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Primary Information | |
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| BoMiProt ID | Bomi8772 |
| Protein Name | Rhodopsin |
| Organism | Bos taurus |
| Uniprot ID | P02699 |
| Milk Fraction | whey |
| Ref Sequence ID | NP_001014890.1 |
| Aminoacid Length | 348 |
| Molecular Weight | 39008 |
| FASTA Sequence | Download |
| Gene Name | RHO |
| Gene ID | 509933 |
| Protein Existence Status | Reviewed |
Secondary Information | |
| Presence in other biological fluids/tissue/cells | Rod cells of retina |
| Protein Function | photoreceptive pigment for twilight vision |
| Biochemical Properties | catalytic centre has 11-cis retinal as the chromophore, which binds covalently with a lysine residue through a protonated Schiff base linkage.Upon light absorption, the covalently bound 11-cis-retinal is converted to all-trans-retinal. In bovine retinal-binding lysine residue was located at position 296 from the N-terminal of rhodopsin (or residue 53 from the C-terminal). |
| PTMs | phosphorylation on Ser and Thr |
| Site(s) of PTM(s) N-glycosylation, O-glycosylation, Phosphorylation | >sp|P02699|OPSD_BOVIN Rhodopsin OS=Bos taurus OX=9913 GN=RHO PE=1 SV=1 MN*2GTEGPNFYVPFSN*15KTGVVRSPFEAPQYYLAEPWQFSMLAAYMFLLIMLGFPINFLTLY VTVQHKKLRTPLNYILLNLAVADLFMVFGGFTTTLYTSLHGYFVFGPTGCNLEGFFATLG GEIALWSLVVLAIERYVVVCKPMSNFRFGENHAIMGVAFTWVMALACAAPPLVGWSRYIP EGMQCSCGIDYYTPHEETNNESFVIYMFVVHFIIPLIVIFFCYGQLVFTVKEAAAQQQES ATTQKAEKEVTRMVIIMVIAFLICWLPYAGVAFYIFTHQGSDFGPIFMTIPAFFAKTSAV YNPVIYIMMNKQFRNCMVTTLCCGKNPLGDDEAS*334T*335T*336VS*338KT*340ET*342S*343QVAPA |
| SCOP | Class : All alpha proteins Fold : G protein-coupled receptors, GPCRs-like Superfamily : G protein-coupled receptor-like Family : Class A (rhodopsin) G protein-coupled receptor-like Domain Name : 1U19 A:1-348 |
| CATH | Matched CATH superfamily 1.20.1070.10 4.10.840.10 |
| Predicted Disorder Regions | (1-12), (239-245), (330-348) |
| DisProt Annotation | Disorder content 11.2% Term disorder: Fragment 334 - 348 Term disorder: Fragment 327 - 348 Term disorder: Fragment 226 - 242 |
| TM Helix Prediction | 7TMHs ; (39-61), (74-96),(115-133), (153-175), (202-224), (254-276), (285-307) |
| Significance of PTMs | Phosphorylated on some or all of the serine 343 and threonine residues present in the C-terminal region.Only the 11-residue peptide (VII, residues 338-348) contained significant threonine phosphorylation, which was about 25% that on serine residues. the absence of the two-terminal residues Pro347 and Ala348 impaired peptide phosphorylation. |
| PDB ID | 1BOJ,1BOK,1EDS,1EDV,1EDW,1EDX,1F88,1FDF,1GZM,1HZX,1JFP,1L9H,1LN6,1N3M,1NZS,1OV0,1OV1,1U19,1VQX,2G87,2HPY,2I35,2I36,2I37,2IQK,2J4Y,2PED, 2X72,3C9L,3C9M,3CAP,3DQB,3OAX,3PQR,3PXO,4A4M,4BEY,4BEZ,4J4Q,4PXF,4X1H,5DYS,5EN0,5TE3,5TE5,5WKT,6FK6,6FK7,6FK8,6FK9,6FKA,6FKB,6FKC,6FKD,6FUF,6NWE,6OFJ,6OY9,6OYA,6PEL,6PGS,6PH7,6QNO, |
| Bibliography | 1.Kandori H, Shichida Y, Yoshizawa T. Photoisomerization in rhodopsin. Biochemistry (Mosc). 2001 Nov;66(11):1197-209. doi: 10.1023/a:1013123016803. PMID: 11743865. 2.Mullen E, Akhtar M. Structural studies on membrane-bound bovine rhodopsin. Biochem J. 1983 Apr 1;211(1):45-54. doi: 10.1042/bj2110045. PMID: 6870827; PMCID: PMC1154327. 3.Brown NG, Fowles C, Sharma R, Akhtar M. Mechanistic studies on rhodopsin kinase. Light-dependent phosphorylation of C-terminal peptides of rhodopsin. Eur J Biochem. 1992 Sep 15;208(3):659-67. doi: 10.1111/j.1432-1033.1992.tb17232.x. Erratum in: Eur J Biochem. 1993 Mar 15;212(3):840. PMID: 1396673. |