ID W8BXV3_CERCA Unreviewed; 929 AA.
AC W8BXV3;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Glutamate receptor ionotropic, kainate 3 {ECO:0000313|EMBL:JAB94069.1};
GN Name=GRIK3 {ECO:0000313|EMBL:JAB94069.1};
OS Ceratitis capitata (Mediterranean fruit fly) (Tephritis capitata).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Tephritoidea;
OC Tephritidae; Ceratitis; Ceratitis.
OX NCBI_TaxID=7213 {ECO:0000313|EMBL:JAB94069.1};
RN [1] {ECO:0000313|EMBL:JAB94069.1}
RP NUCLEOTIDE SEQUENCE.
RA Geib S.;
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:JAB94069.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=24495485; DOI=10.1186/1471-2164-15-98;
RA Calla B., Hall B., Hou S., Geib S.M.;
RT "A genomic perspective to assessing quality of mass-reared SIT flies used
RT in Mediterranean fruit fly (Ceratitis capitata) eradication in
RT California.";
RL BMC Genomics 15:98-98(2014).
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; GAMC01012486; JAB94069.1; -; mRNA.
DR EMBL; GAMC01012485; JAB94070.1; -; mRNA.
DR AlphaFoldDB; W8BXV3; -.
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 CDD; cd06382; PBP1_iGluR_Kainate; 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 PANTHER; PTHR18966:SF349; FI04462P-RELATED; 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 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 2: Evidence at transcript level;
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:JAB94069.1};
KW Signal {ECO:0000256|SAM:SignalP}; 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..39
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 40..929
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007737154"
FT TRANSMEM 553..574
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 629..651
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 818..838
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 422..791
FT /note="Ionotropic glutamate receptor C-terminal"
FT /evidence="ECO:0000259|SMART:SM00079"
FT DOMAIN 432..497
FT /note="Ionotropic glutamate receptor L-glutamate and
FT glycine-binding"
FT /evidence="ECO:0000259|SMART:SM00918"
FT REGION 871..929
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 881..897
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 913..929
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 929 AA; 104513 MW; 0011A3431E2AB792 CRC64;
MAHQLRQHGL PHFRASIPRC LRLAFALLIT LNCLQIANSQ KTNVGLIYES TKPEMEKIFQ
MAIAQANEDS GGELELHGIA VAIEPGNAFE TSKKLCKMLR QNLVAVFGPT TDLAAKHAMS
ICDAKELPFI DTRWDFGVQM PTVNLYPHAS QLALALKDLV VALEWSDTFT IIYETGEFLP
TVNELLQMYG TAGPTITLRR YELDLNGDYR NVLRRIKNSG DYSFVVVGSM ATLPEFFKQA
QQVGLMTSDY RYIVGNLDLQ TIDLEPFQHG DTNITGMRLV SPEMENVQNL AKALYETDDP
FQNVSCPLTT NMALVYDGVQ LLAETFKHVM FRAVPLNCND ASSWDKGYTL VNYMKSLSLN
GLTGEVKFDY EGLRSDFTLD VIELSMSGMQ KIGEWKTEDG FIANRPPPKI VEQDQRSLVN
KSFVVITAIS EPYGMLKETA AKLEGNDQFE GFGIELIEEL GKKLGFSFTF RLQEDNKYGS
FNPKTGKFDG MMLEIIEGRA DMGITDLTMT SIREEGVDFT IPFMNLGIAI LFRKPMKEPP
KLFSFMSPFS GTVWMWLGIA YLSVSLTLFI LGRISPTEWD NPYPCIEEPT ELENQFSFPN
CLWFSTGALL QQGSELAPKA YSTRTVASIW WFFTLILVSS YTANLAAFLT IESLSSPIEN
AEDLAANKGG VKYGAKVGGS TFTFFQDAKY PTYQKMYEFM RDNPEYMTST NAEGVDRVEN
DNYAFLMEST TIEYITERRC SLTQVGSLLD EKGYGIAMRK NWPYRDILSQ AVLELQEQGV
LTKMKTKWWK EKRGGGACSQ EGENDGAEEL GIANLGGVYF VLFVGSIFAS IYGFVEWICH
VYGTARRNKV SFKTELIEEF RFVMQCSGNT RPVKYPKNSS RSRSRSSRSR SHSRSHSRSS
SKSSTLSVDS LPLDESKLHH ISEHTKHAK
//
