OPSD_DANRE
ID OPSD_DANRE Reviewed; 354 AA.
AC P35359; Q9PWN4;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 27-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Rhodopsin;
GN Name=rho; Synonyms=zfo2;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Eye;
RX PubMed=8327475; DOI=10.1073/pnas.90.13.6009;
RA Robinson J., Schmitt E.A., Harosi F.I., Reece R.J., Dowling J.E.;
RT "Zebrafish ultraviolet visual pigment: absorption spectrum, sequence, and
RT localization.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:6009-6012(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RX PubMed=8924413; DOI=10.1017/s0952523800009457;
RA Robinson J., Schmitt E.A., Dowling J.E.;
RT "Temporal and spatial patterns of opsin gene expression in zebrafish (Danio
RT rerio).";
RL Vis. Neurosci. 12:895-906(1995).
RN [3]
RP ERRATUM OF PUBMED:8924413.
RX PubMed=10349978; DOI=10.1017/s0952523899163181;
RA Schmitt E.A., Hyatt G.A., Dowling J.E.;
RL Vis. Neurosci. 16:601-605(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC TISSUE=Eye;
RX PubMed=10349976; DOI=10.1017/s0952523899163168;
RA Vihtelic T.S., Doro C.J., Hyde D.R.;
RT "Cloning and characterization of six zebrafish photoreceptor opsin cDNAs
RT and immunolocalization of their corresponding proteins.";
RL Vis. Neurosci. 16:571-585(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX PubMed=11278688; DOI=10.1074/jbc.m010490200;
RA Kennedy B.N., Vihtelic T.S., Checkley L., Vaughan K.T., Hyde D.R.;
RT "Isolation of a zebrafish rod opsin promoter to generate a transgenic
RT zebrafish line expressing enhanced green fluorescent protein in rod
RT photoreceptors.";
RL J. Biol. Chem. 276:14037-14043(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP IDENTIFICATION AS RHODOPSIN, AND TISSUE SPECIFICITY.
RX PubMed=8603882;
RA Raymond P.A., Barthel L.K., Stenkamp D.L.;
RT "The zebrafish ultraviolet cone opsin reported previously is expressed in
RT rods.";
RL Invest. Ophthalmol. Vis. Sci. 37:948-950(1996).
CC -!- FUNCTION: Photoreceptor required for image-forming vision at low light
CC intensity. While most salt water fish species use retinal as
CC chromophore, most freshwater fish use 3-dehydroretinal, or a mixture of
CC retinal and 3-dehydroretinal (By similarity). Light-induced
CC isomerization of 11-cis to all-trans retinal triggers a conformational
CC change that activates signaling via G-proteins. Subsequent receptor
CC phosphorylation mediates displacement of the bound G-protein alpha
CC subunit by arrestin and terminates signaling (By similarity).
CC {ECO:0000250|UniProtKB:P02699, ECO:0000250|UniProtKB:P08100,
CC ECO:0000250|UniProtKB:P32309}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P08100}; Multi-
CC pass membrane protein {ECO:0000250|UniProtKB:P08100}. Cell projection,
CC cilium, photoreceptor outer segment {ECO:0000269|PubMed:10349976}.
CC Note=Synthesized in the inner segment (IS) of rod photoreceptor cells
CC before vectorial transport to disk membranes in the rod outer segment
CC (OS) photosensory cilia. {ECO:0000250|UniProtKB:P08100}.
CC -!- TISSUE SPECIFICITY: Retinal rod photoreceptor cells, predominantly in
CC the outer segments (at protein level) (PubMed:10349976). Retinal rod
CC photoreceptor cells (PubMed:8327475, PubMed:8603882).
CC {ECO:0000269|PubMed:10349976, ECO:0000269|PubMed:8327475,
CC ECO:0000269|PubMed:8603882}.
CC -!- DEVELOPMENTAL STAGE: First detected at 51 hours post-fertilization
CC (hpf) in the ventral retina. At 60 hpf, expressed in a strip across the
CC ventrotemporal retina. By 96 hpf, also expressed in the dorsal retina.
CC {ECO:0000269|PubMed:8924413}.
CC -!- PTM: Phosphorylated on some or all of the serine and threonine residues
CC present in the C-terminal region. {ECO:0000250|UniProtKB:P02699}.
