1.A.69 The Heteromeric Odorant Receptor Channel (HORC) Family

In insects, each olfactory sensory neuron expresses between one and three ligand-binding members of the olfactory receptor (OR) gene family, along with the highly conserved and broadly expressed Or83b co-receptor. The functional insect OR consists of a heteromeric complex of unknown stoichiometry but comprising at least one variable odorant-binding subunit and one constant Or83b family subunit. Insect ORs lack homology to G-protein-coupled chemosensory receptors in vertebrates and possess a distinct seven-transmembrane topology with the amino terminus located intracellularly. Sato et al. (2008) and Touhara (2009) showed that heteromeric insect ORs comprise a new class of ligand-activated non-selective cation channels. Heterologous cells expressing silkmoth, fruitfly or mosquito heteromeric OR complexes show extracellular Ca2+ influx and cation-non-selective ion conductance on stimulation with odorant or pheromone. Odour-evoked OR currents are independent of known G-protein-coupled second messenger pathways. The fast response kinetics and OR-subunit-dependent K+ ion selectivity of the insect OR complex support the hypothesis that the complex between OR and Or83b itself confers channel activity. The ligand (odorant)-gated ion channels formed by an insect OR complex seem to be the basis for a unique strategy that insects have acquired to respond to the olfactory environment (Sato et al., 2008). These odorant receptors have been reviewed (Wicher 2015).

Insect odorant receptors are composed of conventional odorant receptors (for example, Or22a), dimerized with a ubiquitously expressed chaperone protein, such as Or83b in Drosophila. Or83b has a structure akin to GPCRs, but has an inverted orientation in the plasma membrane. However, G proteins are expressed in insect olfactory receptor neurons, and olfactory perception is modified by mutations affecting the cAMP transduction pathway. Application of odorants to mammalian cells co-expressing Or22a and Or83b results in non-selective cation currents activated by means of ionotropic and metabolotropic pathways, and a subsequent increase in the intracellular Ca2+ concentration (Wicher et al., 2008). Expression of Or83b alone leads to functional ion channels not directly responding to odorants, but being directly activated by intracellular cAMP or cGMP. Insect odorant receptors thus form ligand-gated channels as well as complexes of odorant-sensing units and cyclic-nucleotide-activated non-selective cation channels. They, thereby, provide rapid and transient as well as sensitive and prolonged odorant signalling (Wicher et al., 2008). Their evolution, development, gene expression and funtion have been discussed by Yan et al. 2020.  Insects rely on gustatory receptors (GRs) to encode different taste modalities, such as sweet and bitter. The structures of two sugar receptors have been determined (Ma et al. 2024).

ORs have been identified from four insect orders (Coleoptera, Lepidoptera, Diptera, and Hymenoptera). Although all ORs share the same G-protein coupled receptor structure with seven transmembrane domains, they present poor sequence homologies within and between species. D. melanogaster is the only insect species where Ors have been extensively studied from expression pattern establishment to functional investigations (Jacquin-Joly and Merlin, 2004). One OR type is selectively expressed in a subtype of olfactory receptor neurons, and one olfactory neuron expresses only one type of OR. In addition, all olfactory neurons expressing one OR type converge to the same glomerulus in the antennal lobe. The olfactory mechanism, thus, appears to be conserved between insects and vertebrates (Jacquin-Joly and Merlin, 2004).  ORs have highly variable cell surface expression levels. The majority of both human and murine ORs depend on chaperone proteins to traffic from the endoplasmic reticulum to the cell surface, but a limited subset of ORs express at high levels independently of chaperones (Tewari and Matsunami 2023).

