Reviewed, UniProtKB/Swiss-Prot P02699 (OPSD_BOVIN)

Names and origin

Protein names

Recommended name:
    Rhodopsin

Gene names

Name:

RHO

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	348 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

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.
Subcellular location	Membrane; Multi-pass membrane protein.
Tissue specificity	Rod shaped photoreceptor cells which mediates vision in dim light.
Post-translational modification	Phosphorylated on some or all of the serine and threonine residues present in the C-terminal region.
Sequence similarities	Belongs to the G-protein coupled receptor 1 family. Opsin subfamily.
Biophysicochemical properties	Absorption: Abs(max)=495 nm

Ontologies

Keywords
Biological process	Sensory transduction Vision
Cellular component	Membrane
Domain	Transmembrane
Ligand	Chromophore
Molecular function	G-protein coupled receptor Photoreceptor protein Receptor Retinal protein Transducer
PTM	Acetylation Glycoprotein Lipoprotein Palmitate Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	protein-chromophore linkage Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	G-protein coupled receptor activity Inferred from electronic annotation. Source: UniProtKB-KW photoreceptor activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 348

348

Rhodopsin

PRO_0000197653

Regions

Topological domain

1 – 36

36

Extracellular

Transmembrane

37 – 63

27

1

Topological domain

64 – 73

10

Cytoplasmic

Transmembrane

74 – 96

23

2

Topological domain

97 – 110

14

Extracellular

Transmembrane

111 – 133

23

3

Topological domain

134 – 152

19

Cytoplasmic

Transmembrane

153 – 173

21

4

Topological domain

174 – 202

29

Extracellular

Transmembrane

203 – 224

22

5

Topological domain

225 – 249

25

Cytoplasmic

Transmembrane

250 – 274

25

6

Topological domain

275 – 286

12

Extracellular

Transmembrane

287 – 308

22

7

Topological domain

309 – 348

40

Cytoplasmic

Sites

Binding site

296

1

Retinal chromophore (covalent)

Amino acid modifications

Modified residue

1

1

N-acetylmethionine

Modified residue

334

1

Phosphoserine By similarity

Modified residue

338

1

Phosphoserine By similarity

Modified residue

343

1

Phosphoserine; by RK

Lipidation

322

1

S-palmitoyl cysteine

Lipidation

323

1

S-palmitoyl cysteine

Glycosylation

2

1

N-linked (GlcNAc...)

Glycosylation

15

1

N-linked (GlcNAc...)

Disulfide bond

110 ↔ 187

Experimental info

Sequence conflict

281

1

S → F in AAA30675. Ref.3

Secondary structure

1

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348

Helix Strand Turn

Details...

Beta strand

3 – 5

3

Beta strand

10 – 13

4

Turn

23 – 25

3

Helix

29 – 31

3

Helix

34 – 64

31

Helix

71 – 89

19

Helix

91 – 100

10

Helix

106 – 139

34

Beta strand

143 – 145

3

Helix

150 – 168

19

Helix

170 – 172

3

Beta strand

178 – 181

4

Turn

182 – 185

4

Beta strand

186 – 189

4

Turn

196 – 199

4

Helix

200 – 210

11

Helix

213 – 225

13

Helix

246 – 254

9

Helix

256 – 277

22

Helix

285 – 295

11

Helix

296 – 299

4

Helix

301 – 309

9

Helix

311 – 321

11

Turn

322 – 324

3

Beta strand

338 – 342

5

Sequences

	Sequence		Length	Mass (Da)
	P02699-1 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 33FDA196803E81F3	FASTA	348	39,008
	10 20 30 40 50 60 MNGTEGPNFY VPFSNKTGVV RSPFEAPQYY LAEPWQFSML AAYMFLLIML GFPINFLTLY 70 80 90 100 110 120 VTVQHKKLRT PLNYILLNLA VADLFMVFGG FTTTLYTSLH GYFVFGPTGC NLEGFFATLG 130 140 150 160 170 180 GEIALWSLVV LAIERYVVVC KPMSNFRFGE NHAIMGVAFT WVMALACAAP PLVGWSRYIP 190 200 210 220 230 240 EGMQCSCGID YYTPHEETNN ESFVIYMFVV HFIIPLIVIF FCYGQLVFTV KEAAAQQQES 250 260 270 280 290 300 ATTQKAEKEV TRMVIIMVIA FLICWLPYAG VAFYIFTHQG SDFGPIFMTI PAFFAKTSAV 310 320 330 340 YNPVIYIMMN KQFRNCMVTT LCCGKNPLGD DEASTTVSKT ETSQVAPA

