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Database: UniProt
Entry: A0A2A4JH89_HELVI
LinkDB: A0A2A4JH89_HELVI
Original site: A0A2A4JH89_HELVI 
ID   A0A2A4JH89_HELVI        Unreviewed;       706 AA.
AC   A0A2A4JH89;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Ionotropic glutamate receptor C-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
DE   Flags: Fragment;
GN   ORFNames=B5V51_2395 {ECO:0000313|EMBL:PCG70954.1};
OS   Heliothis virescens (Tobacco budworm moth).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC   Noctuidae; Heliothinae; Heliothis.
OX   NCBI_TaxID=7102 {ECO:0000313|EMBL:PCG70954.1, ECO:0000313|Proteomes:UP000218220};
RN   [1] {ECO:0000313|EMBL:PCG70954.1, ECO:0000313|Proteomes:UP000218220}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HvINT- {ECO:0000313|EMBL:PCG70954.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:PCG70954.1};
RA   Fritz M.L., Deyonke A.M., Papanicolaou A., Micinski S., Westbrook J.,
RA   Gould F.;
RT   "Contemporary evolution of a Lepidopteran species, Heliothis virescens, in
RT   response to modern agricultural practices.";
RL   Submitted (SEP-2017) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PCG70954.1}.
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DR   EMBL; NWSH01001530; PCG70954.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A4JH89; -.
DR   STRING; 7102.A0A2A4JH89; -.
DR   Proteomes; UP000218220; 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   GO; GO:0007154; P:cell communication; IEA:UniProt.
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; 1.
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; 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   Receptor {ECO:0000256|ARBA:ARBA00023170};
KW   Reference proteome {ECO:0000313|Proteomes:UP000218220};
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        299..319
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        386..407
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        570..596
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          175..546
FT                   /note="Ionotropic glutamate receptor C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00079"
FT   DOMAIN          187..253
FT                   /note="Ionotropic glutamate receptor L-glutamate and
FT                   glycine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00918"
FT   REGION          628..706
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        628..643
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        648..663
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:PCG70954.1"
SQ   SEQUENCE   706 AA;  77869 MW;  78D9CC4A0DC60929 CRC64;
     DDALLRNLLL VLKKAGLTNF IVWCEAACAV RVLDAAQRVG LLAERHSYIV LSLDLHTQPL
     HDYSHGGANV TGFRLFDPEA PEVVEVMDQW RKMYAERLGG AADEEGGDNS LEAEEAAAIA
     AAPPTALLLA HLGTELVAEA WRRLQLPPAA AADCAAGAGA FHADTLLNYL RSARAVSYGN
     CLLQSDPYVM MKESTDRLSG NDRYEGFCIE LIDQLARLLQ FNYTFVQNED GDYGPTKDNV
     TGKWTGMLGS LMEDKNIDFA VTDLTITAER ERAVDFTTPF MNLGISILFR TPKQPEPKIF
     AFLLPFSNGV WLCLGFAYLG TSLLLYVVGR LCHEEWQNPY PCIEEPPALE NQFTLANALW
     FNLGAVLLQG SEIAPVAYST RAVASVWWLF ALVITSSYTA NLATLLAKKS SDQVITNVQE
     LADNQLGIDY GAKHGGSTYT FFQHSQSELY QRMFQHMRTR KMPASNPEGI AKVESGKYAF
     LMESTSIDYL TERNCGVTKV GSLLDSKGYG IAMKKNSPYR QAMNLGLLNL QEAGTLREMQ
     HTWWKEKHGG GACKVDEEHE SEELNMSNFL GLWLVLVVGS ALGIVLSCCD LAWAAARRAR
     ASGRRFHVHF WEELRFVFRF EQSVKPLQGP LSGTPSSSAR SEAAEAEAET EAETEAEAEA
     GAEAEEPAEP RGRSGSGARR RRSSMHAASL RLARHTNRDS ATPARR
//
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