ID Q9VDH5_DROME Unreviewed; 853 AA.
AC Q9VDH5;
DT 01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 171.
DE SubName: Full=Kainate-type ionotropic glutamate receptor subunit 1D {ECO:0000313|EMBL:AAF55818.1};
GN Name=KaiR1D {ECO:0000313|EMBL:AAF55818.1,
GN ECO:0000313|FlyBase:FBgn0038837};
GN Synonyms=CT12759 {ECO:0000313|EMBL:AAF55818.1}, DKaiR1D
GN {ECO:0000313|EMBL:AAF55818.1}, DKaiRID {ECO:0000313|EMBL:AAF55818.1},
GN Dmel\CG3822 {ECO:0000313|EMBL:AAF55818.1}, DmelCG3822
GN {ECO:0000313|EMBL:AAF55818.1};
GN ORFNames=CG3822 {ECO:0000313|EMBL:AAF55818.1,
GN ECO:0000313|FlyBase:FBgn0038837}, Dmel_CG3822
GN {ECO:0000313|EMBL:AAF55818.1};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000313|EMBL:AAF55818.1, ECO:0000313|Proteomes:UP000000803};
RN [1] {ECO:0000313|EMBL:AAF55818.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.H., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Gabor G.L., Abril J.F., Agbayani A.,
RA An H.J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D., Scheeler F., Shen H.,
RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., Spier E.,
RA Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C.,
RA Turner R., Venter E., Wang A.H., Wang X., Wang Z.Y., Wassarman D.A.,
RA Weinstock G.M., Weissenbach J., Williams S.M., WoodageT, Worley K.C.,
RA Wu D., Yang S., Yao Q.A., Ye J., Yeh R.F., Zaveri J.S., Zhan M., Zhang G.,
RA Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.,
RA Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000313|EMBL:AAF55818.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=12537568;
RA Celniker S.E., Wheeler D.A., Kronmiller B., Carlson J.W., Halpern A.,
RA Patel S., Adams M., Champe M., Dugan S.P., Frise E., Hodgson A.,
RA George R.A., Hoskins R.A., Laverty T., Muzny D.M., Nelson C.R.,
RA Pacleb J.M., Park S., Pfeiffer B.D., Richards S., Sodergren E.J.,
RA Svirskas R., Tabor P.E., Wan K., Stapleton M., Sutton G.G., Venter C.,
RA Weinstock G., Scherer S.E., Myers E.W., Gibbs R.A., Rubin G.M.;
RT "Finishing a whole-genome shotgun: release 3 of the Drosophila melanogaster
RT euchromatic genome sequence.";
RL Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002).
RN [3] {ECO:0000313|EMBL:AAF55818.1, ECO:0000313|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4] {ECO:0000313|EMBL:AAF55818.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=12537573;
RA Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R.,
RA Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M., Ashburner M.,
RA Celniker S.E.;
RT "The transposable elements of the Drosophila melanogaster euchromatin: a
RT genomics perspective.";
RL Genome Biol. 3:RESEARCH0084.1-RESEARCH0084.20(2002).
RN [5] {ECO:0000313|EMBL:AAF55818.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=12537574;
RA Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A.,
RA Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G.,
RA Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M.,
RA Karpen G.H.;
RT "Heterochromatic sequences in a Drosophila whole-genome shotgun assembly.";
RL Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002).
RN [6] {ECO:0000313|EMBL:AAF55818.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=16110336; DOI=10.1371/journal.pcbi.0010022;
RA Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D.,
RA Ashburner M., Anxolabehere D.;
RT "Combined evidence annotation of transposable elements in genome
RT sequences.";
RL PLoS Comput. Biol. 1:166-175(2005).
RN [7] {ECO:0000313|EMBL:AAF55818.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=17569856; DOI=10.1126/science.1139815;
RA Smith C.D., Shu S., Mungall C.J., Karpen G.H.;
RT "The Release 5.1 annotation of Drosophila melanogaster heterochromatin.";
RL Science 316:1586-1591(2007).
