IR93A_DROME
ID IR93A_DROME Reviewed; 868 AA.
AC Q9VDH6; Q8IH81; Q8T0V7; Q9VDH7;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-2015, sequence version 3.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Ionotropic receptor 93a {ECO:0000303|PubMed:27161501};
DE Flags: Precursor;
GN Name=Ir93a {ECO:0000303|PubMed:27161501, ECO:0000312|FlyBase:FBgn0259215};
GN ORFNames=CG42315 {ECO:0000312|FlyBase:FBgn0259215};
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:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|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.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., 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.A., 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.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., 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.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|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 [3] {ECO:0000312|EMBL:AAL39173.1, ECO:0000312|EMBL:AAN71127.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 232-868 AND 344-868.
RC STRAIN=Berkeley; TISSUE=Head, and Testis;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27161501; DOI=10.1016/j.cub.2016.03.049;
RA Enjin A., Zaharieva E.E., Frank D.D., Mansourian S., Suh G.S., Gallio M.,
RA Stensmyr M.C.;
RT "Humidity Sensing in Drosophila.";
RL Curr. Biol. 26:1352-1358(2016).
RN [5] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=27656904; DOI=10.7554/elife.17879;
RA Knecht Z.A., Silbering A.F., Ni L., Klein M., Budelli G., Bell R.,
RA Abuin L., Ferrer A.J., Samuel A.D., Benton R., Garrity P.A.;
RT "Distinct combinations of variant ionotropic glutamate receptors mediate
RT thermosensation and hygrosensation in Drosophila.";
RL Elife 5:0-0(2016).
CC -!- FUNCTION: Integral part of various neural sensory systems in the
CC antenna that provide the neural basis for the response to environmental
CC changes in temperature (thermosensation) and humidity (hygrosensation)
CC (PubMed:27161501, PubMed:27656904). Together with Ir21a and Ir25a,
CC mediates the response of the larval dorsal organ cool cells, a trio of
CC cool-responsive neurons, to cooling and is required for cool avoidance
CC behavior (PubMed:27656904, PubMed:27161501). Together with Ir25a and
CC Ir40a, mediates the response of the hydrosensory sacculus neurons to
CC changes in relative humidity, and is required for dry detection and
CC humidiy preference behavior (PubMed:27656904, PubMed:27161501).
CC {ECO:0000269|PubMed:27161501, ECO:0000269|PubMed:27656904}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: In the antenna, detected in sacculus neurons which
CC innervate the first and second chambers (at protein level)
CC (PubMed:27656904). Expressed in multiple cells of the larval dorsal
CC organ ganglion, including the dorsal organ cool cells where it is
CC predominately localized to the dendritic bulbs (at protein level).
CC {ECO:0000269|PubMed:27656904}.
CC -!- DISRUPTION PHENOTYPE: Impaired response to environmental cues such as
CC temperature and humidity (PubMed:27161501, PubMed:27656904). Response
CC of dorsal organ cool cells to changes in temperature is abolished and
CC consequently larvae fail to avoid cool temperatures (PubMed:27161501,
CC PubMed:27656904). Response of sacculus neurons to changes in humidity
CC is abolished and consequently larvae fail to move towards their
CC preferred humidity (PubMed:27161501, PubMed:27656904).
CC {ECO:0000269|PubMed:27161501, ECO:0000269|PubMed:27656904}.
CC -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1)
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN71127.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AE014297; AAF55817.3; -; Genomic_DNA.
DR EMBL; AY069028; AAL39173.1; -; mRNA.
DR EMBL; BT001372; AAN71127.1; ALT_SEQ; mRNA.
DR RefSeq; NP_650924.3; NM_142667.3.
DR AlphaFoldDB; Q9VDH6; -.
DR STRING; 7227.FBpp0288996; -.
DR GlyGen; Q9VDH6; 9 sites.
DR PaxDb; Q9VDH6; -.
DR EnsemblMetazoa; FBtr0336970; FBpp0307913; FBgn0259215.
DR GeneID; 42471; -.
DR KEGG; dme:Dmel_CG42315; -.
DR UCSC; CG42315-RA; d. melanogaster.
DR CTD; 42471; -.
DR FlyBase; FBgn0259215; Ir93a.
DR VEuPathDB; VectorBase:FBgn0259215; -.
