IR40A_DROME
ID IR40A_DROME Reviewed; 732 AA.
AC Q9V9N1; B3DNK0;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2013, sequence version 4.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Ionotropic receptor 40a {ECO:0000303|PubMed:27161501};
DE Flags: Precursor;
GN Name=Ir40a {ECO:0000303|PubMed:27161501, ECO:0000312|FlyBase:FBgn0259683};
GN ORFNames=CG42352 {ECO:0000312|FlyBase:FBgn0259683};
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:ACD99552.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 460-732.
RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
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 a neural sensory system in the antenna that
CC provides the neural basis for the response to environmental changes in
CC humidity (hygrosensation) (PubMed:27161501, PubMed:27656904). Together
CC with Ir25a and Ir93a, mediates the response of the hygrosensory
CC sacculus neurons to changes in relative humidity and is required for
CC dry detection behavior (PubMed:27161501, PubMed:27656904).
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 {ECO:0000269|PubMed:27656904}.
CC -!- DISRUPTION PHENOTYPE: Response of sacculus neurons to changes in
CC humidity is abolished and consequently larvae fail to move towards
CC their preferred humidity. {ECO:0000269|PubMed:27161501,
CC ECO:0000269|PubMed:27656904}.
CC -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1)
CC family. {ECO:0000305}.
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DR EMBL; AE014134; AAF57255.4; -; Genomic_DNA.
DR EMBL; BT032988; ACD99552.1; -; mRNA.
DR RefSeq; NP_610140.4; NM_136296.4.
DR AlphaFoldDB; Q9V9N1; -.
DR STRING; 7227.FBpp0290308; -.
DR GlyGen; Q9V9N1; 4 sites.
DR PaxDb; Q9V9N1; -.
DR PRIDE; Q9V9N1; -.
DR EnsemblMetazoa; FBtr0336971; FBpp0307914; FBgn0259683.
DR GeneID; 35449; -.
DR KEGG; dme:Dmel_CG42352; -.
DR UCSC; CG42352-RC; d. melanogaster.
DR CTD; 35449; -.
DR FlyBase; FBgn0259683; Ir40a.
DR VEuPathDB; VectorBase:FBgn0259683; -.
DR eggNOG; KOG2510; Eukaryota.
DR GeneTree; ENSGT00940000176554; -.
DR HOGENOM; CLU_020832_0_0_1; -.
DR InParanoid; Q9V9N1; -.
DR OMA; QPRQLAI; -.
DR OrthoDB; 722721at2759; -.
DR BioGRID-ORCS; 35449; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 35449; -.
DR PRO; PR:Q9V9N1; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0259683; Expressed in sacculus (Drosophila) and 6 other tissues.
DR ExpressionAtlas; Q9V9N1; baseline and differential.
DR Genevisible; Q9V9N1; DM.
DR GO; GO:0016021; C:integral component of membrane; ISM:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015276; F:ligand-gated ion channel activity; ISM:FlyBase.
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..19
FT /evidence="ECO:0000255"
FT CHAIN 20..732
FT /note="Ionotropic receptor 40a"
FT /evidence="ECO:0000255"
FT /id="PRO_5004334452"
FT TOPO_DOM 20..369
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 370..390
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 391..465
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 466..486
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 487..688
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 689..709
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 710..732
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT CARBOHYD 18
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 235
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 299
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 531
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 732 AA; 84084 MW; D6BD5B95EC34C13B CRC64;
MHKFLALGLL PYLLGLLNST RLTFIGNDES DTAIALTQIV RGLQQSSLAI LALPSLALSD
GVCQKERNVY LDDFLQRLHR SNYKSVVFSQ TELFFQHIEE NLQGANECIS LILDEPNQLL
NSLHDRHLGH RLSLFIFYWG ARWPPSSRVI RFREPLRVVV VTRPRKKAFR IYYNQARPCS
DSQLQLVNWY DGDNLGLQRI PLLPTALSVY ANFKGRTFRV PVFHSPPWFW VTYCNNSFEE
DEEFNSLDSI EKRKVRVTGG RDHRLLMLLS KHMNFRFKYI EAPGRTQGSM RSEDGKDSND
SFTGGIGLLQ SGQADFFLGD VGLSWERRKA IEFSFFTLAD SGAFATHAPR RLNEALAIMR
PFKQDIWPHL ILTIIFSGPI FYGIIALPYI WRRRWANSDV EHLGELYIHM TYLKEITPRL
LKLKPRTVLS AHQMPHQLFQ KCIWFTLRLF LKQSCNELHN GYRAKFLTIV YWIAATYVLA
DVYSAQLTSQ FARPAREPPI NTLQRLQAAM IHDGYRLYVE KESSSLEMLE NGTELFRQLY
ALMRQQVIND PQGFFIDSVE AGIKLIAEGG EDKAVLGGRE TLFFNVQQYG SNNFQLSQKL
YTRYSAVAVQ IGCPFLGSLN NVLMQLFESG ILDKMTAAEY AKQYQEVEAT RIYKGSVQAK
NSEAYSRTES YDSTVISPLN LRMLQGAFIA LGVGSLAAGV ILLLEIVFIK LDQARLWMLC
SRLQWIRYDR KV
