1.A.69.4.4 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).
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Accession Number: | Q5FBE0 |
Protein Name: | Odorant receptor |
Length: | 439 |
Molecular Weight: | 50808.00 |
Species: | Bombyx mori (Silk moth) [7091] |
Number of TMSs: | 5 |
Location1 / Topology2 / Orientation3: |
Cell membrane1 / Multi-pass membrane protein2 |
Substrate |
ion |
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1: MIFVDDAVIG IKDPREYRHL RVLRTSLRLL GAWPGHYLGE ETGSKYECAP MFLLMFIKIA
61: CLYLTIVYLR NNADVLGFFE LGHVYLTIFM TFVTLSRGFS LTWNPNYHKV VKKFITEMHL
121: LYFKDNSEYA MKTHRRVHKI SHFYTVFLKV QMIAGLTLFN VIPMYNNYRQ GNYASDRPAN
181: ITYDLSIYYE TFDILNTPNG YIFICVFNWF ASYICCSFFC SFDLILSLMI STVSGHFRIL
241: IHNLLTFPLP EAITASKKFV DKHRCNGNRS EFVLEEAKLY SPAEMWQVTD RLRQCIDYHR
301: KLVEFTGDIS EAFGPMLFVY YLFHQVSGCL LLLECSQLNT AALVRYGVLT VVLYQQLIQL
361: SVIVESVGTV TGRLKDAVYE VPWEYMDTSN RKTVAIFLMN VQEPLHVNAL GLAKVGVQSM
421: AAILKTSFSY FTFLRTVSE