References

[1]	"Rhodopsin and bacteriorhodopsin: structure-function relationships." Ovchinnikov Y.A. FEBS Lett. 148:179-191(1982) [PubMed: 6759163] [Abstract] Cited for: PROTEIN SEQUENCE.
[2]	"Isolation, sequence analysis, and intron-exon arrangement of the gene encoding bovine rhodopsin." Nathans J., Hogness D.S. Cell 34:807-814(1983) [PubMed: 6194890] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Multiple opsin mRNA species in bovine retina." Kuo C.-H., Yamagata K., Moyzis R.K., Bitensky M.W., Miki N. Brain Res. 387:251-260(1986) [PubMed: 2950966] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-348.
[4]	"Isolation and nucleotide sequence of a partial cDNA clone for bovine opsin." Koike S., Nabeshima Y., Ogata K., Fukui T., Ohtsuka E., Ikehara M., Tokunaga F. Biochem. Biophys. Res. Commun. 116:563-567(1983) [PubMed: 6228228] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 205-348.
[5]	"Mass spectrometric analysis of integral membrane proteins: application to complete mapping of bacteriorhodopsins and rhodopsin." Ball L.E., Oatis J.E. Jr., Dharmasiri K., Busman M., Wang J., Cowden L.B., Galijatovic A., Chen N., Crouch R.K., Knapp D.R. Protein Sci. 7:758-764(1998) [PubMed: 9541408] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE, MASS SPECTROMETRY. Tissue: Retina.
[6]	"Rhodopsin carbohydrate. Structure of small oligosaccharides attached at two sites near the NH2 terminus." Fukuda M.N., Papermaster D.S., Hargrave P.A. J. Biol. Chem. 254:8201-8207(1979) [PubMed: 468821] [Abstract] Cited for: GLYCOSYLATION AT ASN-2 AND ASN-15.
[7]	"Structural studies on membrane-bound bovine rhodopsin." Mullen E., Akhtar M. Biochem. J. 211:45-54(1983) [PubMed: 6870827] [Abstract] Cited for: RETINAL-BINDING SITE.
[8]	"Two adjacent cysteine residues in the C-terminal cytoplasmic fragment of bovine rhodopsin are palmitylated." Ovchinnikov Y.A., Abdulaev N.G., Bogachuk A.S. FEBS Lett. 230:1-5(1988) [PubMed: 3350146] [Abstract] Cited for: PALMITOYLATION AT CYS-322 AND CYS-323.
[9]	"Assembly of functional rhodopsin requires a disulfide bond between cysteine residues 110 and 187." Karnik S.S., Khorana H.G. J. Biol. Chem. 265:17520-17524(1990) [PubMed: 2145276] [Abstract] Cited for: DISULFIDE BOND.
[10]	"Mechanistic studies on rhodopsin kinase. Light-dependent phosphorylation of C-terminal peptides of rhodopsin." Brown N.G., Fowles C., Sharma R., Akhtar M. Eur. J. Biochem. 208:659-667(1992) [PubMed: 1396673] [Abstract] Cited for: PHOSPHORYLATION AT SER-343.
[11]	"Palmitylation of a G-protein coupled receptor. Direct analysis by tandem mass spectrometry." Papac D.I., Thornburg K.R., Buellesbach E.E., Crouch R.K., Knapp D.R. J. Biol. Chem. 267:16889-16894(1992) [PubMed: 1512231] [Abstract] Cited for: PALMITOYLATION AT CYS-322 AND CYS-323.
[12]	"Structure and function in rhodopsin: topology of the C-terminal polypeptide chain in relation to the cytoplasmic loops." Cai K., Langen R., Hubbell W.L., Khorana H.G. Proc. Natl. Acad. Sci. U.S.A. 94:14267-14272(1997) [PubMed: 9405601] [Abstract] Cited for: MUTAGENESIS.
[13]	"Crystal structure of rhodopsin: a G protein-coupled receptor." Palczewski K., Kumasaka T., Hori T., Behnke C.A., Motoshima H., Fox B.A., Le Trong I., Teller D.C., Okada T., Stenkamp R.E., Yamamoto M., Miyano M. Science 289:739-745(2000) [PubMed: 10926528] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[14]	"Functional role of internal water molecules in rhodopsin revealed by X-ray crystallography." Okada T., Fujiyoshi Y., Silow M., Navarro J., Landau E.M., Shichida Y. Proc. Natl. Acad. Sci. U.S.A. 99:5982-5987(2002) [PubMed: 11972040] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
[15]	"The retinal conformation and its environment in rhodopsin in light of a new 2.2 A crystal structure." Okada T., Sugihara M., Bondar A.N., Elstner M., Entel P., Buss V. J. Mol. Biol. 342:571-583(2004) [PubMed: 15327956] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[16]	"Structure of bovine rhodopsin in a trigonal crystal form." Li J., Edwards P.C., Burghammer M., Villa C., Schertler G.F. J. Mol. Biol. 343:1409-1438(2004) [PubMed: 15491621] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS).
[17]	"Structure of the third cytoplasmic loop of bovine rhodopsin." Yeagle P.L., Alderfer J.L., Albert A.D. Biochemistry 34:14621-14625(1995) [PubMed: 7578070] [Abstract] Cited for: STRUCTURE BY NMR OF 231-252.
[18]	"Structures of the intradiskal loops and amino terminus of the G-protein receptor, rhodopsin." Yeagle P.L., Salloum A., Chopra A., Bhawsar N., Ali L., Kuzmanovski G., Alderfer J.L., Albert A.D. J. Pept. Res. 55:455-465(2000) [PubMed: 10888202] [Abstract] Cited for: STRUCTURE BY NMR OF 1-40; 93-123; 172-205 AND 268-293.
[19]	"Three dimensional structure of the seventh transmembrane helical domain of the G-protein receptor, rhodopsin." Yeagle P.L., Danis C., Choi G., Alderfer J.L., Albert A.D. Mol. Vis. 6:125-131(2000) [PubMed: 10930473] [Abstract] Cited for: STRUCTURE BY NMR OF 291-315.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

