_N.
DR   PANTHER; PTHR18966; IONOTROPIC GLUTAMATE RECEPTOR; 1.
DR   PANTHER; PTHR18966:SF391; NMDA RECEPTOR 2, ISOFORM C; 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; SSF53850; Periplasmic binding protein-like II; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Coiled coil {ECO:0000256|SAM:Coils};
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   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000313|EMBL:EGI68456.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007755};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
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        118..140
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        160..178
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        190..211
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        373..393
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          2..353
FT                   /note="Ionotropic glutamate receptor C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00079"
FT   DOMAIN          4..62
FT                   /note="Ionotropic glutamate receptor L-glutamate and
FT                   glycine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00918"
FT   COILED          452..479
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EGI68456.1"
SQ   SEQUENCE   536 AA;  61256 MW;  72C4EB46ADE5C6C0 CRC64;
     VDIQSAHRNG SFYQCCSGFC IDLLQKFSEE IGFTFELIRV EDGKWGTLEN GKWNGLIADL
     VNRKTDMVMT SLMINSEREA VVDFTVPYME TGIAIVVAKR TGIISPTAFL EPFDTASWML
     VGIVAIHAAT IMILLFEWAS PSGFDMKNNP STNHRFSFCR TYWLVWAVLF QAAVHIDSPR
     GFTARFMTNV WALFAVVFLA IYTANLAAFM ITREEFHEFS GVDDHRLAKP FSHKPMFKFG
     TIPWSHTDST LAKYFKEMHS YMRAFNKSSV ADGIEAVITG DMDAFIYDGT VLDYLVAQDE
     DCRLLTVGSW YAMTGYGLAF SRNSKYLQMF NKQLLDYRDN GDLERLRRYW MTGTCKPGKE
     VQKSSDPLAL EQFLSAFLLL MMGILLAAVF LLLEHLYFKY IRQHLAKSDD GGTCAIFSLS
     VGKSLTFRGA VYEAQDILRH HRCKDPICDT HLWKVKHELD MAKIRIRQLE KDLEAHGIKP
     TQTKYIDAVE VARPRDMSRN HVVSTEYAET FLPTEIYRIP DDDVTRTEIA EMETVL
//