P04000 (OPSR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Long-wave-sensitive opsin 1

Alternative name(s):
Red cone photoreceptor pigment
Red-sensitive opsin
Short name=ROP

Gene names

Name:	OPN1LW
Synonyms:	RCP

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	364 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Visual pigments are the light-absorbing molecules that mediate vision. They consist of an apoprotein, opsin, covalently linked to cis-retinal.
Subcellular location	Membrane; Multi-pass membrane protein.
Tissue specificity	The three color pigments are found in the cone photoreceptor cells.
Post-translational modification	Phosphorylated on some or all of the serine and threonine residues present in the C-terminal region.
Involvement in disease	Colorblindness, partial, protan series (CBP) [MIM:303900]: A color vision defect characterized by a dichromasy in which red and green are confused, with loss of luminance and shift of brightness and hue curves toward the short wave end of the spectrum. Dichromasy is due to the use of only two types of photoreceptors, blue plus red in deuteranopia and blue plus green in protanopia. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.7 Blue cone monochromacy (BCM) [MIM:303700]: A rare X-linked congenital stationary cone dysfunction syndrome characterized by the absence of functional long wavelength-sensitive and medium wavelength-sensitive cones in the retina. Color discrimination is severely impaired from birth, and vision is derived from the remaining preserved blue (S) cones and rod photoreceptors. BCM typically presents with reduced visual acuity, pendular nystagmus, and photophobia. Patients often have myopia. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.5 Ref.6
Sequence similarities	Belongs to the G-protein coupled receptor 1 family. Opsin subfamily.
Biophysicochemical properties	Absorption: Abs(max)=560 nm

Ontologies

Keywords
Biological process	Sensory transduction Vision
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Domain	Transmembrane Transmembrane helix
Ligand	Chromophore
Molecular function	G-protein coupled receptor Photoreceptor protein Receptor Retinal protein Transducer
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	phototransduction Inferred from electronic annotation. Source: UniProtKB-KW protein-chromophore linkage Inferred from electronic annotation. Source: UniProtKB-KW visual perception Traceable author statement PubMed 7643192. Source: ProtInc
Cellular_component	integral to plasma membrane Traceable author statement PubMed 9860863. Source: ProtInc
Molecular_function	G-protein coupled receptor activity Inferred from electronic annotation. Source: UniProtKB-KW photoreceptor activity Traceable author statement PubMed 9860863. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 364	364	Long-wave-sensitive opsin 1		PRO_0000197802
Regions
	Topological domain	1 – 52	52	Extracellular
	Transmembrane	53 – 77	25	Helical; Name=1; Potential
	Topological domain	78 – 89	12	Cytoplasmic
	Transmembrane	90 – 115	26	Helical; Name=2; Potential
	Topological domain	116 – 129	14	Extracellular
	Transmembrane	130 – 149	20	Helical; Name=3; Potential
	Topological domain	150 – 168	19	Cytoplasmic
	Transmembrane	169 – 192	24	Helical; Name=4; Potential
	Topological domain	193 – 218	26	Extracellular
	Transmembrane	219 – 246	28	Helical; Name=5; Potential
	Topological domain	247 – 268	22	Cytoplasmic
	Transmembrane	269 – 292	24	Helical; Name=6; Potential
	Topological domain	293 – 300	8	Extracellular
	Transmembrane	301 – 325	25	Helical; Name=7; Potential
	Topological domain	326 – 364	39	Cytoplasmic
Amino acid modifications
	Modified residue	312	1	N6-(retinylidene)lysine
	Glycosylation	34	1	N-linked (GlcNAc...) Probable
	Disulfide bond	126 ↔ 203		Potential
Natural variations
	Natural variant	65	1	T → I. Corresponds to variant rs1065419 [ dbSNP | Ensembl ].		VAR_012009
	Natural variant	111	1	I → V. Corresponds to variant rs1065421 [ dbSNP | Ensembl ].		VAR_012010
	Natural variant	116	1	S → Y. Corresponds to variant rs1065422 [ dbSNP | Ensembl ].		VAR_012011
	Natural variant	153	1	L → M. Corresponds to variant rs713 [ dbSNP | Ensembl ].		VAR_012012
	Natural variant	174	1	A → V. Corresponds to variant rs731613 [ dbSNP | Ensembl ].		VAR_012013
	Natural variant	180	1	S → A in 38% of the population. Ref.4 Corresponds to variant rs949431 [ dbSNP | Ensembl ].		VAR_004842
	Natural variant	203	1	C → R in BCM. Ref.5 Ref.6		VAR_009298
	Natural variant	230	1	I → T. Corresponds to variant rs1065425 [ dbSNP | Ensembl ].		VAR_012014
	Natural variant	274	1	I → V. Corresponds to variant rs2315122 [ dbSNP | Ensembl ].		VAR_050612
	Natural variant	298	1	A → P. Corresponds to variant rs1065440 [ dbSNP | Ensembl ].		VAR_012015
	Natural variant	307	1	P → L in BCM. Ref.5		VAR_009299
	Natural variant	309	1	Y → F. Corresponds to variant rs1065441 [ dbSNP | Ensembl ].		VAR_012016
	Natural variant	338	1	G → E in CBP. Ref.7		VAR_064054

