Evidence map›Paper›PMID 24403072›Full record

ArticleThe Journal of biological chemistry2014

Evolution of mammalian Opn5 as a specialized UV-absorbing pigment by a single amino acid mutation.

Takahiro Yamashita, Katsuhiko Ono, Hideyo Ohuchi, Akane Yumoto, Hitoshi Gotoh, Sayuri Tomonari, Kazumi Sakai, Hirofumi Fujita, Yasushi Imamoto, Sumihare Noji and 2 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
1.5field-weighted citation impact, top 21% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

54 citing papers in PubMed, 98 citations in OpenAlex.

  1. Article
  2. Prolonged Light Exposure Induces Long-Lasting Retinal Wave Plasticity via Retrograde Melanopsin-Dopamine Signaling.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2026
    Article
  3. Review
  4. The physiological functions of OPN5m.Eye and vision (London, England) · 2025
    Review
  5. Article
  6. Review
  7. A key spectral tuning site of UV-sensitive vertebrate non-visual opsin Opn5.Cellular and molecular life sciences : CMLS · 2025
    Article
  8. Article
  9. Article
  10. Direct Stimulation of Gastric Smooth Muscle Cells via GNeurogastroenterology and motility · 2025
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. IMI 2023 Digest.Investigative ophthalmology & visual science · 2023
    Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

12 authors at 4 institutions in 1 country.

Takahiro YamashitaFrom the Department of Biophysics, Graduate School of Science, Kyoto University, Kyoto 606-8502, Japan.
Katsuhiko Ono
Hideyo Ohuchi
Akane Yumoto
Hitoshi Gotoh
Sayuri Tomonari
Kazumi Sakai
Hirofumi Fujita
Yasushi Imamoto
Sumihare Noji
Katsuki Nakamura
Yoshinori Shichida
Kyoto University · JPKyoto Prefectural University of Medicine · JPOkayama University · JPTokushima University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Opn5 is one of the recently identified opsin groups that is responsible for nonvisual photoreception in animals. We previously showed that a chicken homolog of mammalian Opn5 (Opn5m) is a Gi-coupled UV sensor having molecular properties typical of bistable pigments. Here we demonstrated that mammalian Opn5m evolved to be a more specialized photosensor by losing one of the characteristics of bistable pigments, direct binding of all-trans-retinal. We first confirmed that Opn5m proteins in zebrafish, Xenopus tropicalis, mouse, and human are also UV-sensitive pigments. Then we found that only mammalian Opn5m proteins lack the ability to directly bind all-trans-retinal. Mutational analysis showed that these characteristics were acquired by a single amino acid replacement at position 168. By comparing the expression patterns of Opn5m between mammals and chicken, we found that, like chicken Opn5m, mammalian Opn5m was localized in the ganglion cell layer and inner nuclear layer of the retina. However, the mouse and primate (common marmoset) opsins were distributed not in the posterior hypothalamus (including the region along the third ventricle) where chicken Opn5m is localized, but in the preoptic hypothalamus. Interestingly, RPE65, an essential enzyme for forming 11-cis-retinal in the visual cycle is expressed near the preoptic hypothalamus of the mouse and common marmoset brain but not near the region of the chicken brain where chicken Opn5m is expressed. Therefore, mammalian Opn5m may work exclusively as a short wavelength sensor in the brain as well as in the retina with the assistance of an 11-cis-retinal-supplying system.

Indexed as

Evolution, MolecularMutation, MissenseUltraviolet RaysAmino Acid SubstitutionAnimalsBrainCallithrixChick Embryocis-trans-IsomerasesHumansMembrane ProteinsMiceMice, Inbred ICROpsinsRetinaRetinaldehydecis-trans-IsomerasesMembrane ProteinsOPN5 protein, humanOPN5 protein, mouseOpsinsRetinaldehydeRetinoid IsomerohydrolaseG ProteinsMolecular EvolutionNonvisual PhotoreceptionPhotoreceptorsRhodopsinSignal Transduction

Identifiers

PMID24403072
PMCPMC3924266
OpenAlexW1979013617

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.