928:
desensitization is accelerated by extracellular H and a negative membrane potential. It may be a photoreceptor for dark adapted cells. A transient increase in hydration of transmembrane α-helices with a t(1/2) = 60 μs tallies with the onset of cation permeation. Aspartate 253 accepts the proton released by the Schiff base (t(1/2) = 10 μs), with the latter being reprotonated by aspartic acid 156 (t(1/2) = 2 ms). The internal proton acceptor and donor groups, corresponding to D212 and D115 in bacteriorhodopsin, are clearly different from other microbial rhodopsins, indicating that their spatial positions in the protein were relocated during evolution. E90 deprotonates exclusively in the nonconductive state. The observed proton transfer reactions and the protein conformational changes relate to the gating of the cation channel.
879:. It is a light-driven proton pump. Trigonal and hexagonal crystals revealed that trimers are arranged on a honeycomb lattice. In these crystals, bacterioruberin binds to crevices between the subunits of the trimer. The polyene chain of the second chromophore is inclined from the membrane normal by an angle of about 20 degrees and, on the cytoplasmic side, it is surrounded by helices AB and DE of neighboring subunits. This peculiar binding mode suggests that bacterioruberin plays a structural role for the trimerization of AR2. When compared with the aR2 structure in another crystal form containing no bacterioruberin, the proton release channel takes a more closed conformation in the P321 or P6(3) crystal; i.e., the native conformation of protein is stabilized in the trimeric protein-bacterioruberin complex.
20:
847:
2982:
392:(GPCR) gene family, which itself arose after the divergence of plants, fungi, choanoflagellates and sponges from the earliest animals. The retinal chromophore is found solely in the opsin branch of this large gene family, meaning its occurrence elsewhere represents convergent evolution, not homology. Microbial rhodopsins are, by sequence, very different from any of the GPCR families.
60:
751:
sensory rhodopsins in any one halophilic archaeon, one (SRI) that responds positively to orange light but negatively to blue light, the other (SRII) that responds only negatively to blue light. Each transducer is specific for its cognate receptor. An x-ray structure of SRII complexed with its transducer (HtrII) at 1.94 Ă… resolution is available (
838:
lipids is highly conserved between archaerhodopsin-2 and bacteriorhodopsin. Since a transmembrane helix facing this space undergoes a large conformational change during the proton pumping cycle, it is feasible that trimerization is an important strategy to capture special lipid components that are relevant to the protein activity.
1147:
Okhrimenko, Ivan S.; Kovalev, Kirill; Petrovskaya, Lada E.; Ilyinsky, Nikolay S.; Alekseev, Alexey A.; Marin, Egor; Rokitskaya, Tatyana I.; Antonenko, Yuri N.; Siletsky, Sergey A.; Popov, Petr A.; Zagryadskaya, Yuliya A.; Soloviov, Dmytro V.; Chizhov, Igor V.; Zabelskii, Dmitrii V.; Ryzhykau, Yury L.
907:
is closely related to the archaeal sensory rhodopsins. It has 712 aas with a signal peptide, followed by a short amphipathic region, and then a hydrophobic N-terminal domain with seven probable TMSs (residues 76-309) followed by a long hydrophilic C-terminal domain of about 400 residues. Part of the
788:
Most of the MR family homologues in yeast and fungi are of about the same size and topology as the archaeal proteins (283-344 amino acyl residues; 7 putative transmembrane α-helical segments), but they are heat shock- and toxic solvent-induced proteins of unknown biochemical function. They have been
387:
to this protein. In a broad non-genetic sense, rhodopsin refers to any molecule, whether related by genetic descent or not (mostly not), consisting of an opsin and a chromophore (generally a variant of retinal). All animal rhodopsins arose (by gene duplication and divergence) late in the history of
927:
is channelrhodopsin-2 (ChR2; Chop2; Cop4; CSOB). This protein is 57% identical, 10% similar to ChR1. It forms a cation-selective ion channel activated by light absorption. It transports both monovalent and divalent cations. It desensitizes to a small conductance in continuous light. Recovery from
919:
gene, or a truncated form of that gene encoding only the hydrophobic core (residues 1-346 or 1–517) in frog oocytes in the presence of all-trans retinal produces a light-gated conductance that shows characteristics of a channel passively but selectively permeable to protons. This channel activity
750:
The association of sensory rhodopsins with their transducer proteins appears to determine whether they function as transporters or receptors. Association of a sensory rhodopsin receptor with its transducer occurs via the transmembrane helical domains of the two interacting proteins. There are two
837:
Most residues participating in the trimerization are not conserved in bacteriorhodopsin, a homologous protein capable of forming a trimeric structure in the absence of bacterioruberin. Despite a large alteration in the amino acid sequence, the shape of the intratrimer hydrophobic space filled by
834:. The changes provide rationales for how relaxation of the distorted retinal causes movements of water and protein atoms that result in vectorial proton transfers to and from the Schiff base. Helix deformation is coupled to vectorial proton transport in the photocycle of bacteriorhodopsin.
942:
Bacteriorhodopsin pumps one Cl ion, from the extracellular medium into the cytosol, per photon absorbed. Although the ions move in the opposite direction, the current generated (as defined by the movement of positive charge) is the same as for bacteriorhodopsin and the archaerhodopsins.
775:, retinal-containing proton pumps isolated from marine bacteria, a green light-activated photoreceptor in cyanobacteria that does not pump ions and interacts with a small (14 kDa) soluble transducer protein and light-gated H channels from the green alga,
1288:
Nordström KJ, Sällman Almén M, Edstam MM, Fredriksson R, Schiöth HB (September 2011). "Independent HHsearch, Needleman--Wunsch-based, and motif analyses reveal the overall hierarchy for most of the G protein-coupled receptor families".