K00506 , K00502, K00503, K00504, K00505 Genomic DNA. Translation: AAA30674.1.
M21606 mRNA. Translation: AAA30675.1.

PIR

OOBO. A90840.

RefSeq

NP_001014890.1.

UniGene

Bt.12753

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BOJ	model	-	A	1-348	[»]
1BOK	model	-	A	1-348	[»]
1EDS	NMR	-	A	93-123	[»]
1EDV	NMR	-	A	172-205	[»]
1EDW	NMR	-	A	268-293	[»]
1EDX	NMR	-	A	1-40	[»]
1F88	X-ray	2.80	A/B	1-348	[»]
1FDF	NMR	-	A	291-315	[»]
1GZM	X-ray	2.65	A/B	1-348	[»]
1HZX	X-ray	2.80	A/B	1-348	[»]
1JFP	NMR	-	A	1-348	[»]
1L9H	X-ray	2.60	A/B	1-348	[»]
1LN6	NMR	-	A	1-348	[»]
1N3M	model	-	A/B/C/D/E/F	1-348	[»]
1NZS	NMR	-	A	330-348	[»]
1OV0	model	-	A	1-348	[»]
1OV1	model	-	A	1-348	[»]
1U19	X-ray	2.20	A/B	1-348	[»]
1VQX	NMR	-	A	330-348	[»]
2G87	X-ray	2.60	A/B	1-348	[»]
2HPY	X-ray	2.80	A/B	1-348	[»]
2I35	X-ray	3.80	A	1-348	[»]
2I36	X-ray	4.10	A/B/C	1-348	[»]
2I37	X-ray	4.15	A/B/C	1-348	[»]
2IQK	model	-	A	1-348	[»]
2J4Y	X-ray	3.40	A/B	1-348	[»]
2PED	X-ray	2.95	A/B	1-348	[»]
3CAP	X-ray	2.90	A/B	1-348<