ID A0A158NYN4_ATTCE Unreviewed; 1030 AA.
AC A0A158NYN4;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Glutamate receptor ionotropic, kainate 2-like {ECO:0008006|Google:ProtNLM};
GN Name=105625941 {ECO:0000313|EnsemblMetazoa:XP_012062642.1};
OS Atta cephalotes (Leafcutter ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Atta.
OX NCBI_TaxID=12957 {ECO:0000313|EnsemblMetazoa:XP_012062642.1, ECO:0000313|Proteomes:UP000005205};
RN [1] {ECO:0000313|Proteomes:UP000005205}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21347285; DOI=10.1371/journal.pgen.1002007;
RA Suen G., Teiling C., Li L., Holt C., Abouheif E., Bornberg-Bauer E.,
RA Bouffard P., Caldera E.J., Cash E., Cavanaugh A., Denas O., Elhaik E.,
RA Fave M.J., Gadau J., Gibson J.D., Graur D., Grubbs K.J., Hagen D.E.,
RA Harkins T.T., Helmkampf M., Hu H., Johnson B.R., Kim J., Marsh S.E.,
RA Moeller J.A., Munoz-Torres M.C., Murphy M.C., Naughton M.C., Nigam S.,
RA Overson R., Rajakumar R., Reese J.T., Scott J.J., Smith C.R., Tao S.,
RA Tsutsui N.D., Viljakainen L., Wissler L., Yandell M.D., Zimmer F.,
RA Taylor J., Slater S.C., Clifton S.W., Warren W.C., Elsik C.G., Smith C.D.,
RA Weinstock G.M., Gerardo N.M., Currie C.R.;
RT "The genome sequence of the leaf-cutter ant Atta cephalotes reveals
RT insights into its obligate symbiotic lifestyle.";
RL PLoS Genet. 7:e1002007-e1002007(2011).
RN [2] {ECO:0000313|EnsemblMetazoa:XP_012062642.1}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (APR-2016) to UniProtKB.
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; ADTU01004095; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADTU01004096; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADTU01004097; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADTU01004098; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADTU01004099; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADTU01004100; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADTU01004101; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADTU01004102; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADTU01004103; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADTU01004104; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_012062642.1; XM_012207252.1.
DR AlphaFoldDB; A0A158NYN4; -.
DR EnsemblMetazoa; XM_012207252.1; XP_012062642.1; LOC105625941.
DR GeneID; 105625941; -.
DR KEGG; acep:105625941; -.
DR eggNOG; KOG1052; Eukaryota.
DR InParanoid; A0A158NYN4; -.
DR OrthoDB; 1011589at2759; -.
DR Proteomes; UP000005205; 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; cd06382; PBP1_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; 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 InterPro; IPR001638; Solute-binding_3/MltF_N.
DR PANTHER; PTHR18966:SF598; EYE-ENRICHED KAINATE RECEPTOR, ISOFORM B; 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; 2.
DR SMART; SM00079; PBPe; 1.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000005205};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
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 SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1030
FT /note="Glutamate receptor ionotropic, kainate 2-like"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007629754"
FT TRANSMEM 611..630
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 687..709
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 873..897
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 423..487
FT /note="Ionotropic glutamate receptor L-glutamate and
FT glycine-binding"
FT /evidence="ECO:0000259|SMART:SM00918"
FT DOMAIN 481..849
FT /note="Ionotropic glutamate receptor C-terminal"
FT /evidence="ECO:0000259|SMART:SM00079"
FT DOMAIN 491..555
FT /note="Ionotropic glutamate receptor L-glutamate and
FT glycine-binding"
FT /evidence="ECO:0000259|SMART:SM00918"
FT REGION 903..929
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 913..929
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1030 AA; 117401 MW; 2D78C87B35D6A91B CRC64;
MNLGCLVASI FVLQLLQLPL VLDALPSVVK IGAIFTHDQK DSSTELAFKY AVYKINKDKI
ILPKTTLEYD IQYVPKDDSF HASKKACQQV KHGVQAVFGP SDPILGQHIH SICDALDIPH
LEARLDLETE AKEFSINLYP AQSLLNTAYQ DIMEFFNWTK VVIIYEDDHG LMKLRELVKS
PKIRGIEVSL RQADPNSYRQ VLSEMKSKEF RNIIVDTKPE HMHHFLRMIL QLQMNDYKYH
YLFTTFDIET FDLEDFKYNF VNITAFRLVD ADDVGVRSIL RDMERYQPSG NTILNKSRII
QAEPALIYDS VQVFAVGLRT LEQSHALRPA NISCELEHPW DGGLSLTNYI NSVEMKGISG
PIEFKEGRRI QFKLDLLKLK QHSLVKVGEW RPGAGVNVTD TAAFFEPNIG NVTLIVITIL
ETPYVMMHHE KNYTGNSRFY GFCMDLLAAV AREVGFSYRL ELVPDRKYGA RDPETGEWNG
IVRELMRHEQ PYVMLKSEGN FSGNMRYEGF CIDLLKKIAH MVGFTYRIEL VPDGKYGVYD
YETGEWNGIV RQLMDKRADL AVGSMTINYA RERVIDFTKP FMNLGISILF KVPTRHQARL
FSFMNPLAIE IWLYVLAAYV LVSVTMFVVA RFSPYEWNNP HPCHPGTEIV ENQFSLSNSF
WFTIGTLMQQ GSDLNPKATS TRIVGGIWWF FTLIIISSYT ANLAAFLTVE RMITPIENAE
DLASQTDIAY GTLDSGSTMT FFRDSMVETY KKMWRFMENK KPSVFVPTYE EGIQRVLHGD
YAFLMESTML DYIVQRDCNL TQIGGLLDTK GYGIATPMGS PWRDKISLAI LELQEKGEIQ
ILYDKWWKSP EDTCMRTEKG KENKANSLGV DNIGGVFVVL LCGLAFAVLI AIFEFCYNSK
RNAPAERQRP PAPSTPISGS LQGISQAVQQ QQQQQQCQQQ HQQPPNQQES LCSEMARELC
RALRCRASSR RRCTCDKCST HVIGYSPDNP TATPVNGMRS QRSNLAVPVV ELPPHIHMHH
HAPPHDYDGN
//
