OR35A_DROME
ID OR35A_DROME Reviewed; 409 AA.
AC Q9V3Q2; Q8IP41;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 3.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Odorant receptor 35a;
GN Name=Or35a; ORFNames=CG17868;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10471707; DOI=10.1093/genetics/153.1.179;
RA Ashburner M., Misra S., Roote J., Lewis S.E., Blazej R.G., Davis T.,
RA Doyle C., Galle R.F., George R.A., Harris N.L., Hartzell G., Harvey D.A.,
RA Hong L., Houston K.A., Hoskins R.A., Johnson G., Martin C., Moshrefi A.R.,
RA Palazzolo M., Reese M.G., Spradling A.C., Tsang G., Wan K.H., Whitelaw K.,
RA Celniker S.E., Rubin G.M.;
RT "An exploration of the sequence of a 2.9-Mb region of the genome of
RT Drosophila melanogaster: the Adh region.";
RL Genetics 153:179-219(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
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]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
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]
RP TISSUE SPECIFICITY.
RX PubMed=10943836; DOI=10.1016/s0092-8674(00)00021-0;
RA Vosshall L.B., Wong A.M., Axel R.;
RT "An olfactory sensory map in the fly brain.";
RL Cell 102:147-159(2000).
RN [5]
RP TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=16162917; DOI=10.1523/jneurosci.2432-05.2005;
RA Yao C.A., Ignell R., Carlson J.R.;
RT "Chemosensory coding by neurons in the coeloconic sensilla of the
RT Drosophila antenna.";
RL J. Neurosci. 25:8359-8367(2005).
RN [6]
RP FUNCTION.
RX PubMed=16615896; DOI=10.1016/j.cell.2006.01.050;
RA Hallem E.A., Carlson J.R.;
RT "Coding of odors by a receptor repertoire.";
RL Cell 125:143-160(2006).
RN [7]
RP INTERACTION WITH ORCO, AND FUNCTION.
RX PubMed=21677030; DOI=10.1093/chemse/bjr053;
RA Nichols A.S., Chen S., Luetje C.W.;
RT "Subunit contributions to insect olfactory receptor function: channel block
RT and odorant recognition.";
RL Chem. Senses 36:781-790(2011).
RN [8]
RP FUNCTION.
RX PubMed=21613503; DOI=10.1523/jneurosci.6254-10.2011;
RA Montague S.A., Mathew D., Carlson J.R.;
RT "Similar odorants elicit different behavioral and physiological responses,
RT some supersustained.";
RL J. Neurosci. 31:7891-7899(2011).
RN [9]
RP FUNCTION.
RX PubMed=21857978; DOI=10.1371/journal.pone.0022996;
RA Hoare D.J., Humble J., Jin D., Gilding N., Petersen R., Cobb M.,
RA McCrohan C.;
RT "Modeling peripheral olfactory coding in Drosophila larvae.";
RL PLoS ONE 6:E22996-E22996(2011).
RN [10]
RP FUNCTION.
RX PubMed=22038943; DOI=10.1093/chemse/bjr097;
RA Richgels P.K., Rollmann S.M.;
RT "Genetic variation in odorant receptors contributes to variation in
RT olfactory behavior in a natural population of Drosophila melanogaster.";
RL Chem. Senses 37:229-240(2012).
CC -!- FUNCTION: Odorant receptor which mediates acceptance or avoidance
CC behavior, depending on its substrates. The odorant receptor repertoire
CC encodes a large collection of odor stimuli that vary widely in
CC identity, intensity, and duration. Forms a complex with Orco to form
CC odorant-sensing units, providing sensitive and prolonged odorant
CC signaling and calcium permeability. Involved in the behavioral
CC responses to esters. Involved in the behavioral responses to butanol,
CC pentanol, hexanol, octanol, propyl acetate, and butyl acetate.
CC {ECO:0000269|PubMed:16162917, ECO:0000269|PubMed:16615896,
CC ECO:0000269|PubMed:21613503, ECO:0000269|PubMed:21677030,
CC ECO:0000269|PubMed:21857978, ECO:0000269|PubMed:22038943}.
CC -!- SUBUNIT: Interacts with Orco. Complexes exist early in the endomembrane
CC system in olfactory sensory neurons (OSNs), coupling these complexes to
CC the conserved ciliary trafficking pathway.