2675:
Schobert B, Brown LS, Lanyi JK (July 2003). "Crystallographic structures of the M and N intermediates of bacteriorhodopsin: assembly of a hydrogen-bonded chain of water molecules between Asp-96 and the retinal Schiff base".
641:
light-driven ion translocation across microbial cytoplasmic membranes or serve as light receptors. Most proteins of the MR family are all of about the same size (250-350 amino acyl residues) and possess seven
829:
Six structural models describe the transformations of the retinal and its interaction with water 402, Asp85, and Asp212 in atomic detail, as well as the displacements of functional residues farther from the
1936:
Zhai Y, Heijne WH, Smith DW, Saier MH (April 2001). "Homologues of archaeal rhodopsins in plants, animals and fungi: structural and functional predications for a putative fungal chaperone protein".
2274:
Gordeliy VI, Labahn J, Moukhametzianov R, Efremov R, Granzin J, Schlesinger R, et al. (October 2002). "Molecular basis of transmembrane signalling by sensory rhodopsin II-transducer complex".
815:
Bacteriorhodopsin pumps one H ion, from the cytosol to the extracellular medium, per photon absorbed. Specific transport mechanisms and pathways have been proposed. The mechanism involves:
2640:
Lanyi JK, Schobert B (April 2003). "Mechanism of proton transport in bacteriorhodopsin from crystallographic structures of the K, L, M1, M2, and M2' intermediates of the photocycle".
2711:
Royant A, Edman K, Ursby T, Pebay-Peyroula E, Landau EM, Neutze R (August 2000). "Helix deformation is coupled to vectorial proton transport in the photocycle of bacteriorhodopsin".
860:
Archaerhodopsins are light-driven H ion transporters. They differ from bacteriorhodopsin in that the claret membrane, in which they are expressed, includes bacterioruberin, a second
789:
suggested to function as pmf-driven chaperones that fold extracellular proteins, but only indirect evidence supports this postulate. The MR family is distantly related to the 7 TMS
670:
Sensory rhodopsins, which normally function as receptors for phototactic behavior, are capable of pumping protons out of the cell if dissociated from their transducer proteins;
951:
A marine bacterial rhodopsin has been reported to function as a proton pump. However, it also resembles sensory rhodopsin II of archaea as well as an Orf from the fungus
219:
2407:
BĂ©jĂ O, Aravind L, Koonin EV, Suzuki MT, Hadd A, Nguyen LP, et al. (September 2000). "Bacterial rhodopsin: evidence for a new type of phototrophy in the sea".
2014:
Luecke H, Schobert B, Richter HT, Cartailler JP, Lanyi JK (October 1999). "Structural changes in bacteriorhodopsin during ion transport at 2 angstrom resolution".
911:
Chop1 serves as a light-gated proton channel and mediates phototaxis and photophobic responses in green algae. Based on this phenotype, Chop1 could be assigned to
270:
and other bacteria. They are integral membrane proteins with seven transmembrane helices, the last of which contains the attachment point (a conserved lysine) for
1694:
Kato HE, Inoue K, Abe-Yoshizumi R, Kato Y, Ono H, Konno M, et al. (May 2015). "Structural basis for Na(+) transport mechanism by a light-driven Na(+) pump".
915:, but because it belongs to a family in which well-characterized homologues catalyze active ion transport, it is assigned to the MR family. Expression of the
2504:
Nagel G, Ollig D, Fuhrmann M, Kateriya S, Musti AM, Bamberg E, Hegemann P (June 2002). "Channelrhodopsin-1: a light-gated proton channel in green algae".
1853:
175:
163:
673:
the Fungal
Chaperones are stress-induced proteins of ill-defined biochemical function, but this subfamily also includes a H-pumping rhodopsin;
785:
NOP-1 protein exhibits a photocycle and conserved H translocation residues that suggest that this putative photoreceptor is a slow H pump.
2171:
Kolbe M, Besir H, Essen LO, Oesterhelt D (May 2000). "Structure of the light-driven chloride pump halorhodopsin at 1.8 A resolution".
2054:"Structures of the archaerhodopsin-3 transporter reveal that disordering of internal water networks underpins receptor sensitization"
107:
757:). Molecular and evolutionary aspects of the light-signal transduction by microbial sensory receptors have been reviewed.
1786:"The rhodopsin-guanylyl cyclase of the aquatic fungus Blastocladiella emersonii enables fast optical control of cGMP signaling"
1536:"A microbial rhodopsin with a unique retinal composition shows both sensory rhodopsin II and bacteriorhodopsin-like properties"
2765:
Yoshimura K, Kouyama T (February 2008). "Structural role of bacterioruberin in the trimeric structure of archaerhodopsin-2".
1394:
1265:
131:
239:
790:
1979:
Sharma AK, Spudich JL, Doolittle WF (November 2006). "Microbial rhodopsins: functional versatility and genetic mobility".
1428:"Functional characterization of flavobacteria rhodopsins reveals a unique class of light-driven chloride pump in bacteria"
3037:
3027:
2802:"Archaerhodopsin variants with enhanced voltage-sensitive fluorescence in mammalian and Caenorhabditis elegans neurons"
274:. Most microbial rhodopsins pump inwards, however "mirror rhodopsins" which function outwards. have been discovered.
822:
deprotonation of the retinal Schiff base and the coupled release of a proton to the extracellular membrane surface,
908:
C-terminal hydrophilic domain is homologous to intersection (EH and SH3 domain protein 1A) of animals (AAD30271).
3022:
2598:"Fungal rhodopsins and opsin-related proteins: eukaryotic homologues of bacteriorhodopsin with unknown functions"
1063:
Oesterhelt D, Tittor J (February 1989). "Two pumps, one principle: light-driven ion transport in halobacteria".