RN [8] {ECO:0000313|EMBL:AAF55818.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=17569867; DOI=10.1126/science.1139816;
RA Hoskins R.A., Carlson J.W., Kennedy C., Acevedo D., Evans-Holm M.,
RA Frise E., Wan K.H., Park S., Mendez-Lago M., Rossi F., Villasante A.,
RA Dimitri P., Karpen G.H., Celniker S.E.;
RT "Sequence finishing and mapping of Drosophila melanogaster
RT heterochromatin.";
RL Science 316:1625-1628(2007).
RN [9] {ECO:0007829|PDB:5DTB, ECO:0007829|PDB:5EHM}
RP X-RAY CRYSTALLOGRAPHY (1.28 ANGSTROMS) OF 650-794, AND DISULFIDE BONDS.
RX PubMed=27889096; DOI=10.1016/j.neuron.2016.10.058;
RA Li Y., Dharkar P., Han T.H., Serpe M., Lee C.H., Mayer M.L.;
RT "Novel Functional Properties of Drosophila CNS Glutamate Receptors.";
RL Neuron 92:1036-1048(2016).
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; AE014297; AAF55818.1; -; Genomic_DNA.
DR RefSeq; NP_650925.1; NM_142668.3.
DR PDB; 5DTB; X-ray; 1.84 A; A/B=411-527, A/B=650-794.
DR PDB; 5EHM; X-ray; 1.28 A; A/B=411-529, A/B=650-794.
DR PDBsum; 5DTB; -.
DR PDBsum; 5EHM; -.
DR AlphaFoldDB; Q9VDH5; -.
DR SMR; Q9VDH5; -.
DR IntAct; Q9VDH5; 1.
DR STRING; 7227.FBpp0083391; -.
DR PaxDb; 7227-FBpp0083391; -.
DR EnsemblMetazoa; FBtr0083987; FBpp0083391; FBgn0038837.
DR GeneID; 42473; -.
DR KEGG; dme:Dmel_CG3822; -.
DR UCSC; CG3822-RA; d. melanogaster.
DR AGR; FB:FBgn0038837; -.
DR CTD; 42473; -.
DR FlyBase; FBgn0038837; KaiR1D.
DR VEuPathDB; VectorBase:FBgn0038837; -.
DR eggNOG; KOG1052; Eukaryota.
DR HOGENOM; CLU_007257_1_1_1; -.
DR InParanoid; Q9VDH5; -.
DR OMA; FICNCRE; -.
DR OrthoDB; 1011589at2759; -.
DR PhylomeDB; Q9VDH5; -.
DR Reactome; R-DME-451307; Activation of Na-permeable kainate receptors.
DR Reactome; R-DME-451308; Activation of Ca-permeable Kainate Receptor.
DR BioGRID-ORCS; 42473; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 42473; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0038837; Expressed in brain and 7 other cell types or tissues.
DR ExpressionAtlas; Q9VDH5; baseline and differential.
DR Genevisible; Q9VDH5; DM.
DR GO; GO:0005886; C:plasma membrane; ISS:FlyBase.
DR GO; GO:0098839; C:postsynaptic density membrane; IBA:GO_Central.
DR GO; GO:0048786; C:presynaptic active zone; IDA:FlyBase.
DR GO; GO:0042734; C:presynaptic membrane; IMP:FlyBase.
DR GO; GO:0008066; F:glutamate receptor activity; IBA:GO_Central.
DR GO; GO:0022849; F:glutamate-gated calcium ion channel activity; IMP:FlyBase.
DR GO; GO:0015277; F:kainate selective glutamate receptor activity; ISS:FlyBase.
DR GO; GO:1904315; F:transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential; IBA:GO_Central.
DR GO; GO:0098703; P:calcium ion import across plasma membrane; IMP:FlyBase.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:1903296; P:positive regulation of glutamate secretion, neurotransmission; IMP:FlyBase.
DR GO; GO:1900075; P:positive regulation of neuromuscular synaptic transmission; IMP:FlyBase.