CC {ECO:0000269|PubMed:21677030}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in ac3B olfactory sensory neurons in the
CC antenna. {ECO:0000269|PubMed:10943836, ECO:0000269|PubMed:16162917}.
CC -!- MISCELLANEOUS: The atypical heteromeric and topological design of the
CC odorant receptors appears to be an insect-specific solution for odor
CC recognition, making the OR/Orco complex an attractive target for the
CC development of highly selective insect repellents to disrupt olfactory-
CC mediated host-seeking behaviors of insect disease vectors. Odor-evoked
CC OR currents are independent of known G-protein-coupled second messenger
CC pathways.
CC -!- SIMILARITY: Belongs to the insect chemoreceptor superfamily.
CC Heteromeric odorant receptor channel (TC 1.A.69) family. Or1a
CC subfamily. {ECO:0000305}.
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DR EMBL; AE014134; AAN10901.1; -; Genomic_DNA.
DR RefSeq; NP_723916.1; NM_165117.2.
DR AlphaFoldDB; Q9V3Q2; -.
DR SMR; Q9V3Q2; -.
DR STRING; 7227.FBpp0080339; -.
DR GlyGen; Q9V3Q2; 1 site.
DR PaxDb; Q9V3Q2; -.
DR EnsemblMetazoa; FBtr0080781; FBpp0080339; FBgn0028946.
DR GeneID; 34918; -.
DR KEGG; dme:Dmel_CG17868; -.
DR CTD; 34918; -.
DR FlyBase; FBgn0028946; Or35a.
DR VEuPathDB; VectorBase:FBgn0028946; -.
DR eggNOG; ENOG502T9IC; Eukaryota.
DR GeneTree; ENSGT00560000077544; -.
DR HOGENOM; CLU_687484_0_0_1; -.
DR InParanoid; Q9V3Q2; -.
DR OMA; KDFLYSM; -.
DR OrthoDB; 800455at2759; -.
DR PhylomeDB; Q9V3Q2; -.
DR BioGRID-ORCS; 34918; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 34918; -.
DR PRO; PR:Q9V3Q2; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0028946; Expressed in antenna and 5 other tissues.
DR ExpressionAtlas; Q9V3Q2; differential.
DR Genevisible; Q9V3Q2; DM.
DR GO; GO:0032590; C:dendrite membrane; ISS:FlyBase.
DR GO; GO:0016021; C:integral component of membrane; HDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005549; F:odorant binding; ISS:FlyBase.
DR GO; GO:0004984; F:olfactory receptor activity; HDA:FlyBase.
DR GO; GO:0050911; P:detection of chemical stimulus involved in sensory perception of smell; HDA:FlyBase.
DR GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR InterPro; IPR004117; 7tm6_olfct_rcpt.
DR PANTHER; PTHR21137; PTHR21137; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; Membrane; Olfaction; Receptor;
KW Reference proteome; Sensory transduction; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..409
FT /note="Odorant receptor 35a"
FT /id="PRO_0000174241"
FT TOPO_DOM 1..35
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 36..56
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 57..64
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 65..85
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 86..139
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..160
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 161..177
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 178..198
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 199..273
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..294
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 295..302
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 303..323
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 324..379
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 380..400
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 401..409
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 409 AA; 47388 MW; EB1EB3ACDCF9581E CRC64;
MVRYVPRFAD GQKVKLAWPL AVFRLNHIFW PLDPSTGKWG RYLDKVLAVA MSLVFMQHND
AELRYLRFEA SNRNLDAFLT GMPTYLILVE AQFRSLHILL HFEKLQKFLE IFYANIYIDP
RKEPEMFRKV DGKMIINRLV SAMYGAVISL YLIAPVFSII NQSKDFLYSM IFPFDSDPLY
IFVPLLLTNV WVGIVIDTMM FGETNLLCEL IVHLNGSYML LKRDLQLAIE KILVARDRPH
MAKQLKVLIT KTLRKNVALN QFGQQLEAQY TVRVFIMFAF AAGLLCALSF KAYTNPMANY
IYAIWFGAKT VELLSLGQIG SDLAFTTDSL STMYYLTHWE QILQYSTNPS ENLRLLKLIN
LAIEMNSKPF YVTGLKYFRV SLQAGLKILQ ASFSYFTFLT SMQRRQMSN