227:
3007:
2916:
LĂłrenz-FonfrĂa VA, Resler T, Krause N, Nack M, Gossing M, Fischer von
Mollard G, et al. (April 2013).
3032:
112:
3017:
3002:
2972:
389:
223:
3012:
777:
144:
2368:"Heme histidine ligands within gp91(phox) modulate proton conduction by the phagocyte NADPH oxidase"
705:
872:
structure that has been observed at the N-terminus of the structures of several archaerhodopsins.
850:
Ground state structure of
Archaerhodopsin-3, showing the covalently bound retinal group: PDB:6S6C.
421:
Below is a list of some of the more well-known microbial rhodopsins and some of their properties.
1485:
Zhang F, Vierock J, Yizhar O, Fenno LE, Tsunoda S, Kianianmomeni A, et al. (December 2011).
704:
A phylogenetic analysis of microbial rhodopsins and a detailed analysis of potential examples of
405:
2857:
Nagel G, Szellas T, Huhn W, Kateriya S, Adeishvili N, Berthold P, et al. (November 2003).
2800:
Flytzanis NC, Bedbrook CN, Chiu H, Engqvist MK, Xiao C, Chan KY, et al. (September 2014).
1326:"Enlightening the life sciences: the history of halobacterial and microbial rhodopsin research"
345:
36:
2109:
Royant A, Nollert P, Edman K, Neutze R, Landau EM, Pebay-Peyroula E, Navarro J (August 2001).
1384:
1207:"MicRhoDE: a curated database for the analysis of microbial rhodopsin diversity and evolution"
2366:
Maturana A, Arnaudeau S, Ryser S, Banfi B, Hossle JP, Schlegel W, et al. (August 2001).
1747:"Regulation of transcription by light in Neurospora crassa: A model for fungal photobiology?"
716:
Among the high resolution structures for members of the MR Family are the archaeal proteins,
1255:
2929:
2918:"Transient protonation changes in channelrhodopsin-2 and their relevance to channel gating"
2870:
2813:
2720:
2513:
2416:
2283:
2230:
2180:
2122:
2065:
2052:
Bada Juarez JF, Judge PJ, Adam S, Axford D, Vinals J, Birch J, et al. (January 2021).
1885:
1703:
1598:
1534:
Sudo Y, Ihara K, Kobayashi S, Suzuki D, Irieda H, Kikukawa T, et al. (February 2011).
1439:
1027:
765:
Homologues include putative fungal chaperone proteins, a retinal-containing rhodopsin from
725:
643:
571:
259:
206:
1784:
Scheib U, Stehfest K, Gee CE, Körschen HG, Fudim R, Oertner TG, Hegemann P (August 2015).
8:
1835:
383:. This is still the meaning of rhodopsin in the narrow sense, any protein evolutionarily
2933:
2874:
2817:
2724:
2517:
2420:
2287:
2234:
2217:
Vogeley L, Sineshchekov OA, Trivedi VD, Sasaki J, Spudich JL, Luecke H (November 2004).
2184:
2126:
2069:
1889:
1707:
1602:
1443:
1182:
1149:
1031:
825:
the switch event that allows reprotonation of the Schiff base from the cytoplasmic side.
2952:
2917:
2834:
2801:
2744:
2537:
2481:
2307:
2251:
2218:
2086:
2053:
1961:
1908:
1873:
1813:
1727:
1632:
1619:
1586:
1562:
1535:
1511:
1486:
1462:
1427:
1231:
1206:
1115:
1040:
1015:
688:
384:
364:
44:
2893:
2858:
2689:
2653:
1949:
1426:
Yoshizawa S, Kumagai Y, Kim H, Ogura Y, Hayashi T, Iwasaki W, et al. (May 2014).
1124:
1099:
2957:
2898:
2839:
2782:
2736:
2693:
2657:
2619:
2578:
2541:
2529:
2473:
2468:
2451:
2432:
2389:
2348:
2299:
2256:
2196:
2150:
2145:
2110:
2091:
2031:
1996:
1953:
1913:
1847:
1805:
1766:
1746:
1719:
1676:
1636:
1624:
1567:
1516:
1467:
1390:
1347:
1342:
1325:
1306:
1261:
1236:
1187:
1169:
1129:
1080:
1076:
1045:
985:
810:
767:
739:
717:
658:
444:
400:
294:
214:
168:
136:
40:
24:
2485:
1817:
1585:
Morizumi T, Ou WL, Van Eps N, Inoue K, Kandori H, Brown LS, Ernst OP (August 2019).
88:
2947:
2937:
2888:
2878:
2829:
2821:
2774:
2748:
2728:
2685:
2649:
2609:
2568:
2521:
2463:
2424:
2379:
2338:
2311:
2291:
2246:
2238:
2188:
2140:
2130:
2081:
2073:
2023:
1988:
1965:
1945:
1903:
1893:
1797:
1758:
1731:
1711:
1666:
1614:
1606:
1557:
1547:
1506:
1498:
1457:
1447:
1337:
1298:
1226:
1218:
1177:
1161:
1119:
1111:
1072:
1035:
900:
895:
798:
667:
pump chloride (and other anions such as bromide, iodide and nitrate) into the cell;
515:
202:
2428:
2192:
794:
409:. Since then, other microbial rhodopsins have been discovered, rendering the term
180:
2343:
2326:
2027:
990:
855:
721:
677:
634:
624:
474:
459:
376:
318:
298:
156:
100:
399:
originally referred to the first microbial rhodopsin discovered, known today as
2986:
2922:
Proceedings of the
National Academy of Sciences of the United States of America
2863:
Proceedings of the
National Academy of Sciences of the United States of America
2115:
Proceedings of the
National Academy of Sciences of the United States of America
2077:
1878:
Proceedings of the
National Academy of Sciences of the United States of America
1610:
1587:"X-ray Crystallographic Structure and Oligomerization of Gloeobacter Rhodopsin"
1502:
1432:
Proceedings of the
National Academy of Sciences of the United States of America
1165:
912:
865:
2859:"Channelrhodopsin-2, a directly light-gated cation-selective membrane channel"
2778:
1992:
1874:"Leptosphaeria rhodopsin: bacteriorhodopsin-like proton pump from a eukaryote"
1801:
1762:
1222:
2996:
1770:
1680:
1173:
1098:
Blanck A, Oesterhelt D, Ferrando E, Schegk ES, Lottspeich F (December 1989).