After the discovery of the complete repertoire of D. melanogaster Olfactory Receptors (ORs), candidate ORs have been identified from at least 12 insect species from four orders (Coleoptera, Lepidoptera, Diptera, and Hymenoptera). Although all ORs share the same G-protein coupled receptor structure with seven TMSs, they share poor sequence identity. One OR type is selectively expressed in a subtype of olfactory receptor neurons, and one olfactory neuron expresses only one type of OR. The olfactory mechanism, further, appears to be conserved between insects and vertebrates. The C-terminal region (TMSs4-7) of OR83b is involved in homodimer and heterodimer formation (with OR22a) which suggests why the C-termini of insect ORs are highly conserved. There may be two possible ion channel pathways, one formed by the TMS4-5 region with the intracellular pore-forming domain and the other formed by TM5-6 with the extracellular pore forming domain. Odorant receptors generally comprise the obligate co-receptor, Orco, and one of a family of highly divergent odorant 'tuning' receptors. The two subunits are thought to come together at some as-yet unknown stoichiometry to form a functional complex that is capable of both ionotropic and metabotropic signalling. Segments and residues involved in this interaction have been identified (Carraher et al. 2015).

Olfactory systems must detect and discriminate among an enormous variety of odorants. To contend with this challenge, diverse species have converged on a common strategy in which odorant identity is encoded through the combinatorial activation of large families of olfactory receptors, thus allowing a finite number of receptors to detect a vast chemical world. Del Mármol et al. 2021 offered structural and mechanistic insight into how an individual olfactory receptor can flexibly recognize diverse odorants. They found that the olfactory receptor MhOR5 from the jumping bristletail, Machilis hrabei, assembles as a homotetrameric odorant-gated ion channel with broad chemical tuning. Using cryo-EM, they elucidated the structure of MhOR5 in multiple gating states, alone and in complex with two of its agonists, the odorant eugenol and the insect repellent DEET. Both ligands are recognized through distributed hydrophobic interactions within the same geometrically simple binding pocket located in the transmembrane region of each subunit, suggesting a structural logic for the promiscuous chemical sensitivity of this receptor. Mutation of individual residues lining the binding pocket predictably altered the sensitivity of MhOR5 to eugenol and DEET and broadly reconfigured the receptor's tuning. Thus, diverse odorants share the same structural determinants for binding (Del Mármol et al. 2021).

The generalized reaction catalyzed by HORC is:

cations (in) cations (out)



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Gong, J., Y. Yuan, A. Ward, L. Kang, B. Zhang, Z. Wu, J. Peng, Z. Feng, J. Liu, and X.Z.S. Xu. (2016). The C. elegans Taste Receptor Homolog LITE-1 Is a Photoreceptor. Cell 167: 1252-1263.e10.

Goya, M.E., A. Romanowski, C.S. Caldart, C.Y. Bénard, and D.A. Golombek. (2016). Circadian rhythms identified in Caenorhabditis elegans by in vivo long-term monitoring of a bioluminescent reporter. Proc. Natl. Acad. Sci. USA 113: E7837-E7845.

Harini, K. and R. Sowdhamini. (2012). Molecular Modelling of Oligomeric States of DmOR83b, an Olfactory Receptor in D. Melanogaster. Bioinform Biol Insights 6: 33-47.

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Lin, J.Y., Z. Yang, C. Yang, J.X. Du, F. Yang, J. Cheng, W. Pan, S.J. Zhang, X. Yan, J. Wang, J. Wang, L. Tie, X. Yu, X. Chen, and J.P. Sun. (2021). An ionic lock and a hydrophobic zipper mediate the coupling between an insect pheromone receptor BmOR3 and downstream effectors. J. Biol. Chem. 297: 101160. [Epub: Ahead of Print]

Liu, J., A. Ward, J. Gao, Y. Dong, N. Nishio, H. Inada, L. Kang, Y. Yu, D. Ma, T. Xu, I. Mori, Z. Xie, and X.Z. Xu. (2010). C. elegans phototransduction requires a G protein-dependent cGMP pathway and a taste receptor homolog. Nat Neurosci 13: 715-722.

