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Database: UniProt
Entry: A0A195FWY9_9HYME
LinkDB: A0A195FWY9_9HYME
Original site: A0A195FWY9_9HYME 
ID   A0A195FWY9_9HYME        Unreviewed;      1374 AA.
AC   A0A195FWY9;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Glutamate receptor, ionotropic kainate 2 {ECO:0000313|EMBL:KYN45170.1};
GN   ORFNames=ALC56_00420 {ECO:0000313|EMBL:KYN45170.1};
OS   Trachymyrmex septentrionalis.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Trachymyrmex.
OX   NCBI_TaxID=34720 {ECO:0000313|EMBL:KYN45170.1, ECO:0000313|Proteomes:UP000078541};
RN   [1] {ECO:0000313|EMBL:KYN45170.1, ECO:0000313|Proteomes:UP000078541}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tsep2-gDNA-1 {ECO:0000313|EMBL:KYN45170.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KYN45170.1};
RA   Nygaard S., Hu H., Boomsma J., Zhang G.;
RT   "Trachymyrmex septentrionalis WGS genome.";
RL   Submitted (MAR-2016) 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; KQ981193; KYN45170.1; -; Genomic_DNA.
DR   STRING; 34720.A0A195FWY9; -.
DR   Proteomes; UP000078541; 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:0007154; P:cell communication; IEA:UniProt.
DR   Gene3D; 1.10.287.70; -; 2.
DR   Gene3D; 3.40.50.2300; -; 3.
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; IPR028082; Peripla_BP_I.
DR   PANTHER; PTHR18966; IONOTROPIC GLUTAMATE RECEPTOR; 1.
DR   PANTHER; PTHR18966:SF422; KAINATE-TYPE IONOTROPIC GLUTAMATE RECEPTOR SUBUNIT 1D; 1.
DR   Pfam; PF01094; ANF_receptor; 2.
DR   Pfam; PF00060; Lig_chan; 2.
DR   Pfam; PF10613; Lig_chan-Glu_bd; 2.
DR   PRINTS; PR00177; NMDARECEPTOR.
DR   SMART; SM00918; Lig_chan-Glu_bd; 2.
DR   SMART; SM00079; PBPe; 2.
DR   SUPFAM; SSF53822; Periplasmic binding protein-like I; 1.
DR   SUPFAM; SSF53850; Periplasmic binding protein-like II; 2.
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:KYN45170.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078541};
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        116..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        154..173
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        222..240
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        418..440
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        476..493
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        996..1015
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1072..1094
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1258..1285
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          20..391
FT                   /note="Ionotropic glutamate receptor C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00079"
FT   DOMAIN          30..98
FT                   /note="Ionotropic glutamate receptor L-glutamate and
FT                   glycine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00918"
FT   DOMAIN          862..1236
FT                   /note="Ionotropic glutamate receptor C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00079"
FT   DOMAIN          872..940
FT                   /note="Ionotropic glutamate receptor L-glutamate and
FT                   glycine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00918"
SQ   SEQUENCE   1374 AA;  155702 MW;  128C380B5EA2B3FD CRC64;
     MESEKQHFRH ILLFYYRKGK NAVQARKNAP YIMEVIDGST RGVLIGQKRY EGYCIDLINK
     IAEFLEFKSV VFQLVTDGYG NYNPQTKTWN GLIRSILDYE ADFAVSDLTI TPLRMAVVDF
     SLPFMITGFS IIISKPEKHT SSFFPVLMPF SIEVWLSMAI ACFVVSIMLF LQAKMTPRKW
     NNRHLCNADP EESNFNFKNS FYLTTGSFMQ QSSNIRTKAS SLRMLASIWW FFTLIMYSSY
     TANQAAFLNM DKISIKGIED LPKQIKIKYG ALKNGATAAF FKNSNHSTYQ QMWIAMVNSS
     PSVFASSYEE GIYRVLRGEG RYAFLMESGA IEYITKRQCN LIKIGNVVEK NRGYGIAMPR
     NSPYRIPINR AILKLGETGT LAEIRKKWWE ERGGGLCKKD EMENDERTNQ LGMASLKGVF
     FVLMCSCSAS FFIAICEFLW NVRKVAVTEK ITTWKVLVAE LKFAVNVFAI TKPVKITYLF
     SIILISLVLA TRIHGLMRPI KIGAIFHKGD ENLNSTFIKA IFDTKYENLA PAFELIPVIK
     YIDANTDSFK TGVAACELLE EGVAAIFGPA SRYTRSIVAS IAARFDIPHI EYVWRENEGL
     IEKNKKKKTL SSMTINVFPA SEKVGQAIAD VIALMNWRNF AAIYETDEGL SRLQKTLTLK
     GDKENPIVHT VRQLNEGSDY RTMLKEIRSL SDSSKLSILE MQHGNVNITG LSIRENDDIE
     GIDWVFIQEP QFFINNEYNL DSAVLYDAVF LLQKALETLN ARNDNEEYID PIPLFCTNST
     NKYQVGRNIT NVMRELSKKG KITGVMNIDE YGRRQDFNVK ILNFQPSGTV KIGFWEPSSG
     VNVIRTEKEE DSYLYKSMEE KIFKISVIEN APYIVEVIDG STRGVLIGQK RYEGYCIDLI
     NEIARSLHFK GVVFEIETDK QGKLDPITKT WNGLIRRIVD HEADLAICDL TITHERKSAV
     DFSHPFMNLG ISIIFGRPEE KTPDFFSFLL PLSTEVWFYM ATAFLGVSIM LFLQARMAPE
     EWDNPHPCIA DPEELENNFN FKNSSWLTIG SLMQQGSDIL PKAPSLRMLA SMWWFFTLIM
     ISSYTANLAA FLTVDKMDAP IKGVEDLAKQ TKIQYGAQEG GSTSTFFKNS NYSTYKRVWT
     AMIDARPSVF TSSNKDGIDR VVKAKGQYAY FMESSSIDYE LERNCEIIKV GGLIDNKGYG
     IAMPRNSPYR IPINRAILKL GETGTLAEIR KKWWEERGGG LCKKDETEKS ENTSELGLAN
     VGGVFFVLMC GLCGSFFIAI CEFLWNIRKV AVTEKITPWE ALIAELKFVV NVFEVTKPVK
     ISKSSNNSAS SMGGLGRAAS TARSIVGSFL RLDMVDKFDK DLSTNNRTND HKIN
//
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