937:
729:
664:
543:
306:
263:
2942:
2883:
2525:
2242:
1898:
1552:
1452:
1302:
963:
The generalized transport reaction for bacterio- and sensory rhodopsins is:
19:
2961:
2902:
2843:
2786:
2740:
2697:
2661:
2623:
2582:
2573:
2557:"Photochemical reaction cycle and proton transfers in Neurospora rhodopsin"
2556:
2533:
2477:
2436:
2393:
2384:
2367:
2352:
2303:
2260:
2200:
2154:
2135:
2095:
2035:
2000:
1957:
1917:
1809:
1723:
1628:
1571:
1520:
1471:
1351:
1310:
1240:
1191:
1049:
883:
819:
photo-isomerization of the retinal and its initial configurational changes,
310:
309:, a light-driven chloride pump; and sensory rhodopsin, which mediates both
290:
286:
278:
267:
28:
1133:
1084:
680:, is a light-driven proton pump that functions as does bacteriorhodopsins;
140:
861:
846:
831:
314:
302:
2295:
1715:
403:. The first bacteriorhodopsin turned out to be of archaeal origin, from
2825:
2555:
Brown LS, Dioumaev AK, Lanyi JK, Spudich EN, Spudich JL (August 2001).
1365:
1287:
1100:"Primary structure of sensory rhodopsin I, a prokaryotic photoreceptor"
869:
651:
647:
586:
372:
124:
753:
317:(in the ultra-violet) responses. Proteins from other bacteria include
2732:
2614:
2597:
638:
380:
360:
333:
282:
2327:"Molecular and evolutionary aspects of microbial sensory rhodopsins"
2273:
1671:
1654:
1146:
955:(AF290180). These proteins exhibit 20-30% identity with each other.
2981:
1785:
1744:
734:
613:
329:
95:
2219:"Anabaena sensory rhodopsin: a photochromic color sensor at 2.0 A"
1659:
1205:
Boeuf D, Audic S, Brillet-Guéguen L, Caron C, Jeanthon C (2015).
341:
325:
271:
119:
32:
2216:
1016:"Molecular ecology of extremely halophilic Archaea and Bacteria"
2013:
882:
694:
the green algal light-gated proton channel, Channelrhodopsin-1;
368:
234:
2915:
2710:
1204:
1097:
2799:
2111:"X-ray structure of sensory rhodopsin II at 2.1-A resolution"
1836:"3.E.1 The ion-translocating microbial rhodopsin (MR) family"
995:
337:
1745:
Olmedo M, Ruger-Herreros C, Luque EM, Corrochano LM (2013).
2365:
1257:
Optogenetics: Light-Sensing Proteins and Their Applications
875:
Archaerhodopsin-2 (AR2) is found in the claret membrane of
797:). Representative members of MR family can be found in the
324:
As their name indicates, microbial rhodopsins are found in
289:, as well as light sensors. For example, the proteins from
196:
151:
83:
59:
2503:
2051:
1693:
2554:
2170:
1783:
654:
on the inside. There are 9 subfamilies in the MR family:
2856:
2108:
1738:
1533:
1425:
2406:
1484:
1421:
1419:
1417:
1415:
1413:
1978:
1871:
1584:
2970:
2452:"Demonstration of a sensory rhodopsin in eubacteria"
1935:
1872:
Waschuk SA, Bezerra AG, Shi L, Brown LS (May 2005).
1410:
2331:
Biochimica et Biophysica Acta (BBA) - Bioenergetics
1056:
903:-1 (ChR1) or channelopsin-1 (Chop1; Cop3; CSOA) of
2674:
2449:
2324:
2166:
2164:
1938:Biochimica et Biophysica Acta (BBA) - Biomembranes
1253:
1487:"The microbial opsin family of optogenetic tools"
1323:
620:ion-translocating microbial rhodopsin (MR) family
2994:
2764:
1478:
1062:
637:of secondary carriers. Members of the MR family
614:The ion-translocating microbial rhodopsin family
2161:
1648:
1646:
2450:Jung KH, Trivedi VD, Spudich JL (March 2003).
2047:
2045:
1840:Transporter Classification Database (tcdb.org)
1247:
629:Transporter Classification Database (tcdb.org)
2639:
2318:
1687:
1527:
1198:
946:
2602:Photochemical & Photobiological Sciences
1852:: CS1 maint: multiple names: authors list (
1643:
1372:. Oxford University Press. 19 December 2012.
1254:Yawo H, Kandori H, Koizumi A (5 June 2015).
2042:
1281:
1777:
1091:
700:Light-activated rhodopsin/guanylyl cyclase
277:This protein family includes light-driven
2951:
2941:
2892:
2882:
2833:
2793:
2613:
2572:
2467:
2383:
2342:
2325:Inoue K, Tsukamoto T, Sudo Y (May 2014).
2250:
2144:
2134:
2085:
1907:
1897:
1670:
1618:
1561:
1551:
1510:
1461:
1451:
1341:
1230:
1181:
1123:
1039:
920:probably generates bioelectric currents.
