Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Rhodopsin  

UniProtKB / Swiss-Prot ID :  OPSD_BOVIN

Gene Name (Synonyms) : 
RHO  

Species :  Bos taurus (Bovine). 

Subcellular Localization :  Membrane; Multi-pass membrane protein. Note=Synthesized in the inner segment (IS) of rod photoreceptor cells before vectorial transport to the rod outer segment (OS) photosensory cilia (By similarity). 

Protein 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 and release of all-trans retinal (By similarity). 

Transmembrane Topology (topPTM) : OPSD_BOVIN 

Protein Sequence MNGTEGPNFYVPFSNKTGVVRSPFEAPQYYLAEPWQFSMLAAYMFLLIMLGFPINFLTLYVTVQHKKLRT...
Predicted Secondary Structure CCCCCCCCCEECCCCCCCCCCCCCCCCCCCCCCHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCCCC...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
1N-acetylmethionine.----MNGTE
----CCCCC
10.61UniProtKB
Link-
2N-linked (GlcNAc...).---MNGTEG
---CCCCCC
67.12UniProtKB
Link-
15N-linked (GlcNAc...).VPFSNKTGV
ECCCCCCCC
46.41UniProtKB
Link-
296N6-(retinylidene)lysine.AFFAKTSAV
HHHHHHHHH
37.54UniProtKB
Link
322S-palmitoyl cysteine.VTTLCCGKN
HHHHHCCCC
2.43UniProtKB
Link-
323S-palmitoyl cysteine.TTLCCGKNP
HHHHCCCCC
11.06UniProtKB
Link-
334PhosphoserineDDEASTTVS
CCCCCCCCC
23.67Phosphositeplus
Link-
334Phosphoserine (PKC_group)DDEASTTVS
CCCCCCCCC
23.67PhosphoELM
Link-
335PhosphothreonineDEASTTVSK
CCCCCCCCC
37.96Phosphositeplus
Link-
335Phosphothreonine (PKC_group)DEASTTVSK
CCCCCCCCC
37.96PhosphoELM
Link-
335Phosphothreonine.DEASTTVSK
CCCCCCCCC
37.96UniProtKB
Link-
336PhosphothreonineEASTTVSKT
CCCCCCCCC
21.93Phosphositeplus
Link-
336Phosphothreonine (PKC_group)EASTTVSKT
CCCCCCCCC
21.93PhosphoELM
Link-
336Phosphothreonine.EASTTVSKT
CCCCCCCCC
21.93UniProtKB
Link-
338PhosphoserineSTTVSKTET
CCCCCCCCC
31.59Phosphositeplus
Link-
338Phosphoserine (PKC_group)STTVSKTET
CCCCCCCCC
31.59PhosphoELM
Link-
340PhosphothreonineTVSKTETSQ
CCCCCCCCC
36.67Phosphositeplus
Link-
340Phosphothreonine (GRK-1)TVSKTETSQ
CCCCCCCCC
36.67PhosphoELM
Link-
340Phosphothreonine.TVSKTETSQ
CCCCCCCCC
36.67UniProtKB
Link-
342PhosphothreonineSKTETSQVA
CCCCCCCCC
29.68Phosphositeplus
Link-
342Phosphothreonine.SKTETSQVA
CCCCCCCCC
29.68UniProtKB
Link-
343PhosphoserineKTETSQVAP
CCCCCCCCC
19.20Phosphositeplus
Link-
343Phosphoserine (GRK-1)KTETSQVAP
CCCCCCCCC
19.20PhosphoELM
Link-
343Phosphoserine; by RK and GRK7.KTETSQVAP
CCCCCCCCC
19.20UniProtKB
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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Disease Reference
Drug Reference
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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Advances in determination of a high-resolution three-dimensionalstructure of rhodopsin, a model of G-protein-coupled receptors(GPCRs).";
Teller D.C., Okada T., Behnke C.A., Palczewski K., Stenkamp R.E.;
Biochemistry 40:7761-7772(2001).
Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH RETINALCHROMOPHORE AND ZINC ION, PALMITOYLATION AT CYS-322 AND CYS-323, ANDGLYCOSYLATION AT ASN-2 AND ASN-15.
"Rhodopsin and bacteriorhodopsin: structure-function relationships.";
Ovchinnikov Y.A.;
FEBS Lett. 148:179-191(1982).
Cited for: PROTEIN SEQUENCE.
"Rhodopsin carbohydrate. Structure of small oligosaccharides attachedat two sites near the NH2 terminus.";
Fukuda M.N., Papermaster D.S., Hargrave P.A.;
J. Biol. Chem. 254:8201-8207(1979).
Cited for: GLYCOSYLATION AT ASN-2 AND ASN-15.
Palmitoylation
ReferencePubMed
"Palmitylation of a G-protein coupled receptor. Direct analysis bytandem mass spectrometry.";
Papac D.I., Thornburg K.R., Buellesbach E.E., Crouch R.K., Knapp D.R.;
J. Biol. Chem. 267:16889-16894(1992).
Cited for: PALMITOYLATION AT CYS-322 AND CYS-323.
"Advances in determination of a high-resolution three-dimensionalstructure of rhodopsin, a model of G-protein-coupled receptors(GPCRs).";
Teller D.C., Okada T., Behnke C.A., Palczewski K., Stenkamp R.E.;
Biochemistry 40:7761-7772(2001).
Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH RETINALCHROMOPHORE AND ZINC ION, PALMITOYLATION AT CYS-322 AND CYS-323, ANDGLYCOSYLATION AT ASN-2 AND ASN-15.
"Two adjacent cysteine residues in the C-terminal cytoplasmic fragmentof bovine rhodopsin are palmitylated.";
Ovchinnikov Y.A., Abdulaev N.G., Bogachuk A.S.;
FEBS Lett. 230:1-5(1988).
Cited for: PALMITOYLATION AT CYS-322 AND CYS-323.
Phosphorylation
ReferencePubMed
"Mechanistic studies on rhodopsin kinase. Light-dependentphosphorylation of C-terminal peptides of rhodopsin.";
Brown N.G., Fowles C., Sharma R., Akhtar M.;
Eur. J. Biochem. 208:659-667(1992).
Cited for: PHOSPHORYLATION AT SER-343.
"The arrestin-bound conformation and dynamics of the phosphorylatedcarboxy-terminal region of rhodopsin.";
Kisselev O.G., McDowell J.H., Hargrave P.A.;
FEBS Lett. 564:307-311(2004).
Cited for: STRUCTURE BY NMR OF 330-348 IN COMPLEX WITH THE INHIBITOR VISUALARRESTIN, AND PHOSPHORYLATION AT SER-334; THR-335; THR-336; SER-338;THR-340; THR-342 AND SER-343.
"Conformational changes in the phosphorylated C-terminal domain ofrhodopsin during rhodopsin arrestin interactions.";
Kisselev O.G., Downs M.A., McDowell J.H., Hargrave P.A.;
J. Biol. Chem. 279:51203-51207(2004).
Cited for: STRUCTURE BY NMR OF 330-348 IN COMPLEX WITH THE INHIBITOR VISUALARRESTIN, AND PHOSPHORYLATION AT SER-334; THR-335; THR-336; SER-338;THR-340; THR-342 AND SER-343.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures