ID A0A0L0BWW1_LUCCU Unreviewed; 1778 AA.
AC A0A0L0BWW1;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Glutamate receptor ionotropic, kainate 2 {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=FF38_05203 {ECO:0000313|EMBL:KNC24496.1};
OS Lucilia cuprina (Green bottle fly) (Australian sheep blowfly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Oestroidea;
OC Calliphoridae; Luciliinae; Lucilia.
OX NCBI_TaxID=7375 {ECO:0000313|EMBL:KNC24496.1, ECO:0000313|Proteomes:UP000037069};
RN [1] {ECO:0000313|EMBL:KNC24496.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LS {ECO:0000313|EMBL:KNC24496.1};
RC TISSUE=Full body {ECO:0000313|EMBL:KNC24496.1};
RX PubMed=26108605; DOI=10.1038/ncomms8344;
RA Anstead C.A., Korhonen P.K., Young N.D., Hall R.S., Jex A.R., Murali S.C.,
RA Hughes D.S., Lee S.F., Perry T., Stroehlein A.J., Ansell B.R.,
RA Breugelmans B., Hofmann A., Qu J., Dugan S., Lee S.L., Chao H., Dinh H.,
RA Han Y., Doddapaneni H.V., Worley K.C., Muzny D.M., Ioannidis P.,
RA Waterhouse R.M., Zdobnov E.M., James P.J., Bagnall N.H., Kotze A.C.,
RA Gibbs R.A., Richards S., Batterham P., Gasser R.B.;
RT "Lucilia cuprina genome unlocks parasitic fly biology to underpin future
RT interventions.";
RL Nat. Commun. 6:7344-7344(2015).
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:KNC24496.1}.
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DR EMBL; JRES01001223; KNC24496.1; -; Genomic_DNA.
DR EnsemblMetazoa; KNC24496; KNC24496; FF38_05203.
DR OMA; SIEYETQ; -.
DR Proteomes; UP000037069; 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; 2.
DR CDD; cd13714; PBP2_iGluR_Kainate; 2.
DR Gene3D; 1.10.287.70; -; 2.
DR Gene3D; 3.40.50.2300; -; 4.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 4.
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:SF349; FI04462P-RELATED; 1.
DR PANTHER; PTHR18966; IONOTROPIC GLUTAMATE RECEPTOR; 1.
DR Pfam; PF01094; ANF_receptor; 2.
DR Pfam; PF00060; Lig_chan; 2.
DR Pfam; PF10613; Lig_chan-Glu_bd; 2.
DR Pfam; PF00497; SBP_bac_3; 2.
DR PRINTS; PR00177; NMDARECEPTOR.
DR SMART; SM00918; Lig_chan-Glu_bd; 2.
DR SMART; SM00079; PBPe; 2.
DR SUPFAM; SSF53822; Periplasmic binding protein-like I; 2.
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:UP000037069};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
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 TRANSMEM 494..511
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 531..552
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 605..627
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 801..820
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1425..1444
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1501..1523