1842:. Saier Lab Bioinformatics Group (SDSC).
1652:
845:
687:retinal-containing receptor serves as a
367:(light-sensitive molecule) found in the
18:
1376:
1007:
2995:
1324:Grote M, O'Malley MA (November 2011).
738:cyanobacterial sensory rhodopsin (TC#
697:Sensory rhodopsins from cyanobacteria.
2760:
2758:
2635:
2633:
2595:
2499:
2497:
2495:
2212:
2210:
1931:
1929:
1927:
1867:
1865:
1863:
1829:
1827:
1382:
958:
1013:
889:
804:
344:; although they are rare in complex
53:Archaeal/bacterial/fungal rhodopsins
2561:The Journal of Biological Chemistry
2372:The Journal of Biological Chemistry
1540:The Journal of Biological Chemistry
868:. Bacteriorhodopsin also lacks the
799:Transporter Classification Database
530:Krokinobacter eikastus rhodopsin 2
13:
2755:
2630:
2492:
2207:
1924:
1860:
1824:
1116:10.1002/j.1460-2075.1989.tb08579.x
1041:10.1111/j.1574-6941.2002.tb00900.x
841:
14:
3049:
1833:
931:
2980:
2469:10.1046/j.1365-2958.2003.03395.x
1655:"Plant and fungal photopigments"
1343:10.1111/j.1574-6976.2011.00281.x
676:the bacterial rhodopsin, called
58:
2909:
2850:
2704:
2668:
2589:
2548:
2443:
2400:
2359:
2267:
2102:
2007:
1972:
1578:
1291:Molecular Biology and Evolution
351:
1358:
1317:
1140:
1065:Trends in Biochemical Sciences
359:was originally a synonym for "
1:
2690:10.1016/s0022-2836(03)00576-x
2654:10.1016/s0022-2836(03)00263-8
2429:10.1126/science.289.5486.1902
2193:10.1126/science.288.5470.1390
1950:10.1016/s0005-2736(00)00389-8
1001:
771:, a H-pumping rhodopsin from
760:
661:pump protons out of the cell;
262:that provide light-dependent
191:Available protein structures:
2767:Journal of Molecular Biology
2678:Journal of Molecular Biology
2642:Journal of Molecular Biology
2344:10.1016/j.bbabio.2013.05.005
2028:10.1126/science.286.5438.255
1077:10.1016/0968-0004(89)90044-3
711:
646:helical spanners with their
7:
1260:. Springe r. pp. 3–4.
979:
971:That for halorhodopsin is:
886:for neuroscience research.
864:thought to protect against
745:
602:rhodopsin guanylyl cyclase
10:
3054:
3038:Integral membrane proteins
3028:Transmembrane transporters
2078:10.1038/s41467-020-20596-0
1611:10.1038/s41598-019-47445-5
1503:10.1016/j.cell.2011.12.004
1166:10.1038/s42004-023-00884-8
947:Marine Bacterial Rhodopsin
935:
893:
853:
808:
390:G-protein coupled receptor
2779:10.1016/j.jmb.2007.11.039
1993:10.1016/j.tim.2006.09.006
1802:10.1126/scisignal.aab0611
1763:10.1016/j.fbr.2013.02.004
1330:FEMS Microbiology Reviews
1150:"Mirror proteorhodopsins"
1020:FEMS Microbiology Ecology
778:Chlamydomonas reinhardtii
650:on the outside and their
301:, which are light-driven
266:and sensory functions in
233:
213:
195:
190:
186:
174:
162:
150:
130:
118:
106:
94:
82:
74:
69:
57:
52:
1389:. OUP USA. p. 375.
1154:Communications Chemistry
975:Cl (out) + hν → Cl (in).
706:horizontal gene transfer
416:
260:retinal-binding proteins
64:Bacteriorhodopsin trimer
16:Retinal-binding proteins
2943:10.1073/pnas.1219502110
2884:10.1073/pnas.1936192100
2526:10.1126/science.1072068
2243:10.1126/science.1103943
1899:10.1073/pnas.0409659102
1553:10.1074/jbc.M110.190058
1453:10.1073/pnas.1403051111
1383:Mason P (26 May 2011).
1223:10.1093/database/bav080
1014:Oren A (January 2002).
923:A homologue of ChR1 in
599:light-activated enzyme
406:Halobacterium salinarum
379:, and usually found in
346:multicellular organisms
3023:Transmembrane proteins
2596:Brown LS (June 2004).
2574:10.1074/jbc.M102652200
2456:Molecular Microbiology
2385:10.1074/jbc.M010438200
2136:10.1073/pnas.181203898
1981:Trends in Microbiology
1751:Fungal Biology Reviews
967:H (in) + hν → H (out).
953:Leptosphaeria maculans
851:
773:Leptosphaeria maculans
502:Gloeobacter rhodopsin
47:
37:salt evaporation ponds
2806:Nature Communications
2058:Nature Communications
1303:10.1093/molbev/msr061
849:
708:have been published.
691:(Neurospora ospin I);
633:) is a member of the
22:
1386:Medical Neurobiology
726:sensory rhodopsin II
572:sensory rhodopsin II
558:sensory rhodopsin I
256:bacterial rhodopsins
252:Microbial rhodopsins
3008:Biological pigments
2934:2013PNAS..110E1273L
2875:2003PNAS..10013940N
2818:2014NatCo...5.4894F
2725:2000Natur.406..645R
2518:2002Sci...296.2395N
2421:2000Sci...289.1902B
2296:10.1038/nature01109
2288:2002Natur.419..484G
2235:2004Sci...306.1390V
2185:2000Sci...288.1390K
2127:2001PNAS...9810131R
2070:2021NatCo..12..629B
1890:2005PNAS..102.6879W
1716:10.1038/nature14322
1708:2015Natur.521...48K
1653:Heintzen C (2012).