Ma, D., M. Hu, X. Yang, Q. Liu, F. Ye, W. Cai, Y. Wang, X. Xu, S. Chang, R. Wang, W. Yang, S. Ye, N. Su, M. Fan, H. Xu, and J. Guo. (2024). Structural basis for sugar perception by gustatory receptors. Science 383: eadj2609.

Mang, D., M. Shu, S. Tanaka, S. Nagata, T. Takada, H. Endo, S. Kikuta, H. Tabunoki, K. Iwabuchi, and R. Sato. (2016). Expression of the fructose receptor BmGr9 and its involvement in the promotion of feeding, suggested by its co-expression with neuropeptide F1 in Bombyx mori. Insect Biochem Mol Biol 75: 58-69. [Epub: Ahead of Print]

McBride, C.S., F. Baier, A.B. Omondi, S.A. Spitzer, J. Lutomiah, R. Sang, R. Ignell, and L.B. Vosshall. (2014). Evolution of mosquito preference for humans linked to an odorant receptor. Nature 515: 222-227.

Miura, N., T. Nakagawa, K. Touhara, and Y. Ishikawa. (2010). Broadly and narrowly tuned odorant receptors are involved in female sex pheromone reception in Ostrinia moths. Insect Biochem Mol Biol 40: 64-73.

Miyamoto, T., J. Slone, X. Song, and H. Amrein. (2012). A fructose receptor functions as a nutrient sensor in the Drosophila brain. Cell 151: 1113-1125.

Morinaga, S., K. Nagata, S. Ihara, T. Yumita, Y. Niimura, K. Sato, and K. Touhara. (2022). Structural model for ligand binding and channel opening of an insect gustatory receptor. J. Biol. Chem. 102573. [Epub: Ahead of Print]

Mukunda, L., S. Lavista-Llanos, B.S. Hansson, and D. Wicher. (2014). Dimerisation of the Drosophila odorant coreceptor Orco. Front Cell Neurosci 8: 261.

Nakagawa, T., M. Pellegrino, K. Sato, L.B. Vosshall, and K. Touhara. (2012). Amino acid residues contributing to function of the heteromeric insect olfactory receptor complex. PLoS One 7: e32372.

Nichols, A.S. and C.W. Luetje. (2010). Transmembrane segment 3 of Drosophila melanogaster odorant receptor subunit 85b contributes to ligand-receptor interactions. J. Biol. Chem. 285: 11854-11862.

Ramdya, P. and R. Benton. (2010). Evolving olfactory systems on the fly. Trends Genet. 26: 307-316.

Sang, J., S. Rimal, and Y. Lee. (2019). is necessary for avoiding saponin in. EMBO Rep 20:.

Sato, K., K. Tanaka, and K. Touhara. (2011). Sugar-regulated cation channel formed by an insect gustatory receptor. Proc. Natl. Acad. Sci. USA 108: 11680-11685.

Sato, K., M. Pellegrino, T. Nakagawa, T. Nakagawa, L.B. Vosshall, and K. Touhara. (2008). Insect olfactory receptors are heteromeric ligand-gated ion channels. Nature. 452: 1002-1006.

Stensmyr, M.C., H.K. Dweck, A. Farhan, I. Ibba, A. Strutz, L. Mukunda, J. Linz, V. Grabe, K. Steck, S. Lavista-Llanos, D. Wicher, S. Sachse, M. Knaden, P.G. Becher, Y. Seki, and B.S. Hansson. (2012). A conserved dedicated olfactory circuit for detecting harmful microbes in Drosophila. Cell 151: 1345-1357.

Tewari, J. and H. Matsunami. (2023). Measuring Cell Surface Expression of Odorant Receptors via Flow Cytometry. Methods Mol Biol 2710: 99-109.

Thorne, N. and H. Amrein. (2008). Atypical expression of Drosophila gustatory receptor genes in sensory and central neurons. J Comp Neurol 506: 548-568.

Thorne, N., C. Chromey, S. Bray, and H. Amrein. (2004). Taste perception and coding in Drosophila. Curr. Biol. 14: 1065-1079.

