IR25A_DROME
ID IR25A_DROME Reviewed; 947 AA.
AC E9NA96;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Ionotropic receptor 25a {ECO:0000312|EMBL:ADU79032.1};
DE Flags: Precursor;
GN Name=Ir25a {ECO:0000312|FlyBase:FBgn0031634};
GN ORFNames=CG15627 {ECO:0000312|FlyBase:FBgn0031634};
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|EMBL:ADU79032.1};
RN [1] {ECO:0000312|EMBL:ADU79032.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=21220098; DOI=10.1016/j.neuron.2010.11.042;
RA Abuin L., Bargeton B., Ulbrich M.H., Isacoff E.Y., Kellenberger S.,
RA Benton R.;
RT "Functional architecture of olfactory ionotropic glutamate receptors.";
RL Neuron 69:44-60(2011).
RN [2] {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 [3] {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 [4] {ECO:0000305}
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=19135896; DOI=10.1016/j.cell.2008.12.001;
RA Benton R., Vannice K.S., Gomez-Diaz C., Vosshall L.B.;
RT "Variant ionotropic glutamate receptors as chemosensory receptors in
RT Drosophila.";
RL Cell 136:149-162(2009).
RN [5] {ECO:0000305}
RP FUNCTION, INTERACTION WITH NOCTE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DISRUPTION PHENOTYPE, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=26580016; DOI=10.1038/nature16148;
RA Chen C., Buhl E., Xu M., Croset V., Rees J.S., Lilley K.S., Benton R.,
RA Hodge J.J., Stanewsky R.;
RT "Drosophila ionotropic receptor 25a mediates circadian clock resetting by
RT temperature.";
RL Nature 527:516-520(2015).
RN [6] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=27126188; DOI=10.7554/elife.13254;
RA Ni L., Klein M., Svec K.V., Budelli G., Chang E.C., Ferrer A.J., Benton R.,
RA Samuel A.D., Garrity P.A.;
RT "The ionotropic receptors IR21a and IR25a mediate cool sensing in
RT Drosophila.";
RL Elife 5:0-0(2016).
RN [7]
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 [8]
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), humidity (hygrosensation) and
CC odor detection (PubMed:21220098, PubMed:27161501, PubMed:27656904).
CC Required for odor-evoked electrophysiological responses in multiple
CC neuron classes in the antenna and is likely to function as part of an
CC olfactory receptor complex with Ir76a and Ir76b (PubMed:21220098).
CC Together with Ir21a and Ir93a, mediates the response of the larval
CC dorsal organ cool cells, a trio of cool-responsive neurons, to cooling
CC and is required for cool avoidance behavior (PubMed:27126188,
CC PubMed:27161501, PubMed:27656904). Required in chordonotal organ
CC neurons for behavioral synchronization to low-amplitude temperature
CC cycles and mediates circadian clock resetting by temperature
CC (PubMed:26580016). Together with Ir40a and Ir93a, mediates the response
CC of the hydrosensory sacculus neurons to changes in relative humidity,
CC and is required for dry detection and humidiy preference behavior
CC (PubMed:27161501, PubMed:27656904). {ECO:0000269|PubMed:21220098,
CC ECO:0000269|PubMed:26580016, ECO:0000269|PubMed:27126188,
CC ECO:0000269|PubMed:27161501, ECO:0000269|PubMed:27656904}.
CC -!- SUBUNIT: Interacts with nocte. {ECO:0000269|PubMed:26580016}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}. Cell projection, axon
CC {ECO:0000269|PubMed:19135896}. Cell projection, dendrite
CC {ECO:0000269|PubMed:19135896, ECO:0000269|PubMed:26580016,
CC ECO:0000269|PubMed:27126188}. Perikaryon {ECO:0000269|PubMed:19135896,
CC ECO:0000269|PubMed:26580016}. Cell projection, cilium
CC {ECO:0000269|PubMed:19135896}. Note=Low levels detected in the axon
CC segment adjacent to the perikaryon in some sensory neurons of the
CC antenna but not detected along axons as they enter the brain or at
CC synapses within antennal lobe glomeruli. In coeloconic neurons,
CC prominently expressed both in the perikaryon and in the distal tip of
CC the dendrite which corresponds to the ciliated outer dendritic segment
CC innervating the sensory hair. Relatively low levels detected in inner
CC dendrites (PubMed:19135896). Detected in dendritic bulbs of the dorsal
CC organ cool cells (PubMed:27126188). {ECO:0000269|PubMed:19135896,
CC ECO:0000269|PubMed:27126188}.
