IR75A_DROME
ID IR75A_DROME Reviewed; 629 AA.
AC Q9VVL1; E7E521;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Ionotropic receptor 75a {ECO:0000312|FlyBase:FBgn0036757};
GN Name=Ir75a {ECO:0000312|FlyBase:FBgn0036757};
GN ORFNames=CG14585 {ECO:0000312|FlyBase:FBgn0036757};
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|EMBL:ADQ74919.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
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|EMBL:APD16193.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF THR-289; GLN-536 AND
RP PHE-538.
RX PubMed=27776356; DOI=10.1038/nature19824;
RA Prieto-Godino L.L., Rytz R., Bargeton B., Abuin L., Arguello J.R.,
RA Peraro M.D., Benton R.;
RT "Olfactory receptor pseudo-pseudogenes.";
RL Nature 539:93-97(2016).
RN [3] {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 [4] {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).
CC -!- FUNCTION: Odorant receptor for acetic and propionic acid. Functions as
CC part of an olfactory receptor complex including the ionotropic receptor
CC coreceptor Ir8a. {ECO:0000269|PubMed:21220098,
CC ECO:0000269|PubMed:27776356}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:27776356};
CC Multi-pass membrane protein {ECO:0000255}. Cell projection, dendrite
CC {ECO:0000269|PubMed:27776356}.
CC -!- TISSUE SPECIFICITY: Expressed in acetic-acid-sensing neurons in the
CC antennal coeloconic 2 (ac2) and antennal coeloconic 3 (ac3) sensilla
CC class of sensory hairs (at protein level).
CC {ECO:0000269|PubMed:21220098, ECO:0000269|PubMed:27776356}.
CC -!- DISRUPTION PHENOTYPE: Severely reduced response to acetic and propionic
CC acid. {ECO:0000269|PubMed:27776356}.
CC -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1)
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HQ612239; ADQ74919.1; -; mRNA.
DR EMBL; KX694388; APD16193.1; -; mRNA.
DR EMBL; AE014296; AAF49300.2; -; Genomic_DNA.
DR RefSeq; NP_649012.2; NM_140755.3.
DR AlphaFoldDB; Q9VVL1; -.
DR STRING; 7227.FBpp0271900; -.
DR GlyGen; Q9VVL1; 6 sites.
DR PaxDb; Q9VVL1; -.
DR EnsemblMetazoa; FBtr0273392; FBpp0271900; FBgn0036757.
DR GeneID; 39982; -.
DR KEGG; dme:Dmel_CG14585; -.
DR UCSC; CG14585-RB; d. melanogaster.
DR CTD; 39982; -.
DR FlyBase; FBgn0036757; Ir75a.
DR VEuPathDB; VectorBase:FBgn0036757; -.
DR eggNOG; KOG1052; Eukaryota.
DR GeneTree; ENSGT00940000171120; -.
DR HOGENOM; CLU_015993_3_0_1; -.
DR InParanoid; Q9VVL1; -.
DR OMA; SHEMSCD; -.
DR OrthoDB; 388658at2759; -.
DR PhylomeDB; Q9VVL1; -.
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; 39982; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 39982; -.
DR PRO; PR:Q9VVL1; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0036757; Expressed in antenna and 3 other tissues.
DR Genevisible; Q9VVL1; DM.
DR GO; GO:0044297; C:cell body; IDA:UniProtKB.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; ISM:FlyBase.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:FlyBase.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0017146; C:NMDA selective glutamate receptor complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0071683; C:sensory dendrite; IDA:FlyBase.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0015276; F:ligand-gated ion channel activity; ISM:FlyBase.
DR GO; GO:0004984; F:olfactory receptor activity; IMP:UniProtKB.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
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; IDA:FlyBase.
DR GO; GO:0035235; P:ionotropic glutamate receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central.
DR GO; GO:0007605; P:sensory perception of sound; IMP:FlyBase.
DR InterPro; IPR001320; Iontro_rcpt.
DR Pfam; PF00060; Lig_chan; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell projection; Glycoprotein; Membrane; Olfaction;
KW Receptor; Reference proteome; Sensory transduction; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..629
FT /note="Ionotropic receptor 75a"
FT /evidence="ECO:0000305"
FT /id="PRO_0000444755"
FT TOPO_DOM 1..335
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 336..356
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 357..374
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 375..395
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 396..402
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 403..423
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 424..592
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 593..613
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 614..629
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 289
FT /note="T->S: Results in a loss of odor-evoked response to
FT acetic acid and a gain of response to butyric acid and 2-
FT oxopentanoic acid; when associated with K-536 and L-538."
FT /evidence="ECO:0000269|PubMed:27776356"
FT MUTAGEN 536
FT /note="Q->K: Results in a loss of odor-evoked response to
FT acetic acid and a gain of response to butyric acid and 2-
FT oxopentanoic acid; when associated with T-289 and L-538."
FT /evidence="ECO:0000269|PubMed:27776356"
FT MUTAGEN 538
FT /note="F->L: Results in a loss of odor-evoked response to
FT acetic acid and a gain of response to butyric acid and 2-
FT oxopentanoic acid; when associated with T-289 and K-536."
FT /evidence="ECO:0000269|PubMed:27776356"
FT CONFLICT 60
FT /note="L -> F (in Ref. 1; ADQ74919)"
FT /evidence="ECO:0000305"
FT CONFLICT 68
FT /note="S -> N (in Ref. 1; ADQ74919)"
FT /evidence="ECO:0000305"
FT CONFLICT 88
FT /note="T -> A (in Ref. 1; ADQ74919)"
FT /evidence="ECO:0000305"
FT CONFLICT 152
FT /note="H -> Y (in Ref. 1; ADQ74919)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 629 AA; 72760 MW; 1BF4066D00609E1B CRC64;
MQLVQLANFV LDNLVQSRIG FIVLFHCWQS DESLKFAQQF MKPIHPILVY HQFVQMRGVL
NWSHLELSYM GHTQPTLAIY VDIKCDQTQD LLEEASREQI YNQHYHWLLV GNQSKLEFYD
LFGLFNISID ADVSYVKEQI QDNNDSVAYA VHDVYNNGKI IGGQLNVTGS HEMSCDPFVC
RRTRHLSSLQ KRSKYGNREQ LTDVVLRVAT VVTQRPLTLS DDELIRFLSQ ENDTHIDSLA
RFGFHLTLIL RDLLHCKMKF IFSDSWSKSD VVGGSVGAVV DQTADLTATP SLATEGRLKY
LSAIIETGFF RSVCIFRTPH NAGLRGDVFL QPFSPLVWYL FGGVLSLIGV LLWITFYMEC
KRMQKRWRLD YLPSLLSTFL ISFGAACIQS SSLIPRSAGG RLIYFALFLI SFIMYNYYTS
VVVSSLLSSP VKSKIKTMRQ LAESSLTVGL EPLPFTKSYL NYSRLPEIHL FIKRKIESQT
QNPELWLPAE QGVLRVRDNP GYVYVFETSS GYAYVERYFT AQEICDLNEV LFRPEQLFYT
HLHRNSTYKE LFRLRFLRIL ETGVYRKQRS YWVHMKLHCV AQNFVITVGM EYVAPLLLML
ICADILVVVI LLVELAWKRF FTRHLTFHP