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1694..1719
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 400..775
FT /note="Ionotropic glutamate receptor C-terminal"
FT /evidence="ECO:0000259|SMART:SM00079"
FT DOMAIN 411..475
FT /note="Ionotropic glutamate receptor L-glutamate and
FT glycine-binding"
FT /evidence="ECO:0000259|SMART:SM00918"
FT DOMAIN 1298..1668
FT /note="Ionotropic glutamate receptor C-terminal"
FT /evidence="ECO:0000259|SMART:SM00079"
FT DOMAIN 1305..1369
FT /note="Ionotropic glutamate receptor L-glutamate and
FT glycine-binding"
FT /evidence="ECO:0000259|SMART:SM00918"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KNC24496.1"
SQ SEQUENCE 1778 AA; 200884 MW; AFF38C5C14E631D5 CRC64;
DNFDISPPVE PNYHIPIGLI TDVNSEILRQ TFDYAISIIN SDLSVPLMGY QEEIDYGNSL
QGFNRLCKLM QTGVGAVFGP SAKHTGTHLM NVCDSKDLPY VYSHMSEAIE GFNLHPHPLD
IAKALHAIIT EFEWTRFIFL YENSEYLSIL NSLMSFYGTK GPIISVMRYD LNLNGNFKSV
LRRVRKSVDS RIVVVGSTTS VAELLKQAQQ VGIINEDYKY IIGNLDFHTF DLEEYKYSEA
NITGFRLFSA EQPEVQNLML ELGFIDDLEE NEMITNGSCP ITTEMALIYD AVIAFAETTK
HIHYMPQALN CSVFADNVQE DGSTFKNYMR SLLIDKNTLT GRIFFEGNVR KGFTLDVIEL
QSTGLVKVGT WEDNKNFTFQ RPPQIKIMLD TDDNSMVNKT FRVLIAVPNK PYASLVDSHK
KLDGNAQYEG YSIDLIKELA DKLGFNFTFI NGGNDYGSFN KTTNVTTGML KEIVEGRADL
AITDLTITSE REEVIDFSIP FMNLGIAILY LKPQKGEPTT FSFMDPFSKQ VWKYLGIAYL
GVSICFFILG RLSPTEWDNP YPCIEEPEEL ENQFTINNSL WFTTGAFLQQ GSEIAPKALS
TRTVAAIWCF FTLIMVSSYT ANLAAFLTIE NPTKVLENVK DLADNKGGVQ YGAKRTGSTR
NFFLTSEEEI YKKMNEYMLE NPHLLTETNL EGVQRVVNSD VASGSTYAFL MESTSIEYNI
VRECMLQKVG EPLDEKGYGI AMVKNWPYRD KFNNALLELQ EQGVLAQLKQ KWWNEVGAGV
CNAKNDGGMV SALDFANLEG IYYVLIVGST ISMCYGIILW CFNVNKKARY YDVPFRDALT
EEFKVLIDFT NNVRMLKSAH SVYSRSRHSS LDSFETDSGE ESEDAILKTT SAQYGGYSHY
DDISSSSADI ITIGLLTDQQ HEEMNIVVDF AIENVNMELQ SALAVIRDQV PYGNSFLGYG
KLCRMMKNGI AAVLGPSSKH TAFHLMSICD AKDIPYFYSF MGDAEAEAFN LYPHQDDLSK
ALYSLLTEFE WSRFIFLYES SEYLNILNGL MAQFGTNSPV ITVLRYDLNL NGNYKTVLRK
VRKSVDNRIV VVGSTETMPE FLKQAQQVGI INEDYKYIIA NLDFHSFDLE EFKYSEANIT
SLRMFSPENN LVRELMEKLG HSFITEGFQN GSCPITMEMA LTYDAIQLFA ETTKHIPLKP
TPLNCTDRSD SVRDDGSTFK NYMRSLNIHE NTLTGRIYFE GNVRKGFTFD VIELQPSGIV
QVGTWDETNN YTSQRLAPTN AIFENVDNSL ANKTFIILLS VPNKPYASLV ESHKKLEGNS
QYEGYSVDLI KELSGKLGFN YTFVNGGNDY GTFNKTSNIS TGMLKEIMEG RADLAITDLT
ITSEREEAID FTIPFMNLGI AILFLKPQKA APDTFSFMDP FNKDVWEYLG LAFIGVSLSF
YILGRLSPTE WDNPYPCIEE PTELENQFTL SNSLWFTTGA LLQQGSEIAP KALSVRTMAS
IWWFFTLIMV SSYTANLAAF LTVETPKVLI ENVDDLAENK EGVVYGAKRT GSTRNFFLTS
ADPRYKKMNL FMEKHPELLT ENNQEGVQRV IDAKDSEPKY AFLMESTSIE YNTVRECSLK
KIGDALDEKG YGIAMRKNWA YRDKFNNALL ELQEQGVLAK MKNKWWNEVG AGICASKKEQ
SDANSLNMKN LEGIYVVLVF GSGMALIHGI ISWICFVIHK ARSHKVPLKA AFVEEFKFVM
EFTTYTRELK NSASIYSRSR NSSINIESLD NVLNTIDN
//