CC -!- TISSUE SPECIFICITY: In the antenna, detected in neurons of the arista
CC and also detected in sacculus neurons which innervate the first and
CC second chambers (at protein level) (PubMed:21220098, PubMed:19135896,
CC PubMed:27656904). Throughout the main body of the antenna, expressed in
CC neurons which innervate the coeloconic class of olfactory sensilla (at
CC protein level) (PubMed:21220098, PubMed:19135896). Expressed in
CC multiple cells of the dorsal organ including the dorsal organ cool
CC cells (at protein level) (PubMed:27126188, PubMed:27656904). Detected
CC in femur and retina (PubMed:26580016). Expressed in a subset of femur
CC chordonotal neurons and antennal Johnston's Organ neurons
CC (PubMed:26580016). {ECO:0000269|PubMed:19135896,
CC ECO:0000269|PubMed:21220098, ECO:0000269|PubMed:26580016,
CC ECO:0000269|PubMed:27126188, ECO:0000269|PubMed:27656904}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype (PubMed:21220098). Viable
CC and fertile but their response to environmental cues such as
CC temperature, humidity and odorants is impaired (PubMed:21220098,
CC PubMed:26580016, PubMed:27126188, PubMed:27161501, PubMed:27656904).
CC Response of ac4 coeloconic sensilla neurons to agonist phenylethylamine
CC and of ac2 sensilla neurons to agonist 1,4-diaminobutane is abolished
CC (PubMed:21220098). Response of dorsal organ cool cells to changes in
CC temperature is abolished and consequently larvae fail to avoid cool
CC temperatures (PubMed:27126188, PubMed:27161501, PubMed:27656904).
CC Response of sacculus neurons to changes in humidity is also abolished
CC and consequently larvae fail to move towards their preferred humidity
CC (PubMed:27161501, PubMed:27656904). Failure to synchronize in constant
CC light or constant dark to shallow temperature cycles with an amplitude
CC of 2 degrees Celsius (PubMed:26580016). In constant light, mutants
CC display constant activity throughout the temperature cycle in contrast
CC to controls which show a clear activity peak in the second part of the
CC warm period before and after a 6 hour shift of the temperature cycle
CC (PubMed:26580016). In constant dark, mutants do not shift their evening
CC peak during the temperature cycle in contrast to controls which advance
CC or delay their evening activity peak during phase-advanced or phase-
CC delayed temperature cycles (PubMed:26580016). Barely detectable levels
CC of circadian rhythm protein tim in dorsal neurons DN1 and DN2
CC (PubMed:26580016). RNAi-mediated knockdown in chordonotal neurons
CC disrupts synchronization of locomotor activity rhythms with temperature
CC cycles (PubMed:26580016). {ECO:0000269|PubMed:21220098,
CC ECO:0000269|PubMed:26580016, ECO:0000269|PubMed:27126188,
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:0000255}.
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DR EMBL; HQ600588; ADU79032.1; -; mRNA.
DR EMBL; AE014134; AGB92585.1; -; Genomic_DNA.
DR RefSeq; NP_001260049.1; NM_001273120.1.
DR AlphaFoldDB; E9NA96; -.
DR SMR; E9NA96; -.
DR STRING; 7227.FBpp0304756; -.
DR TCDB; 1.A.10.1.14; the glutamate-gated ion channel (gic) family of neurotransmitter receptors.
DR GlyGen; E9NA96; 7 sites.
DR PaxDb; E9NA96; -.
DR DNASU; 33683; -.
DR EnsemblMetazoa; FBtr0332480; FBpp0304756; FBgn0031634.
DR GeneID; 33683; -.
DR KEGG; dme:Dmel_CG15627; -.
DR CTD; 33683; -.
DR FlyBase; FBgn0031634; Ir25a.
DR VEuPathDB; VectorBase:FBgn0031634; -.
DR eggNOG; KOG1052; Eukaryota.
DR GeneTree; ENSGT00940000174434; -.
DR OMA; LMWVFDR; -.
