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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P08100: Variant p.Pro23His

Rhodopsin
Gene: RHO
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Variant information Variant position: help 23 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help LP/P [Disclaimer] The variants are classified into three categories: LP/P, LB/B and US.
  • LP/P: likely pathogenic or pathogenic.
  • LB/B: likely benign or benign.
  • US: uncertain significance
Residue change: help From Proline (P) to Histidine (H) at position 23 (P23H, p.Pro23His). Indicates the amino acid change of the variant. The one-letter and three-letter codes for amino acids used in UniProtKB/Swiss-Prot are those adopted by the commission on Biochemical Nomenclature of the IUPAC-IUB.
Physico-chemical properties: help Change from medium size and hydrophobic (P) to medium size and polar (H) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -2 The score within a Blosum matrix for the corresponding wild-type to variant amino acid change. The log-odds score measures the logarithm for the ratio of the likelihood of two amino acids appearing by chance. The Blosum62 substitution matrix is used. This substitution matrix contains scores for all possible exchanges of one amino acid with another:
  • Lowest score: -4 (low probability of substitution).
  • Highest score: 11 (high probability of substitution).
More information can be found on the following page
Variant description: help In RP4; most common variant; impairs protein folding; leads to interaction with EDEM1 followed by degradation by the ERAD system. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 23 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 348 The length of the canonical sequence.
Location on the sequence: help GTEGPNFYVPFSNATGVVRS P FEYPQYYLAEPWQFSMLAAY The residue change on the sequence. Unless the variant is located at the beginning or at the end of the protein sequence, both residues upstream (20) and downstream (20) of the variant will be shown.
Residue conservation: help The multiple alignment of the region surrounding the variant against various orthologous sequences. 
Human                         GTEGPNFYVPFSNATGVVRSPFEYPQYYLAEPWQFSMLAAY

                              GTEGPNFYVPFSNKTGVVRSPFEYPQYYLAEPWQFSMLAAY

Mouse                         GTEGPNFYVPFSNVTGVVRSPFEQPQYYLAEPWQFSMLAAY

Rat                           GTEGPNFYVPFSNITGVVRSPFEQPQYYLAEPWQFSMLAAY

Pig                           GTEGPNFYVPFSNKTGVVRSPFEYPQYYLAEPWQFSMLAAY

Bovine                        GTEGPNFYVPFSNKTGVVRSPFEAPQYYLAEPWQFSMLAAY

Rabbit                        GTEGPDFYIPMSNQTGVVRSPFEYPQYYLAEPWQFSMLAAY

Sheep                         GTEGPNFYVPFSNKTGVVRSPFEAPQYYLAEPWQFSMLAAY

Cat                           GTEGPNFYVPFSNKTGVVRSPFEYPQYYLAEPWQFSMLAAY

Chicken                       GTEGQDFYVPMSNKTGVVRSPFEYPQYYLAEPWKFSALAAY

Xenopus laevis                GTEGPNFYVPMSNKTGVVRSPFDYPQYYLAEPWQYSALAAY

Zebrafish                     GTEGPAFYVPMSNATGVVRSPYEYPQYYLVAPWAYGLLAAY
Sequence annotation in neighborhood: help The regions or sites of interest surrounding the variant. In general the features listed are posttranslational modifications, binding sites, enzyme active sites, local secondary structure or other characteristics reported in the cited references. The "Sequence annotation in neighborhood" lines have a fixed format:
  • Type: the type of sequence feature.
  • Positions: endpoints of the sequence feature.
  • Description: contains additional information about the feature.
TypePositionsDescription
Chain 1 – 348 Rhodopsin
Topological domain 1 – 36 Extracellular
Glycosylation 15 – 15 N-linked (GlcNAc...) asparagine
Turn 23 – 25



Literature citations
A point mutation of the rhodopsin gene in one form of retinitis pigmentosa.
Dryja T.P.; McGee T.L.; Reichei E.; Hahn L.B.; Cowley G.S.; Yandell D.W.; Sandberg M.A.; Berson E.L.;
Nature 343:364-366(1990)
Cited for: VARIANT RP4 HIS-23; Mutations within the rhodopsin gene in patients with autosomal dominant retinitis pigmentosa.
Dryja T.P.; McGee T.L.; Hahn L.B.; Cowley G.S.; Olsson J.E.; Reichel E.; Sandberg M.A.; Berson E.L.;
N. Engl. J. Med. 323:1302-1307(1990)
Cited for: VARIANTS RP4 HIS-23; ARG-58; LEU-347 AND SER-347; FUNCTION; Identification of novel rhodopsin mutations associated with retinitis pigmentosa by GC-clamped denaturing gradient gel electrophoresis.
Sheffield V.C.; Fishman G.A.; Beck J.S.; Kimura A.E.; Stone E.M.;
Am. J. Hum. Genet. 49:699-706(1991)
Cited for: VARIANTS RP4 MET-17; HIS-23; ARG-58; SER-182 AND LEU-267; Pharmacological chaperone-mediated in vivo folding and stabilization of the P23H-opsin mutant associated with autosomal dominant retinitis pigmentosa.
Noorwez S.M.; Kuksa V.; Imanishi Y.; Zhu L.; Filipek S.; Palczewski K.; Kaushal S.;
J. Biol. Chem. 278:14442-14450(2003)
Cited for: CHARACTERIZATION OF VARIANT RP4 HIS-23; FUNCTION; SUBCELLULAR LOCATION; A dual role for EDEM1 in the processing of rod opsin.
Kosmaoglou M.; Kanuga N.; Aguila M.; Garriga P.; Cheetham M.E.;
J. Cell Sci. 122:4465-4472(2009)
Cited for: CHARACTERIZATION OF VARIANT RP4 HIS-23; SUBCELLULAR LOCATION;
Disclaimer: Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. They are not in any way intended to be used as a substitute for professional medical advice, diagnostic, treatment or care.