1603:2019NatSR...911283M
1444:2014PNAS..111.6732Y
1032:2002FEMME..39....1O
512:cation channel (+)
411:bacterial rhodopsin
397:bacterial rhodopsin
371:of frogs and other
3033:Transport proteins
2826:10.1038/ncomms5894
1591:Scientific Reports
959:Transport Reaction
852:
659:Bacteriorhodopsins
527:cation pump (Na+)
48:
45:Newark, California
3018:Membrane proteins
3003:Sensory receptors
2567:(35): 32495–505.
1834:Saier, M.H., Jr.
1790:Science Signaling
1396:978-0-19-533997-0
1267:978-4-431-55516-2
986:Bacteriorhodopsin
890:Channelrhodopsins
811:Bacteriorhodopsin
805:Bacteriorhodopsin
768:Neurospora crassa
718:bacteriorhodopsin
685:Neurospora crassa
611:
610:
540:anion pump (Cl-)
499:proton pump (H+)
486:proton pump (H+)
471:proton pump (H+)
456:proton pump (H+)
445:bacteriorhodopsin
441:proton pump (H+)
401:bacteriorhodopsin
313:(in the red) and
295:bacteriorhodopsin
249:
248:
245:
244:
240:structure summary
41:San Francisco Bay
25:bacteriorhodopsin
3045:
3013:Protein families
2985:
2984:
2976:
2966:
2965:
2955:
2945:
2928:(14): E1273-81.
2913:
2907:
2906:
2896:
2886:
2854:
2848:
2847:
2837:
2797:
2791:
2790:
2762:
2753:
2752:
2733:10.1038/35020599
2708:
2702:
2701:
2672:
2666:
2665:
2637:
2628:
2627:
2617:
2615:10.1039/b315527g
2593:
2587:
2586:
2576:
2552:
2546:
2545:
2512:(5577): 2395–8.
2501:
2490:
2489:
2471:
2447:
2441:
2440:
2415:(5486): 1902–6.
2404:
2398:
2397:
2387:
2378:(32): 30277–84.
2363:
2357:
2356:
2346:
2322:
2316:
2315:
2271:
2265:
2264:
2254:
2229:(5700): 1390–3.
2214:
2205:
2204:
2179:(5470): 1390–6.
2168:
2159:
2158:
2148:
2138:
2106:
2100:
2099:
2089:
2049:
2040:
2039:
2022:(5438): 255–61.
2011:
2005:
2004:
1976:
1970:
1969:
1933:
1922:
1921:
1911:
1901:
1869:
1858:
1857:
1851:
1843:
1831:
1822:
1821:
1781:
1775:
1774:
1742:
1736:
1735:
1691:
1685:
1684:
1674:
1650:
1641:
1640:
1622:
1582:
1576:
1575:
1565:
1555:
1531:
1525:
1524:
1514:
1482:
1476:
1475:
1465:
1455:
1423:
1408:
1407:
1405:
1403:
1380:
1374:
1373:
1362:
1356:
1355:
1345:
1321:
1315:
1314:
1285:
1279:
1278:
1276:
1274:
1251:
1245:
1244:
1234:
1202:
1196:
1195:
1185:
1144:
1138:
1137:
1127:
1104:The EMBO Journal
1095:
1089:
1088:
1060:
1054:
1053:
1043:
1011:
913:TC category #1.A
901:Channelrhodopsin
896:Channelrhodopsin
756:
732:, as well as an
632:
516:channelrhodopsin
489:xanthorhodopsin
424:
423:
377:dim-light vision
254:, also known as
188:
187:
62:
50:
49:
3053:
3052:
3048:
3047:
3046:
3044:
3043:
3042:
2993:
2992:
2991:
2979:
2971:
2969:
2914:
2910:
2869:(24): 13940–5.
2855:
2851:
2798:
2794:
2763:
2756:
2719:(6796): 645–8.
2709:
2705:
2673:
2669:
2638:
2631:
2594:
2590:
2553:
2549:
2502:
2493:
2448:
2444:
2405:
2401:
2364:
2360:
2323:
2319:
2282:(6906): 484–7.
2272:
2268:
2215:
2208:
2169:
2162:
2121:(18): 10131–6.
2107:
2103:
2050:
2043:
2012:
2008:
1977:
1973:
1934:
1925:
1884:(19): 6879–83.
1870:
1861:
1845:
1844:
1832:
1825:
1782:
1778:
1743:
1739:
1702:(7550): 48–53.
1692:
1688:
1672:10.1002/wmts.36
1651:
1644:
1583:
1579:
1532:
1528:
1483:
1479:
1424:
1411:
1401:
1399:
1397:
1381:
1377:
1366:"rhodopsin, n."
1364:
1363:
1359:
1322:
1318:
1286:
1282:
1272:
1270:
1268:
1252:
1248:
1203:
1199:
1145:
1141:
1110:(13): 3963–71.
1096:
1092:
1061:
1057:
1012:
1008:
1004:
991:Proteorhodopsin
982:
961:
949:
940:
934:
898:
892:
858:
856:Archaerhodopsin
844:
842:Archaerhodopsin
813:
807:
763:
752:
748:
722:archaerhodopsin
714:
678:Proteorhodopsin
635:TOG Superfamily
623:
616:
475:archaerhodopsin
460:proteorhodopsin
419:
354:
319:proteorhodopsin
311:photoattractant
299:archaerhodopsin
164:OPM superfamily
65:
17:
12:
11:
5:
3051:
3041:
3040:
3035:
3030:
3025:
3020:
3015:
3010:
3005:
2990:
2989:
2968:
2967:
2908:
2849:
2792:
2773:(5): 1267–81.