DR eggNOG; KOG1052; Eukaryota.
DR GeneTree; ENSGT00930000152474; -.
DR InParanoid; Q9VDH6; -.
DR OMA; HIDRMFR; -.
DR OrthoDB; 188544at2759; -.
DR Reactome; R-DME-204005; COPII-mediated vesicle transport.
DR Reactome; R-DME-399710; Activation of AMPA receptors.
DR Reactome; R-DME-438066; Unblocking of NMDA receptors, glutamate binding and activation.
DR Reactome; R-DME-451308; Activation of Ca-permeable Kainate Receptor.
DR Reactome; R-DME-5694530; Cargo concentration in the ER.
DR BioGRID-ORCS; 42471; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 42471; -.
DR PRO; PR:Q9VDH6; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0259215; Expressed in embryonic head sensory system (Drosophila) and 7 other tissues.
DR Genevisible; Q9VDH6; DM.
DR GO; GO:0016021; C:integral component of membrane; ISM:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0015276; F:ligand-gated ion channel activity; ISM:FlyBase.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0007610; P:behavior; IEA:UniProtKB-KW.
DR GO; GO:0050907; P:detection of chemical stimulus involved in sensory perception; IEP:FlyBase.
DR InterPro; IPR001320; Iontro_rcpt.
DR Pfam; PF00060; Lig_chan; 1.
PE 1: Evidence at protein level;
KW Behavior; Cell membrane; Glycoprotein; Ion channel; Ion transport;
KW Ligand-gated ion channel; Membrane; Receptor; Reference proteome;
KW Sensory transduction; Signal; Transmembrane; Transmembrane helix;
KW Transport.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..868
FT /note="Ionotropic receptor 93a"
FT /evidence="ECO:0000255"
FT /id="PRO_5004334488"
FT TOPO_DOM 29..565
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 566..586
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 587..642
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 643..663
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 664..832
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 833..853
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 854..868
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 294
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 305
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 432
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 475
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 499
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 543
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 691
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 494
FT /note="T -> A (in Ref. 3; AAN71127)"
FT /evidence="ECO:0000305"
FT CONFLICT 812
FT /note="N -> S (in Ref. 3; AAN71127)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 868 AA; 99639 MW; 28BD2D1BDF1B46EF CRC64;
MNPGEMRPSA CLLLLAGLQL SILVPTEAND FSSFLSANAS LAVVVDHEYM TVHGENILAH
FEKILSDVIR ENLRNGGINV KYFSWNAVRL KKDFLAAITV TDCENTWNFY KNTQETSILL
IAITDSDCPR LPLNRALMVP IVENGDEFPQ LILDAKVQQI LNWKTAVVFV DQTILEENAL
LVKSIVHESI TNHITPISLI LYEINDSLRG QQKRVALRQA LSQFAPKKHE EMRQQFLVIS
AFHEDIIEIA ETLNMFHVGN QWMIFVLDMV ARDFDAGTVT INLDEGANIA FALNETDPNC
QDSLNCTISE ISLALVNAIS KITVEEESIY GEISDEEWEA IRFTKQEKQA EILEYMKEFL
KTNAKCSSCA RWRVETAITW GKSQENRKFR STPQRDAKNR NFEFINIGYW TPVLGFVCQE
LAFPHIEHHF RNITMDILTV HNPPWQILTK NSNGVIVEHK GIVMEIVKEL SRALNFSYYL
HEASAWKEED SLSTSAGGNE SDELVGSMTF RIPYRVVEMV QGNQFFIAAV AATVEDPDQK
PFNYTQPISV QKYSFITRKP DEVSRIYLFT APFTVETWFC LMGIILLTAP TLYAINRLAP
LKEMRIVGLS TVKSCFWYIF GALLQQGGMY LPTADSGRLV VGFWWIVVIV LVTTYCGNLV
AFLTFPKFQP GVDYLNQLED HKDIVQYGLR NGTFFERYVQ STTREDFKHY LERAKIYGSA
QEEDIEAVKR GERINIDWRI NLQLIVQRHF EREKECHFAL GRESFVDEQI AMIVPAQSAY
LHLVNRHIKS MFRMGFIERW HQMNLPSAGK CNGKSAQRQV TNHKVNMDDM QGCFLVLLLG
FTLALLIVCG EFWYRRFRAS RKRRQFTN
