Search by BoMiProt ID - Bomi8772

Primary Information

BoMiProt ID Bomi8772
Protein Name Rhodopsin
Organism Bos taurus
Uniprot IDP02699
Milk Fractionwhey
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,
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
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.