2754:
2703:
2667:
2629:
2588:
2547:
2491:
2462:(6): 1513–22.
2442:
2399:
2358:
2317:
2266:
2206:
2160:
2101:
2041:
2006:
1971:
1923:
1859:
1823:
1776:
1737:
1686:
1665:(4): 411–432.
1642:
1577:
1546:(8): 5967–76.
1526:
1497:(7): 1446–57.
1477:
1438:(18): 6732–7.
1409:
1395:
1375:
1357:
1336:(6): 1082–99.
1316:
1297:(9): 2471–80.
1280:
1266:
1246:
1197:
1148:(2023-05-02).
1139:
1090:
1055:
1005:
1003:
1000:
999:
998:
993:
988:
981:
978:
977:
976:
969:
968:
960:
957:
948:
945:
936:Main article:
933:
932:Halorhodopsins
930:
925:C. reinhardtii
905:C. reinhardtii
894:Main article:
891:
888:
866:photobleaching
854:Main article:
843:
840:
827:
826:
823:
820:
809:Main article:
806:
803:
762:
759:
747:
744:
742:) and others.
713:
710:
702:
701:
698:
695:
692:
681:
674:
671:
668:
665:Halorhodopsins
662:
615:
612:
609:
608:
606:
603:
600:
596:
595:
593:
590:
584:
580:
579:
577:
574:
569:
565:
564:
562:
559:
556:
552:
551:
549:
546:
541:
537:
536:
534:
531:
528:
524:
523:
521:
518:
513:
509:
508:
506:
503:
500:
496:
495:
493:
490:
487:
483:
482:
480:
477:
472:
468:
467:
465:
462:
457:
453:
452:
450:
447:
442:
438:
437:
434:
431:
428:
418:
415:
353:
350:
332:, and also in
247:
246:
243:
242:
237:
231:
230:
217:
211:
210:
200:
193:
192:
184:
183:
178:
172:
171:
166:
160:
159:
154:
148:
147:
134:
128:
127:
122:
116:
115:
110:
104:
103:
98:
92:
91:
86:
80:
79:
76:
72:
71:
67:
66:
63:
55:
54:
15:
9:
6:
4:
3:
2:
3050:
3039:
3036:
3034:
3031:
3029:
3026:
3024:
3021:
3019:
3016:
3014:
3011:
3009:
3006:
3004:
3001:
3000:
2998:
2988:
2983:
2978:
2977:
2974:
2963:
2959:
2954:
2949:
2944:
2939:
2935:
2931:
2927:
2923:
2919:
2912:
2904:
2900:
2895:
2890:
2885:
2880:
2876:
2872:
2868:
2864:
2860:
2853:
2845:
2841:
2836:
2831:
2827:
2823:
2819:
2815:
2811:
2807:
2803:
2796:
2788:
2784:
2780:
2776:
2772:
2768:
2761:
2759:
2750:
2746:
2742:
2738:
2734:
2730:
2726:
2722:
2718:
2714:
2707:
2699:
2695:
2691:
2687:
2684:(3): 553–70.
2683:
2679:
2671:
2663:
2659:
2655:
2651:
2648:(2): 439–50.
2647:
2643:
2636:
2634:
2625:
2621:
2616:
2611:
2608:(6): 555–65.
2607:
2603:
2599:
2592:
2584:
2580:
2575:
2570:
2566:
2562:
2558:
2551:
2543:
2539:
2535:
2531:
2527:
2523:
2519:
2515:
2511:
2507:
2500:
2498:
2496:
2487:
2483:
2479:
2475:
2470:
2465:
2461:
2457:
2453:
2446:
2438:
2434:
2430:
2426:
2422:
2418:
2414:
2410:
2403:
2395:
2391:
2386:
2381:
2377:
2373:
2369:
2362:
2354:
2350:
2345:
2340:
2337:(5): 562–77.
2336:
2332:
2328:
2321:
2313:
2309:
2305:
2301:
2297:
2293:
2289:
2285:
2281:
2277:
2270:
2262:
2258:
2253:
2248:
2244:
2240:
2236:
2232:
2228:
2224:
2220:
2213:
2211:
2202:
2198:
2194:
2190:
2186:
2182:
2178:
2174:
2167:
2165:
2156:
2152:
2147:
2142:
2137:
2132:
2128:
2124:
2120:
2116:
2112:
2105:
2097:
2093:
2088:
2083:
2079:
2075:
2071:
2067:
2063:
2059:
2055:
2048:
2046:
2037:
2033:
2029:
2025:
2021:
2017:
2010:
2002:
1998:
1994:
1990:
1987:(11): 463–9.
1986:
1982:
1975:
1967:
1963:
1959:
1955:
1951:
1947:
1944:(2): 206–23.
