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Rhodopsin; opsin-2 (RHO OPN2)
Function:
- photoreceptor required for image-forming vision at low light intensity
- required for photoreceptor cell viability after birth
- light-induced isomerization of 11-cis to all-trans retinal triggers a conformational change leading to G-protein activation & release of all-trans retinal
- absorption (max)=495 nm
- phosphorylated on some or all of Ser & Thr in the C-terminal region
- phosphorylation lead to deactivation
- linked to transducin
Structure:
- belongs to the G-protein coupled receptor 1 family opsin subfamily
Compartment: membrane
Expression:
- rod shaped photoreceptor cells which mediate vision in dim light
Pathology:
- defects in RHO are the cause of
a) retinitis pigmentosa type 4
b) retinitis pigmentosa autosomal recessive
c) congenital stationary night blindness 1 autosomal dominant
Interactions
molecular events
General
phosphoprotein
G-protein coupled receptor; serpentine receptor
Properties
SIZE: entity length = 348 aa
MW = 39 kD
COMPARTMENT: cellular membrane
MOTIF: exoplasmic domain {1-36}
MOTIF: acetylation site
SITE: 1
EFFECTOR-BOUND: acetyl
N-glycosylation site {N2}
N-glycosylation site {N15}
transmembrane domain {37-61}
cytoplasmic loop {62-73}
transmembrane domain {74-98}
exoplasmic loop {99-113}
MOTIF: cysteine residue {C110}
MODIFICATION: cysteine residue {C187}
transmembrane domain {114-133}
cytoplasmic loop {134-152}
transmembrane domain {153-176}
exoplasmic loop {177-202}
MOTIF: cysteine residue {C187}
MODIFICATION: cysteine residue {C110}
transmembrane domain {203-230}
cytoplasmic loop {231-252}
transmembrane domain {253-276}
exoplasmic loop {277-284}
transmembrane domain {285-309}
MOTIF: binding site
SITE: 296-296
EFFECTOR-BOUND: RETINALDYHYDE
cytoplasmic domain {310-348}
MOTIF: cysteine residue {C322}
MODIFICATION: palmitate
COMPARTMENT: membrane
cysteine residue {C323}
MODIFICATION: palmitate
COMPARTMENT: membrane
Ser phosphorylation site {S334}
Ser phosphorylation site {S338}
Ser phosphorylation site {S343}
Database Correlations
OMIM correlations
MORBIDMAP 180380
UniProt P08100
Pfam PF00001
Kegg hsa:6010
References
- UniProt :accession P08100
- Stryer Biochemistry WH Freeman & Co, New York,
1988 pg 1030
- Schertler GF, Villa C, Henderson R.
Projection structure of rhodopsin.
Nature. 1993 Apr 22;362(6422):770-2.
- RHO; Rhodopsin mutations page
http://mol.ophth.uiowa.edu/MOL_WWW/Rhotab.html
- Mutations of the RHO gene;
Retina International Newsletter
http://www.retina-international.com/sci-news/rhomut.htm
- GeneReviews
https://www.genecards.org/cgi-bin/carddisp.pl?gene=RHO
- Wikipedia; Note: Rhodopsin entry
http://en.wikipedia.org/wiki/Rhodopsin