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; 33683; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 33683; -.
DR PRO; PR:E9NA96; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0031634; Expressed in labral sensory complex primordium (Drosophila) and 12 other tissues.
DR ExpressionAtlas; E9NA96; baseline and differential.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0005929; C:cilium; IDA:FlyBase.
DR GO; GO:0016021; C:integral component of membrane; ISM:FlyBase.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0071683; C:sensory dendrite; IDA:FlyBase.
DR GO; GO:0015026; F:coreceptor activity; IMP:FlyBase.
DR GO; GO:0004970; F:ionotropic glutamate receptor activity; IEA:InterPro.
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 GO; GO:0050911; P:detection of chemical stimulus involved in sensory perception of smell; IMP:FlyBase.
DR GO; GO:0009649; P:entrainment of circadian clock; IMP:FlyBase.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR GO; GO:0010378; P:temperature compensation of the circadian clock; IMP:FlyBase.
DR GO; GO:0019226; P:transmission of nerve impulse; IMP:FlyBase.
DR InterPro; IPR019594; Glu/Gly-bd.
DR InterPro; IPR001508; Iono_rcpt_met.
DR InterPro; IPR001320; Iontro_rcpt.
DR InterPro; IPR028082; Peripla_BP_I.
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; SSF53822; 1.
PE 1: Evidence at protein level;
KW Behavior; Biological rhythms; Cell membrane; Cell projection; Glycoprotein;
KW Ion channel; Ion transport; Ligand-gated ion channel; Membrane; Olfaction;
KW Receptor; Reference proteome; Sensory transduction; Signal; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..947
FT /note="Ionotropic receptor 25a"
FT /id="PRO_5007189792"
FT TOPO_DOM 31..562
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 563..583
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 584..641
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 642..662
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 663..858
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 859..879
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 880..947
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 277
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 434
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 687
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 715
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 762
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 947 AA; 108122 MW; E8834A2127F6FE77 CRC64;
MILMNPKTSK ILWLLGFLSL LSSFSLEIAA QTTQNINVLF INEVDNEPAA KAVEVVLTYL
KKNIRYGLSV QLDSIEANKS DAKVLLEAIC NKYATSIEKK QTPHLILDTT KSGIASETVK
SFTQALGLPT ISASYGQQGD LRQWRDLDEA KQKYLLQVMP PADIIPEAIR SIVIHMNITN
AAILYDDSFV MDHKYKSLLQ NIQTRHVITA IAKDGKRERE EQIEKLRNLD INNFFILGTL
QSIRMVLESV KPAYFERNFA WHAITQNEGE ISSQRDNATI MFMKPMAYTQ YRDRLGLLRT
TYNLNEEPQL SSAFYFDLAL RSFLTIKEML QSGAWPKDME YLNCDDFQGG NTPQRNLDLR
DYFTKITEPT SYGTFDLVTQ STQPFNGHSF MKFEMDINVL QIRGGSSVNS KSIGKWISGL
NSELIVKDEE QMKNLTADTV YRIFTVVQAP FIMRDETAPK GYKGYCIDLI NEIAAIVHFD
YTIQEVEDGK FGNMDENGQW NGIVKKLMDK QADIGLGSMS VMAEREIVID FTVPYYDLVG
ITIMMQRPSS PSSLFKFLTV LETNVWLCIL AAYFFTSFLM WIFDRWSPYS YQNNREKYKD
DEEKREFNLK ECLWFCMTSL TPQGGGEAPK NLSGRLVAAT WWLFGFIIIA SYTANLAAFL
TVSRLDTPVE SLDDLAKQYK ILYAPLNGSS AMTYFERMSN IEQMFYEIWK DLSLNDSLTA
VERSKLAVWD YPVSDKYTKM WQAMQEAKLP ATLDEAVARV RNSTAATGFA FLGDATDIRY
LQLTNCDLQV VGEEFSRKPY AIAVQQGSHL KDQFNNAILT LLNKRQLEKL KEKWWKNDEA
LAKCDKPEDQ SDGISIQNIG GVFIVIFVGI GMACITLVFE YWWYRYRKNP RIIDVAEANA
ERSNAADHPG KLVDGVILGH SGEKFEKSKA ALRPRFNQYP ATFKPRF