DR GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; IMP:FlyBase.
DR GO; GO:0099171; P:presynaptic modulation of chemical synaptic transmission; IMP:FlyBase.
DR GO; GO:0060025; P:regulation of synaptic activity; ISS:FlyBase.
DR GO; GO:0035249; P:synaptic transmission, glutamatergic; IBA:GO_Central.
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; 2.
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; IONOTROPIC GLUTAMATE RECEPTOR; 1.
DR PANTHER; PTHR18966:SF422; KAINATE-TYPE IONOTROPIC GLUTAMATE RECEPTOR SUBUNIT 1D; 1.
DR Pfam; PF01094; ANF_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 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:5DTB, ECO:0007829|PDB:5EHM};
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 Proteomics identification {ECO:0007829|PeptideAtlas:Q9VDH5};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000313|EMBL:AAF55818.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000803};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
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 SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..853
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004334582"
FT TRANSMEM 548..567
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 622..644
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 815..836
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 417..786
FT /note="Ionotropic glutamate receptor C-terminal"
FT /evidence="ECO:0000259|SMART:SM00079"
FT DOMAIN 427..492
FT /note="Ionotropic glutamate receptor L-glutamate and
FT glycine-binding"
FT /evidence="ECO:0000259|SMART:SM00918"
FT BINDING 501
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0007829|PDB:5DTB"
FT BINDING 503
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0007829|PDB:5DTB"
FT BINDING 508
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0007829|PDB:5DTB"
FT BINDING 672
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0007829|PDB:5DTB"
FT BINDING 673
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0007829|PDB:5DTB"
FT BINDING 723
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0007829|PDB:5DTB"
FT DISULFID 735..793
FT /evidence="ECO:0007829|PDB:5DTB"
SQ SEQUENCE 853 AA; 95868 MW; BDEE6481C681F23C CRC64;
MRSSGVLVLP LLLLQLILNC RKAQSLPDII KIGGLFHPAD DHQELAFRQA VDRINADRSI
LPRSKLVAQI ERISPFDSFH AGKRVCGLLN IGVAAIFGPQ SSHTASHVQS ICDNMEIPHL
ENRWDYRLRR ESCLVNLYPH PNTLSKAYVD IVRHWGWKTF TIIYENNDGI VRLQELLKAH
GMTPFPITVR QLSDSGDYRP LLKQIKNSAE AHIVLDCSTE RIHEVLKQAQ QIGMMSDYHS
YLVTSLDLHT VNLDEFRYGG TNITGFRLIN EKIVSDVVRQ WSIDEKGLLR SANLTTVRSE
TALMYDAVHL FAKALHDLDT SQQIDIHPIS CDGQSTWQHG FSLINYMKIV EMKGLTNVIK
FDHQGFRTDF MLDIVELTPA GIRKIGTWNS TLPDGINFTR TFSQKQQEIE ANLKNKTLVV
TTILSNPYCM RKESAIPLSG NDQFEGYAVD LIHEISKSLG FNYKIQLVPD GSYGSLNKLT
GEWNGMIREL LEQRADLAIA DLTITFEREQ AVDFTTPFMN LGVSILYRKP IKQPPNLFSF
LSPLSLDVWI YMATAYLGVS VLLFILAKFT PYEWPAYTDA HGEKVESQFT LLNCMWFAIG
SLMQQGCDFL PKALSTRMVA GIWWFFTLIM ISSYTANLAA FLTVERMDSP IESAEDLAKQ
TRIKYGALKG GSTAAFFRDS KISTYQRMWS FMESARPSVF TASNGEGVER VAKGKGSYAF
LMESTSIEYV TERNCELTQV GGMLDTKSYG IATPPNSPYR TAINSVILKL QEEGKLHILK
TKWWKEKRGG GKCRVETSKS SSAANELGLA NVGGVFVVLM GGMGVACVIA VCEFVWKSRK
VAVEERLSAI LNE
//