Tiwari, V. and R. Sowdhamini. (2023). Structure modelling of odorant receptor from and identification of potential repellent molecules. Comput Struct Biotechnol J 21: 2204-2214.

Touhara, K. (2009). Insect olfactory receptor complex functions as a ligand-gated ionotropic channel. Ann. N.Y. Acad. Sci. 1170: 177-180.

Ueno, K., M. Ohta, H. Morita, Y. Mikuni, S. Nakajima, K. Yamamoto, and K. Isono. (2001). Trehalose sensitivity in Drosophila correlates with mutations in and expression of the gustatory receptor gene Gr5a. Curr. Biol. 11: 1451-1455.

Wicher, D. (2015). Olfactory signaling in insects. Prog Mol Biol Transl Sci 130: 37-54.

Wicher, D., R. Schäfer, R. Bauernfeind, M.C. Stensmyr, R. Heller, S.H. Heinemann, and B.S. Hansson. (2008). Drosophila odorant receptors are both ligand-gated and cyclic-nucleotide-activated cation channels. Nature. 452: 1007-1011.

Yan, H., S. Jafari, G. Pask, X. Zhou, D. Reinberg, and C. Desplan. (2020). Evolution, developmental expression and function of odorant receptors in insects. J Exp Biol 223:.


TC#NameOrganismal TypeExample

Heteromeric odorant receptor, OR (Sato et al., 2008). OR22a senses fruit-derived esters. These olfactory receptors may have 3-d structures resembling animal rhodopsins, human citronellic terpenoid receptors, OR1A1 and OA1A2 and the mouse eugenol receptor, OR-EG (Ramdya and Benton, 2010). Molecular modelling of oligomeric states of DmOR83b has been reported (Harini and Sowdhamini, 2012).  Recombinant receptor together with the co-receptor, Orco, has been overproduced, purified and reconstituted in a lipid bilayer (Carraher et al. 2013).  Orco (Or83b) forms a dimer that is fully functional for Ca2+ transport, is regulated by calmodulin and interacts normally with Or22a.  The native Orco is therefore probably a dimer (Mukunda et al. 2014). Fertility decline in female mosquitoes is regulated by the orco olfactory co-receptor (David et al. 2023).


Heterometic odorant receptor (OR) of Drosophila melanogaster:
OR83b (Q9VNB5)
OR46a (P81919)
OR43b (P81918)
OR22a (P81909)
OR22b (P81910)


Odorant receptor, OR2 (Carraher et al., 2012) of 378 aas and 7 TMSs.


OR2 of Anopheles gambiae (Q8WTE6)


Odorant receptor 56a of419 aas and 7 TMSs.  Mediates aversive responses to harmful microbial (bacterial and fungal) products such as geosmin (trans-1,10-dimetnyl-trans-9-decalol). (Stensmyr et al. 2012).


OR56a of Drosophila melanogaster


Ordorant receptor 67b of 421 aas and 8 TMSs  (Identical to Or67b of D. melanogaster)

Animals (Insects)

Or67b of Drosophila simulans


Odorant receptor 10b of 406 aas and 7 TMSs


Or10b of Drosophila melanogaster


TC#NameOrganismal TypeExample

The insect heteromeric CO2 receptor: GR21a (Olfactory receptor 21a; 454 aas with 7 or 8 TMSs) GR63a (Olfactory receptor 63a; 512 aas) are coexpressed in antennal neurons of insects and together comprise the peripheral sensory receptor for CO2 (Ramdya and Benton, 2010). These proteins are members of the 7Tm-7 superfamily of putative 7TMS proteins.

Invertebrate Animals

The gustatory receptor for CO2, GR21a/GRG3a of Drosophila melanogaster
GR21a (Q9VPT1)
GR63a (Q9VZL7)


Uncharacterized protein of 382 aas and 9 TMSs.

