GEPHE SUMMARY Print
Gephebase Gene
Entry Status
Published
GepheID
GP00000783
Main curator
Martin
PHENOTYPIC CHANGE
Trait Category
Trait State in Taxon A
Other Vespertilionoidea bats
Trait State in Taxon B
four Vespertilionoidea bats
Ancestral State
Data not curated
Taxonomic Status
Taxon A
Common Name
common bats
Synonyms
common bats; vespertilionid bats
Rank
family
Lineage
Show more ... ta; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi; Sarcopterygii; Dipnotetrapodomorpha; Tetrapoda; Amniota; Mammalia; Theria; Eutheria; Boreoeutheria; Laurasiatheria; Chiroptera; Microchiroptera
NCBI Taxonomy ID
is Taxon A an Infraspecies?
No
Taxon B
Common Name
-
Synonyms
Flaveria australasica; Flaveria australasica Hook.; Flaveria trinervia (Spreng.) C.Mohr
Rank
species
Lineage
Show more ... hyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; asterids; campanulids; Asterales; Asteraceae; Asteroideae; Heliantheae alliance; Tageteae; Flaveria
NCBI Taxonomy ID
is Taxon B an Infraspecies?
No
GENOTYPIC CHANGE
Generic Gene Name
RHO
Synonyms
RP4; OPN2; CSNBAD1
Sequence Similarities
Belongs to the G-protein coupled receptor 1 family. Opsin subfamily.
UniProtKB
Homo sapiens
GenebankID or UniProtKB
Presumptive Null
No
Molecular Type
Aberration Type
SNP
SNP Coding Change
Nonsynonymous
Molecular Details of the Mutation
D83N
Experimental Evidence
Taxon A Taxon B Position
Codon - - -
Amino-acid - - -
Authors
Sugawara T; Imai H; Nikaido M; Imamoto Y; Okada N
Abstract
Rhodopsin is a photoreceptive protein present in vertebrate rod photoreceptor cells, which are responsible for scotopic vision. Recent molecular studies have shown that several aquatic vertebrate species have independently acquired rhodopsin containing Asp83Asn, Glu122Gln, and Ala292Ser substitutions, causing a blue shift in the rhodopsin absorption spectra for adaptation to the blue-green photic environment in deep water. Here, we provide new evidence for the evolutionary and functional relevance of the Asp83Asn substitution. Spectroscopic and kinetic analyses of rhodopsins in six cichlid fishes from the East African Great Lakes using charge-coupled device spectrophotometer revealed that the Asp83Asn substitution accelerated the formation of meta-II, a rhodopsin intermediate crucial for activation of the G-protein transducin. Because rapid formation of meta-II likely results in effective transduction of photic signals, it is reasonable to assume that deep-water cichlid species have acquired rhodopsin containing Asn83 to adapt to dim lighting. Remarkably, rhodopsin containing Asn83 has been identified in terrestrial vertebrates such as bats, and these rhodopsin variants also exhibit accelerated meta-II formation. Our results indicated that the Asp83Asn substitution observed in a variety of animal species was acquired independently in many different lineages during vertebrate evolution for adaptation to dimly lit environments.
Additional References
RELATED GEPHE
Related Genes
No matches found.
Related Haplotypes
No matches found.
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