ID W8BBL3_CERCA Unreviewed; 967 AA.
AC W8BBL3;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Glutamate receptor ionotropic, kainate 2 {ECO:0000313|EMBL:JAB96067.1};
GN Name=GRIK2 {ECO:0000313|EMBL:JAB96067.1};
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:JAB96067.1};
RN [1] {ECO:0000313|EMBL:JAB96067.1}
RP NUCLEOTIDE SEQUENCE.
RA Geib S.;
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:JAB96067.1}
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; GAMC01010490; JAB96065.1; -; mRNA.
DR EMBL; GAMC01010488; JAB96067.1; -; mRNA.
DR RefSeq; XP_004521947.1; XM_004521890.2.
DR RefSeq; XP_004521948.1; XM_004521891.2.
DR RefSeq; XP_012155442.1; XM_012300052.1.
DR RefSeq; XP_012155443.1; XM_012300053.1.
DR AlphaFoldDB; W8BBL3; -.
DR EnsemblMetazoa; XM_012300052.2; XP_012155442.1; LOC101456558.
DR EnsemblMetazoa; XM_020857544.1; XP_020713203.1; LOC101456558.
DR EnsemblMetazoa; XM_020857545.1; XP_020713204.1; LOC101456558.
DR EnsemblMetazoa; XM_020857546.1; XP_020713205.1; LOC101456558.
DR EnsemblMetazoa; XM_020857548.1; XP_020713207.1; LOC101456558.
DR GeneID; 101456558; -.
DR OrthoDB; 1011589at2759; -.
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; 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; 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:SF599; FI01405P; 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:JAB96067.1};
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..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..967
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007737044"
FT TRANSMEM 610..629
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 686..708
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 872..896
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 480..848
FT /note="Ionotropic glutamate receptor C-terminal"
FT /evidence="ECO:0000259|SMART:SM00079"
FT DOMAIN 490..554
FT /note="Ionotropic glutamate receptor L-glutamate and
FT glycine-binding"
FT /evidence="ECO:0000259|SMART:SM00918"
SQ SEQUENCE 967 AA; 111341 MW; 3B3C03CCF5307ECF CRC64;
MIMLLINVIY FQLLKALNFV YITLPKIIKN GTEKAIEFTW IEVISKTECN CVLYYFNRRF
AIKYYTLTSR KVSTSHFLLL YFLSNILCAA ALPPVIRLGA IFTEDQRDSS VEFSFKYAVY
RINKDKLLLS NTQLIYDIEY VPRDDSFRTT KKVCRQLELG VNAIFGPSDP LLAAHVQSIC
ESFDIPHIES RIDYKASIKE FSINLYPSQR LMNLAHRDLM VFLNWTKTAI IYEDDFGLFN
QQDLIRATTD LKIEIYIRQA SPETYRRVLR AIRQKEIYKI IVDTNPAYIN SFFRTILQLQ
MNDYRYHYMF TTFDLETFDL EDFKYNGVNI TAFRLVDVKS QRYEEVIEQM MKLPHSGLEY
INGQPYIQTQ SALMFDSVYT FAAGLTELDR SHLLRFHNIS CSNDMSWNDG LSLYNYINSV
SIHGLTGHVS FVEGYRNRFQ IDLLKLKHKK IEKVGIWKPD VGVNITDPTA FYEIHTSNTT
LIVMTREEKP YVMVRNEGNQ IGNSRFEGFC IDLLEAIATQ VGFHYKIELV PDNMYGVYNP
DSNSWNGIVR ELMERRADLA VASMTINYAR ESVIDFTKPF MNLGIGILFK VPTSQPTRLF
SFMNPLAMEI WLYVLGAYVL VSFTLFVMAR FSPYEWNNPH PCLIDSDIVE NQFSVSNSFW
FITGTFLRQG SGLNPKATST RIVGGIWWFF TLIIISSYTA NLAAFLTVER MITPIESASD
LADQTDISYG TLEGGSTMTF FRDSKIDIYR KMWEYMEKRR SSVFVKTYEE GIKHVLEGNY
AFLMESTMLD YAVQRDCNLT QIGGLLDSKG YGIATPKGSI WRDPMSLAIL ELQEKGIIQI
LYDKWWKNTG DVCNRDEKSK ESKANALGIE NIGGVFVVLL CGLALAVVVA ILEFCWHSKK
TVQLTENQSL CSEMAEELRY AIHCHASKKR PSLKRICVKC TPDSTYVPVN LGSGTPNISG
VHYNFFN
//