UP of Frankliniella occidentalis (western flower thrips)


Gustatory receptor for sugar taste 64e-like protein, GR64e, of 486 aas and 8 TMSs.

GR64e protein of Atta cephalotes (Leafcutter ant)


Uncharacterized protein of 416 aas and 7 TMSs.

UP of Aphis gossypii (cotton aphid)


Uncharacterized protein of 425 aas and 7 TMSs.

UP of Amphibalanus amphitrite


Gustatory receptor-like (Grl or Gr5a) protein of 444 aas and 8 TMSs. Insect odorant receptors and gustatory receptors define a superfamily of seven- or 8-TMS ligand-gated ion channels (referred to here as 7TMICs), with homologs identified across Animalia, except Chordata, as well as in plants and uncellular eukaryotes (DUF3537 proteins). Several Drosophila melanogaster Grls display selective expression in subsets of taste neurons, suggesting that they are previously- unrecognized insect chemoreceptors. Their origin may be in a eukaryotic common ancestor (Benton and Himmel 2023). It is required for a response to the sugar trehalose in taste neurons (Ueno et al. 2001). Gr5a neurons selectively respond to sugars, in contrast to Gr66a cells which respond to bitter compounds. Flies are attracted to sugars and avoid bitter substances, suggesting that Gr5a neuron activity is sufficient to mediate acceptance behavior. Sugar signal transduction occurs through coupling with G-proteins such as Galpha49B and G-salpha60A.

Grl of Drosophila melanogaster


Gustatory receptor GR64a specific for sugars (sucrose, maltose and glucose). The structures of two sugar GRs have been determined (Ma et al. 2024), the Drosophila sweet taste receptors GR43a and GR64a in the apo and sugar-bound states. Both GRs form tetrameric sugar-gated cation channels composed of one central pore domain (PD) and four peripheral ligand-binding domains (LBDs). Whereas GR43a is specifically activated by the monosaccharide fructose that binds to a narrow pocket in LBDs, disaccharides sucrose and maltose selectively activate GR64a by binding to a larger and flatter pocket in LBDs. Sugar binding to LBDs induces local conformational changes, which are subsequently transferred to the PD to cause channel opening (Ma et al. 2024).

GR64a of


TC#NameOrganismal TypeExample

Fructose-regulated Ca2+/cation channel, Gustatory (fructose) receptor-9, Gr9 (Sato et al., 2011),which has 8 TMSs in a 5 + 2 + 1 TMS arrangement. Gr9 is widely expressed in the central nervous system (CNS), as well as oral sensory organs and is involved in the promotion of feeding behaviors (Mang et al. 2016). GRs play roles in sensing tastants, such as sugars and bitter substances. The BmGr9 silkworm GR is a d-fructose-gated ion channel receptor. Morinaga et al. 2022 presented a structural model for a channel pore and a D-fructose binding site in BmGr9. Since the membrane topology and oligomeric state of BmGr9 appears similar to those of an insect odorant receptor co-receptor, Orco, they constructed a structural model of BmGr9 based on the cryo-EM Orco structure. Their site-directed mutagenesis data suggested that transmembrane region 7 forms channel pore and controls channel gating. This model also suggested that a pocket formed by transmembrane helices 2-4 and 6 binds D-fructose. They determined the potent binding mode of D-fructose. They proposed a conformational change that leads to channel opening upon D-fructose binding (Morinaga et al. 2022).  Structures of BmGr9, a fructose-gated cation channel, in agonist-free and fructose-bound states have been determined (Frank et al. 2023).  BmGr9 forms a tetramer similar to distantly related insect Olfactory Receptors (ORs). Upon fructose binding, BmGr9's ion channel gate opens through helix S7b movements. In contrast to ORs, BmGR9's ligand-binding pocket, shaped by a kinked helix S4 and a shorter extracellular S3-S4 loop, is larger and solvent accessible in both agonist-free and fructose-bound states. Also unlike ORs, fructose binding by BmGr9 involves helix S5 and a binding pocket lined with aromatic and polar residues. Structure-based sequence alignments revealed distinct patterns of ligand-binding pocket residue conservation in GR subfamilies associated with distinct ligand classes (Frank et al. 2023).