1943:
1939:
1932:
1930:
1928:
1919:
1915:
1910:
1905:
1900:
1895:
1891:
1887:
1883:
1879:
1875:
1868:
1866:
1864:
1855:
1849:
1841:
1837:
1830:
1828:
1819:
1815:
1811:
1807:
1803:
1799:
1795:
1791:
1787:
1780:
1772:
1768:
1764:
1760:
1756:
1752:
1748:
1741:
1733:
1729:
1725:
1721:
1717:
1713:
1709:
1705:
1701:
1697:
1690:
1682:
1678:
1673:
1668:
1664:
1660:
1656:
1649:
1647:
1638:
1634:
1630:
1626:
1621:
1616:
1612:
1608:
1604:
1600:
1596:
1592:
1588:
1581:
1573:
1569:
1564:
1559:
1554:
1549:
1545:
1541:
1537:
1530:
1522:
1518:
1513:
1508:
1504:
1500:
1496:
1492:
1488:
1481:
1473:
1469:
1464:
1459:
1454:
1449:
1445:
1441:
1437:
1433:
1429:
1422:
1420:
1418:
1416:
1414:
1398:
1392:
1388:
1387:
1379:
1371:
1367:
1361:
1353:
1349:
1344:
1339:
1335:
1331:
1327:
1320:
1312:
1308:
1304:
1300:
1296:
1292:
1284:
1269:
1263:
1259:
1258:
1250:
1242:
1238:
1233:
1228:
1224:
1220:
1216:
1212:
1208:
1201:
1193:
1189:
1184:
1179:
1175:
1171:
1167:
1163:
1159:
1155:
1151:
1143:
1135:
1131:
1126:
1121:
1117:
1113:
1109:
1105:
1101:
1094:
1086:
1082:
1078:
1074:
1070:
1066:
1059:
1051:
1047:
1042:
1037:
1033:
1029:
1025:
1021:
1017:
1010:
1006:
997:
994:
992:
989:
987:
984:
983:
974:
973:
972:
966:
965:
964:
956:
954:
944:
939:
938:Halorhodopsin
929:
926:
921:
918:
914:
909:
906:
902:
897:
887:
885:
880:
878:
877:Halorubrum sp
873:
871:
867:
863:
857:
848:
839:
835:
833:
824:
821:
818:
817:
816:
812:
802:
800:
796:
792:
786:
784:
780:
779:
774:
770:
769:
758:
755:
743:
741:
737:
736:
731:
730:halorhodopsin
727:
723:
719:
709:
707:
699:
696:
693:
690:
689:photoreceptor
686:
682:
679:
675:
672:
669:
666:
663:
660:
657:
656:
655:
653:
649:
645:
644:transmembrane
640:
636:
630:
626:
621:
607:
604:
601:
598:
597:
594:
591:
588:
585:
582:
581:
578:
575:
573:
570:
567:
566:
563:
560:
557:
554:
553:
550:
547:
545:
544:halorhodopsin
542:
539:
538:
535:
532:
529:
526:
525:
522:
519:
517:
514:
511:
510:
507:
504:
501:
498:
497:
494:
491:
488:
485:
484:
481:
478:
476:
473:
470:
469:
466:
463:
461:
458:
455:
454:
451:
448:
446:
443:
440:
439:
435:
432:
429:
426:
425:
422:
414:
412:
408:
407:
402:
398:
393:
391:
386:
382:
378:
374:
370:
366:
362:
361:visual purple
358:
349:
347:
343:
339:
335:
331:
327:
322:
320:
316:
312:
308:
307:halorhodopsin
304:
300:
296:
292:
288:
284:
280:
275:
273:
269:
265:
264:ion transport
261:
257:
253:
241:
238:
236:
232:
229:
225:
221:
218:
216:
212:
208:
204:
201:
198:
194:
189:
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583:photosensor
568:photosensor
555:photosensor
420:
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363:", a visual
356:
355:
352:Nomenclature
323:
303:proton pumps
291:halobacteria
287:ion channels
279:proton pumps
276:
255:
251:
250:
29:Halobacteria
862:chromophore
832:Schiff base
625:"TC# 3.E.1"
413:ambiguous.
375:, used for
373:vertebrates
315:photophobic
176:OPM protein
70:Identifiers
2997:Categories
2064:(1): 629.
1370:OED Online
1217:: bav080.
1026:(1): 1–7.
1002:References
870:omega loop
795:TC# 2.A.43
791:LCT family
761:Homologues
587:Neurospora
388:the large
385:homologous
268:halophilic
203:structures
2542:206506942
1771:1749-4613
1681:2190-460X
1637:199389292
1174:2399-3669
1160:(1): 88.
783:N. crassa
740:3.E.1.1.6
712:Structure
652:C-termini
648:N-termini
427:Function
395:The term
381:rod cells
357:Rhodopsin
336:(such as
334:Eukaryota
283:ion pumps
125:PDOC00291
101:IPR001425
2962:23509282
2903:14615590
2844:25222271
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2787:18082767
2741:10949307
2698:12842471
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2624:15170485
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2486:12052542
2478:12622809
2437:10988064
2394:11389135
2353:23732219
2304:12368857
2261:15459346
2201:10827943
2155:11504917
2096:33504778
2036:10514362
2001:17008099
1958:11286964
1918:15860584
1848:cite web
1818:13140205
1810:26268609
1724:25849775
1629:31375689
1572:21135094
1521:22196724
1472:24706784
1352:21623844
1311:21402729
1241:26286928
1211:Database
1192:37130895
1183:10154332
1050:19709178
980:See also
746:Function
735:Anabaena
639:catalyze
589:opsin I
330:Bacteria
293:include
220:RCSB PDB
96:InterPro
2987:Biology
2953:3619329
2930:Bibcode
2871:Bibcode
2835:4166526
2814:Bibcode
2749:4345380
2721:Bibcode
2514:Bibcode
2506:Science
2417:Bibcode
2409:Science
2312:4425659
2284:Bibcode
2252:5017883
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2123:Bibcode
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2066:Bibcode
2016:Science
1966:7931370
1909:1100770
1886:Bibcode
1732:4451644
1704:Bibcode
1620:6677831
1599:Bibcode
1563:3057805
1512:4166436
1463:4020065
1440:Bibcode
1232:4539915
1134:2591367
1085:2468194
1028:Bibcode
369:retinas
365:pigment
342:viruses
326:Archaea
272:retinal
120:PROSITE
113:SM01021
89:PF01036
33:Cargill
23:Purple
2973:Portal
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1962:S2CID
1814:S2CID
1728:S2CID
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479:Arch
436:Ref.
430:Name
417:Table
338:algae
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