P04001 (OPSG_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Medium-wave-sensitive opsin 1

Alternative name(s):
Green cone photoreceptor pigment
Green-sensitive opsin
Short name=GOP

Gene names

Name:	OPN1MW
Synonyms:	GCP
AND
Name:	OPN1MW2

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, deutan series (CBD) [MIM:303800]: A color vision defect characterized by a dichromasy in which red and green are confused, without loss of luminance or shift or shortening 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.5 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.6 Cone dystrophy 5 (COD5) [MIM:303700]: A X-linked cone dystrophy. Cone dystrophies are retinal dystrophies characterized by progressive degeneration of the cone photoreceptors with preservation of rod function, as indicated by electroretinogram. However, some rod involvement may be present in some cone dystrophies, particularly at late stage. Affected individuals suffer from photophobia, loss of visual acuity, color vision and central visual field. Another sign is the absence of macular lesions for many years. Cone dystrophies are distinguished from the cone-rod dystrophies in which some loss of peripheral vision also occurs. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.8
Sequence similarities	Belongs to the G-protein coupled receptor 1 family. Opsin subfamily.
Biophysicochemical properties	Absorption: Abs(max)=530 nm

Ontologies

Keywords
Biological process	Sensory transduction Vision
Cellular component	Membrane
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	G-protein coupled receptor signaling pathway Traceable author statement Ref.1. Source: ProtInc phototransduction Inferred from electronic annotation. Source: UniProtKB-KW protein-chromophore linkage Inferred from electronic annotation. Source: UniProtKB-KW visual perception Traceable author statement PubMed 10319869. Source: ProtInc
Cellular_component	integral to plasma membrane Traceable author statement Ref.1. Source: ProtInc
Molecular_function	G-protein coupled receptor activity Inferred from electronic annotation. Source: UniProtKB-KW photoreceptor activity Traceable author statement Ref.5. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 364	364	Medium-wave-sensitive opsin 1		PRO_0000197785
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	94	1	N → K in CBD. Ref.7		VAR_064051
	Natural variant	177	1	W → R in COD5; results in protein misfolding and retention in the endoplasmic reticulum. Ref.8		VAR_064052
	Natural variant	203	1	C → R in CBD and BCM. Ref.5 Ref.6		VAR_004841
	Natural variant	330	1	R → Q in CBD. Ref.7		VAR_064053

Sequences

	Sequence		Length	Mass (Da)
	P04001 [UniParc]. Last modified October 23, 1986. Version 1. Checksum: A98D046958C72AE9	FASTA	364	40,584
	10 20 30 40 50 60 MAQQWSLQRL AGRHPQDSYE DSTQSSIFTY TNSNSTRGPF EGPNYHIAPR WVYHLTSVWM 70 80 90 100 110 120 IFVVIASVFT NGLVLAATMK FKKLRHPLNW ILVNLAVADL AETVIASTIS VVNQVYGYFV 130 140 150 160 170 180 LGHPMCVLEG YTVSLCGITG LWSLAIISWE RWMVVCKPFG NVRFDAKLAI VGIAFSWIWA 190 200 210 220 230 240 AVWTAPPIFG WSRYWPHGLK TSCGPDVFSG SSYPGVQSYM IVLMVTCCIT PLSIIVLCYL 250 260 270 280 290 300 QVWLAIRAVA KQQKESESTQ KAEKEVTRMV VVMVLAFCFC WGPYAFFACF AAANPGYPFH 310 320 330 340 350 360 PLMAALPAFF 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]	Buck D. Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 194-364.
[4]	"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.
[5]	"Defective colour vision associated with a missense mutation in the human green visual pigment gene." Winderickx J., Sanocki E., Lindsey D.T., Teller D.Y., Motulsky A.G., Deeb S.S. Nat. Genet. 1:251-256(1992) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT CBD ARG-203.
[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: VARIANTS CBD LYS-94 AND GLN-330.
[8]	"X-linked cone dystrophy caused by mutation of the red and green cone opsins." Gardner J.C., Webb T.R., Kanuga N., Robson A.G., Holder G.E., Stockman A., Ripamonti C., Ebenezer N.D., Ogun O., Devery S., Wright G.A., Maher E.R., Cheetham M.E., Moore A.T., Michaelides M., Hardcastle A.J. Am. J. Hum. Genet. 87:26-39(2010) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT COD5 ARG-177, CHARACTERIZATION OF VARIANT COD5 ARG-177.
+	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

K03494 , M13306, K03490, K03491, K03492, K03493 Genomic DNA. Translation: AAB59503.1.
K03497, K03495, K03496 Genomic DNA. Translation: AAB59525.1. Sequence problems.
AC092402 Genomic DNA. No translation available.
Z46936 Genomic DNA. No translation available.

IPI

IPI00021725.

PIR

OOHUG. A03158.

RefSeq

NP_000504.1. NM_000513.2.
NP_001041646.1. NM_001048181.2.
XP_003960138.1. XM_003960089.1.

UniGene

Hs.247787.
Hs.571751.

3D structure databases

PDBe
RCSB PDB
PDBj

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

ProteinModelPortal

P04001.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000358945.

Protein family/group databases

GPCRDB

Search...

PTM databases

PhosphoSite

P04001.

Proteomic databases

PaxDb

P04001.

PRIDE

P04001.

Protocols and materials databases

DNASU

2652.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000369929; ENSP00000358945; ENSG00000166160.
ENST00000369935; ENSP00000358951; ENSG00000147380.
ENST00000595290; ENSP00000472316; ENSG00000268221.
ENST00000599007; ENSP00000470778; ENSG00000269133.

GeneID

101060233.
2652.
728458.

KEGG

hsa:101060233.
hsa:2652.
hsa:728458.

UCSC

uc004fkb.3. human.

Organism-specific databases

CTD

2652.
728458.

GeneCards

GC0XP153448.
GC0XP153485.

H-InvDB

HIX0056274.

HGNC

HGNC:4206. OPN1MW.
HGNC:26952. OPN1MW2.

MIM

300821. gene.
303700. phenotype.
303800. phenotype.

neXtProt

NX_P04001.

Orphanet

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

PharmGKB

PA142671229.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG240324.

HOGENOM

HOG000253932.

HOVERGEN

HBG107442.

InParanoid

P04001.

KO

K04251.

OMA

FCWGPYT.

OrthoDB

EOG40K806.

PhylomeDB

P04001.

Enzyme and pathway databases

Reactome

REACT_111102. Signal Transduction.

Gene expression databases

Bgee

P04001.

CleanEx

HS_OPN1MW.
HS_OPN1MW2.

Genevestigator

P04001.

GermOnline

ENSG00000147380. Homo sapiens.
ENSG00000166160. 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

NextBio

10480.

SOURCE

Search...

Entry information

Entry name

OPSG_HUMAN

Accession

Primary (citable) accession number: P04001

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 23, 1986
Last sequence update:	October 23, 1986
Last modified:	May 1, 2013
This is version 134 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.