GR-9 of Bombyx mori (B3GTD7)


Gustatory receptor 43a isoform A.  Functions as a narrowly tuned fructose receptor in taste neurons (Miyamoto et al. 2012), being both necessary and sufficient to sense hemolymph fructose.  The structures of two sugar GRs have been determined (Ma et al. 2024), the Drosophila sweet taste receptors GR43a and GR64a in the apo and sugar-bound states. Both GRs form tetrameric sugar-gated cation channels composed of one central pore domain (PD) and four peripheral ligand-binding domains (LBDs). Whereas GR43a is specifically activated by the monosaccharide fructose that binds to a narrow pocket in LBDs, disaccharides sucrose and maltose selectively activate GR64a by binding to a larger and flatter pocket in LBDs. Sugar binding to LBDs induces local conformational changes, which are subsequently transferred to the PD to cause channel opening (Ma et al. 2024).


GR43a of Drosophila melanogaster (Q9V4K2)


Gustatory receptor 28b isoform D of 470 aas and 8 TMSs. It mediates acceptance or avoidance behavior, depending on its substrates. Its atypical expression suggests additional nongustatory roles in the nervous system and tissues involved in proprioception (warmth receptor), hygroreception, and other sensory modalities. It is also possible that it has chemosensory roles in the detection of internal ligands (Thorne and Amrein 2008). Saponins function in natural self-defense for plants to deter various insects due to their unpleasant taste and toxicity. Sang et al. 2019 provided evidence that saponin from Quillaja saponaria functions as an antifeedant as well as an insecticide to ward off insects in both the larval and the adult stages.


GR28b of Drosophila melanogaster (Q9VM08)


Gustatory receptor 2a isoform B


GR2a of Drosophila melanogaster (Q9W594)


High energy light unresponsive protein 1, Lite1; chemoreceptor GUR-2 of 439 aas and 8 TMSs. It is a photoreceptor for short wavelength (UV) light that mediates UV-light-induced avoidance behavior (Edwards et al. 2008, Liu et al. 2010, Gong et al. 2016). It directly senses and absorbs both UV-A and UV-B light with very high efficiency (Gong et al. 2016). Absorption of UV-B but not UV-A light shows resistance to photobleaching. In contrast to other photoreceptors, it does not use a prosthetic chromophore to capture photons and only depends on its protein conformation. It may play a role in response to white light exposure (De Magalhaes Filho et al. 2018) as well as color detection (Ghosh et al. 2021).

Animals (worm)

GUR-2 of Caenorhabditis elegans


Gustatory receptor, GPRGR53, of 430 aas and 7 TMSs. It mediates acceptance or avoidance behavior, depending on its substrates.

GPRGR53 of Anopheles gambiae (African malaria mosquito)


Putative gustatory receptor 98b of 402 aas and 7 TMSs.

GR98b of Bactrocera latifrons


Gustatory receptor family protein 3, Gur-3, of 447 aas and 8 - 9 TMSs. It is a chemoreceptor involved in light-induced avoidance behavior (Bhatla and Horvitz 2015) and probably acts as a molecular sensor in I2 pharyngeal neurons, required for the inhibition of feeding in response to light and hydrogen peroxide. It may be involved in circadian rhythms, probably by acting as a light sensor (Goya et al. 2016). Although it acts with Lite-1 in color detection, it does not act as a photoreceptor (Ghosh et al. 2021).