Sequences

	Sequence		Length	Mass (Da)
	P04000 [UniParc]. Last modified October 23, 1986. Version 1. Checksum: D9DACDC17BF20DB3	FASTA	364	40,572
	10 20 30 40 50 60 MAQQWSLQRL AGRHPQDSYE DSTQSSIFTY TNSNSTRGPF EGPNYHIAPR WVYHLTSVWM 70 80 90 100 110 120 IFVVTASVFT NGLVLAATMK FKKLRHPLNW ILVNLAVADL AETVIASTIS IVNQVSGYFV 130 140 150 160 170 180 LGHPMCVLEG YTVSLCGITG LWSLAIISWE RWLVVCKPFG NVRFDAKLAI VGIAFSWIWS 190 200 210 220 230 240 AVWTAPPIFG WSRYWPHGLK TSCGPDVFSG SSYPGVQSYM IVLMVTCCII PLAIIMLCYL 250 260 270 280 290 300 QVWLAIRAVA KQQKESESTQ KAEKEVTRMV VVMIFAYCVC WGPYTFFACF AAANPGYAFH 310 320 330 340 350 360 PLMAALPAYF AKSATIYNPV IYVFMNRQFR NCILQLFGKK VDDGSELSSA SKTEVSSVSS VSPA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular genetics of human color vision: the genes encoding blue, green, and red pigments." Nathans J., Thomas D., Hogness D.S. Science 232:193-202(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Retinal cone cell.
[2]	"The DNA sequence of the human X chromosome." Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R. Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"Molecular biology of the visual pigments." Applebury M.L., Hargrave P.A. Vision Res. 26:1881-1895(1986) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
[4]	"Polymorphism in red photopigment underlies variation in colour matching." Winderickx J., Lindsey D.T., Sanocki E., Teller D.Y., Motulsky A.G., Deeb S.S. Nature 356:431-433(1992) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ALA-180.
[5]	"Genetic heterogeneity among blue-cone monochromats." Nathans J., Maumenee I.H., Zrenner E., Sadowski B., Sharpe L.T., Lewis R.A., Hansen E., Rosenberg T., Schwartz M., Heckenlively J.R. Am. J. Hum. Genet. 53:987-1000(1993) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS BCM ARG-203 AND LEU-307.
[6]	"Gene conversion between red and defective green opsin gene in blue cone monochromacy." Reyniers E., Van Thienen M.N., Meire F., De Boulle K., Devries K., Kestelijn P., Willems P.J. Genomics 29:323-328(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT BCM ARG-203.
[7]	"Novel missense mutations in red/green opsin genes in congenital color-vision deficiencies." Ueyama H., Kuwayama S., Imai H., Tanabe S., Oda S., Nishida Y., Wada A., Shichida Y., Yamade S. Biochem. Biophys. Res. Commun. 294:205-209(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT CBP GLU-338.
+	Additional computationally mapped references.

Web resources

Mutations of the color pigment genes

Retina International's Scientific Newsletter

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M13305 , M13300, M13301, M13302, M13303, M13304 Genomic DNA. Translation: AAB59524.1.
Z68193 Genomic DNA. Translation: CAA92342.1.

IPI

IPI00021724.

PIR

OOHUR. A03157.

RefSeq

NP_064445.1. NM_020061.4.

UniGene

Hs.592247.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1KPX	model	-	A	1-364	[»]

ProteinModelPortal

P04000.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000358967.

Protein family/group databases

GPCRDB

Search...

Polymorphism databases

DMDM

129219.

Proteomic databases

PaxDb

P04000.

PRIDE

P04000.

Protocols and materials databases

DNASU

5956.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000369951; ENSP00000358967; ENSG00000102076.

GeneID

5956.

KEGG

hsa:5956.

UCSC

uc004fjz.4. human.

Organism-specific databases

CTD

5956.

GeneCards

GC0XP153409.

H-InvDB

HIX0203334.

HGNC

HGNC:9936. OPN1LW.

MIM

300822. gene.
303700. phenotype.
303900. phenotype.

neXtProt

NX_P04000.

Orphanet

16. Blue cone monochromatism.
1872. Cone rod dystrophy.

PharmGKB

PA31936.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG240324.

HOGENOM

HOG000253932.

HOVERGEN

HBG107442.

InParanoid

P04000.

KO

K04251.

OMA

MIFAYCV.

OrthoDB

EOG40K806.

PhylomeDB

P04000.

Enzyme and pathway databases

Reactome

REACT_111102. Signal Transduction.

Gene expression databases

ArrayExpress

P04000.

Bgee

P04000.

CleanEx

HS_OPN1LW.

Genevestigator

P04000.

GermOnline

ENSG00000102076. Homo sapiens.

Family and domain databases

InterPro

IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR001760. Opsin.
IPR000378. Opsin_red/grn.
[Graphical view]

Pfam

PF00001. 7tm_1. 1 hit.
[Graphical view]

PRINTS

PR00237. GPCRRHODOPSN.
PR00238. OPSIN.
PR00575. OPSINREDGRN.

PROSITE

PS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
PS00238. OPSIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL1949482.

ChiTaRS

OPN1LW. human.

GenomeRNAi

5956.

NextBio

23196.

SOURCE

Search...

Entry information

Entry name

OPSR_HUMAN

Accession

Primary (citable) accession number: P04000

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 23, 1986
Last sequence update:	October 23, 1986
Last modified:	May 1, 2013
This is version 137 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.