ID A0A1A9UPZ5_GLOAU Unreviewed; 915 AA.
AC A0A1A9UPZ5;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Ionotropic glutamate receptor C-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
OS Glossina austeni (Savannah tsetse fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Hippoboscoidea;
OC Glossinidae; Glossina.
OX NCBI_TaxID=7395 {ECO:0000313|EnsemblMetazoa:GAUT011688-PA, ECO:0000313|Proteomes:UP000078200};
RN [1] {ECO:0000313|Proteomes:UP000078200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TTRI {ECO:0000313|Proteomes:UP000078200};
RA Aksoy S., Warren W., Wilson R.K.;
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:GAUT011688-PA}
RP IDENTIFICATION.
RC STRAIN=TTRI {ECO:0000313|EnsemblMetazoa:GAUT011688-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) 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 AlphaFoldDB; A0A1A9UPZ5; -.
DR STRING; 7395.A0A1A9UPZ5; -.
DR EnsemblMetazoa; GAUT011688-RA; GAUT011688-PA; GAUT011688.
DR VEuPathDB; VectorBase:GAUT011688; -.
DR OrthoDB; 1011589at2759; -.
DR Proteomes; UP000078200; 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 CDD; cd13717; PBP2_iGluR_putative; 1.
DR Gene3D; 1.10.287.70; -; 1.
DR Gene3D; 3.40.50.2300; -; 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; IPR028082; Peripla_BP_I.
DR InterPro; IPR001638; Solute-binding_3/MltF_N.
DR PANTHER; PTHR18966; IONOTROPIC GLUTAMATE RECEPTOR; 1.
DR PANTHER; PTHR18966:SF411; IONOTROPIC RECEPTOR 25A; 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.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 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 Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
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..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..915
FT /note="Ionotropic glutamate receptor C-terminal domain-
FT containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008398740"
FT TRANSMEM 535..554
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 610..633
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 830..854
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 411..808
FT /note="Ionotropic glutamate receptor C-terminal"
FT /evidence="ECO:0000259|SMART:SM00079"
FT DOMAIN 421..480
FT /note="Ionotropic glutamate receptor L-glutamate and
FT glycine-binding"
FT /evidence="ECO:0000259|SMART:SM00918"
SQ SEQUENCE 915 AA; 104687 MW; 297C601F9C44569C CRC64;
MRDFNALLAL TAIVAVLALF NSNVNGQTSQ NINVLFINEI DNDPASKAVE VVETYLKKNA
QYGLTLRIER IEANKTDAKD LLETSVASET VKSFTQALGL PTISASYGQE GDLRQWRDID
ANKQKYLLQI MPPADIIPEV VRSIVRKMNI TNAAILYDET FIMDHKYKSL LQNIQTRHVI
ARIAQGDRER TEEIEKLRNL DINNFFILGS LRTIGPVLEA VKSAYFQRNF AWHVITQDEG
EIASKRDNAT LMFLKPVVYA QRRERLGQLR TTYNLNEPPQ IMTVFYFDLA LRAFLTVRDM
IQANAWPKDM IYMGCDDYQG ENTPIRNLDL KEYFIKVNEP TSYGQFELVS EQGKPFNGYS
YVKFEMDIDM VEIRGGNSVN SKPIGRWTAG LDTPLMIKDA TAINNLTADT IYRVYTVLQA
PFIMRDAKAP KGYKGYCIDL INEIAAIVHF DYTIQEVEDG KFGNMDENGH WNGVVKKLID
KQADIGLGSM SVMAEREIVI DYTVPYYDLV GITIMMQRPS APSSLFKFLT VLETNVWLCI
LAAYFFTSFL MWIFDRWSPY SYQNNREKYK DDDEKREFNL KECLWFCMTS LTPQGGGEAP
KNLSGRLVAA TWWLFGFIII ASYTANLAAF LTVSRLDTPV ESLDDLAKQY KILYAPLNGS
SAMTYFERMA NIEQMFYEIW KDLSLNDSLT PLERSKLAVW DYPVSDKYTK MWQAMQEAQL
PANLEEAVAR VRNSTSATGF AFLGDATDIR YLVMTNCDLQ VVGEEFSRKP YAIAVQQGSH
LKDQFNNAIL TLLNKRQLEK LKEKWWKNDE IQAKCDKPED QSDGISIENI GGVFIVIFVG
IGMACITLLF EYWWYKYRKN PRIIDVTEAV PSGKRGKIPE GIILGRNEKH GNVKSNIVLR
SRFNQYPSKT PKPRF
//