Gur-3 of Caenorhabditis elegans


Gustatory receptor Gr66a of 527 aas and 8 TMSs, specific for bitter compounds (Thorne et al. 2004). Gr66a cells respond to bitter compounds such as caffeine, theophylline, threonine or valine. Flies avoid bitter substances, suggesting that Gr66a neuron activity is sufficient to mediate avoidance behavior. This receptor is required for sensing and avoiding N,N-Diethyl-meta-toluamide (DEET), the most widely used insect repellent worldwide, as well as L-canavanine, a plant-derived insecticide. Gr66a neurons are also involved in the sex-specific perception of molecules inducing male avoidance behavior, probably through sensing 7-tricosene (7-T), a male cuticular pheromone and leading to inhibition of male-male courtship.

Gr66a of Drosophila melanogaster (fruit fly)


TC#NameOrganismal TypeExample

The pheromone receptor, Or-1 (Nakagawa et al., 2012)


Or-1 of Bombyx mori (Q5WA61)


Sex pheromone receptor of 416 aas and 7 TMSs (Miura et al. 2010).


pheromone receptor of Ostrinia nubilalis (European corn borer) (Pyralis nubilalis)


Odorant receptor 3, Or3 of 410 aas and 7 TMSs.


Or3 of Epiphyas postvittana (Light brown apple moth)


Odorant (pheromone) receptor, OR-3, BmOR3, Or-3, PR-3, of 439 aas and 7 TMSs in a 2 + 1 + 2 + 2 TMS arrangement. The activation of PRs is coupled to the calcium permeability of their coreceptor (Orco (see TC# 1.A.69.1.1)) or putatively with G proteins (Lin et al. 2021). Using the PR BmOR3 from the silk moth B. mori and its coreceptor BmOrco as a template, Lin et al. 2021 showed that an agonist-induced conformational change of BmOR3 is transmitted to BmOrco through TMS7s of both receptors, resulting in the activation of BmOrco. Key interactions, including an ionic lock and a hydrophobic zipper, are essential for mediating the functional coupling between BmOR3 and BmOrco. BmOR3 also selectively coupled with Gi proteins, which is dispensable for BmOrco coupling. Moreover, trans-7TM BmOR3 recruited arrestin (see TC# 8.A.136) in an agonist-dependent manner, which indicated an important role for BmOR3-BmOrco complex formation in ionotropic functions. Thus, the coupling of G protein and arrestin to a prototype trans-7TMS PR, BmOR3, has been demonstrated (Lin et al. 2021).

OR3 of Bombyx mori (Silk moth)


TC#NameOrganismal TypeExample

Odorant receptor 85b (or85b) of 302 aas and 5 putative TMSs.  Binds the odorant, heptanone, for activation; 2-nananone is a competitive antagonist.  The second half of TMS3 is involved in odorant binding and activation (Nichols and Luetje 2010).


animals (Invertebrates; insects)

Or85b of Drosophila melanogaster


Odorant Receptor 4, OR4 or GPROR4, of 406 aas and 7 or 8 TMSs; if 8, the C-terminal TMS may not be a TMS. This odorant receptor specifically recognizes the human odorant sulcatone (6-methylhept-5-en-2-onesul), a volatile odorant emitted at uniquely high levels in humans, thereby playing a key role in mosquito's preference in biting human compared to other animals (McBride et al. 2014). Aedes aegypti is a vector for viruses that spread diseases like dengue, Zika and Chikungunya. Tiwari and Sowdhamini 2023 have modeled the full-length structure of OR4 and the ORco of A. aegypti.

OR4 of Aedes aegypti (Yellowfever mosquito; Culex aegypti)


TC#NameOrganismal TypeExample

Odorant receptor 22 of 312 aas and 6 TMSs


Or22 of Bombyx mori


Odorant receptor 17 of 401 aas and 8 TMSs


Or17 of Bombyx mori (Silk moth)


TC#NameOrganismal TypeExample

Odorant recpetor 278 if 385 aas and 8 TMSs


Or278 of Tribolium castaneum (Red flour beetle)


Odorant receptor 205 of 406 aas and 9 putative TMSs.


Or205 of Tribolium castaneum (Red flour beetle)