CC -!- PTM: Contains one covalently linked retinal chromophore.
CC {ECO:0000250|UniProtKB:P02699}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Opsin
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC -!- CAUTION: Was originally (PubMed:8327475 and PubMed:8924413) thought to
CC be an ultraviolet-sensitive opsin present in short single cones.
CC {ECO:0000305}.
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DR EMBL; L11014; AAA85566.1; -; mRNA.
DR EMBL; AF105152; AAD14679.1; -; mRNA.
DR EMBL; AF109368; AAD24751.1; -; mRNA.
DR EMBL; AF331797; AAK01136.1; -; Genomic_DNA.
DR EMBL; BC063938; AAH63938.1; -; mRNA.
DR PIR; A48191; A48191.
DR RefSeq; NP_571159.1; NM_131084.1.
DR AlphaFoldDB; P35359; -.
DR SMR; P35359; -.
DR STRING; 7955.ENSDARP00000011562; -.
DR TCDB; 9.A.14.1.12; the g-protein-coupled receptor (gpcr) family.
DR PaxDb; P35359; -.
DR Ensembl; ENSDART00000027000; ENSDARP00000011562; ENSDARG00000002193.
DR GeneID; 30295; -.
DR KEGG; dre:30295; -.
DR CTD; 6010; -.
DR ZFIN; ZDB-GENE-990415-271; rho.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01030000234549; -.
DR HOGENOM; CLU_009579_3_0_1; -.
DR InParanoid; P35359; -.
DR OMA; QYYLVNP; -.
DR OrthoDB; 940057at2759; -.
DR PhylomeDB; P35359; -.
DR TreeFam; TF324998; -.
DR Reactome; R-DRE-2453902; The canonical retinoid cycle in rods (twilight vision).
DR Reactome; R-DRE-2485179; Activation of the phototransduction cascade.
DR Reactome; R-DRE-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR Reactome; R-DRE-418594; G alpha (i) signalling events.
DR Reactome; R-DRE-419771; Opsins.
DR Reactome; R-DRE-5620916; VxPx cargo-targeting to cilium.
DR PRO; PR:P35359; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 8.
DR Bgee; ENSDARG00000002193; Expressed in photoreceptor cell and 14 other tissues.
DR ExpressionAtlas; P35359; baseline.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0097381; C:photoreceptor disc membrane; ISS:UniProtKB.
DR GO; GO:0001750; C:photoreceptor outer segment; IDA:ZFIN.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005502; F:11-cis retinal binding; ISS:UniProtKB.
DR GO; GO:0008020; F:G protein-coupled photoreceptor activity; IDA:ZFIN.
DR GO; GO:0009881; F:photoreceptor activity; IDA:ZFIN.
DR GO; GO:0016918; F:retinal binding; IDA:ZFIN.
DR GO; GO:0016038; P:absorption of visible light; IDA:ZFIN.
DR GO; GO:0071482; P:cellular response to light stimulus; IBA:GO_Central.
DR GO; GO:0009583; P:detection of light stimulus; IDA:ZFIN.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007602; P:phototransduction; IBA:GO_Central.
DR GO; GO:0016056; P:rhodopsin mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR001760; Opsin.
DR InterPro; IPR027430; Retinal_BS.
DR InterPro; IPR000732; Rhodopsin.
DR InterPro; IPR019477; Rhodopsin_N.
DR Pfam; PF00001; 7tm_1; 1.
DR Pfam; PF10413; Rhodopsin_N; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00238; OPSIN.
DR PRINTS; PR00579; RHODOPSIN.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR PROSITE; PS00238; OPSIN; 1.
PE 1: Evidence at protein level;
KW Cell projection; Chromophore; Disulfide bond; G-protein coupled receptor;
KW Glycoprotein; Membrane; Phosphoprotein; Photoreceptor protein; Receptor;
KW Reference proteome; Retinal protein; Sensory transduction; Transducer;
KW Transmembrane; Transmembrane helix; Vision.
FT CHAIN 1..354
FT /note="Rhodopsin"
FT /id="PRO_0000197654"
FT TOPO_DOM 1..36
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 37..61
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT TOPO_DOM 62..73
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 74..96
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT TOPO_DOM 97..110
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 111..133
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT TOPO_DOM 134..152
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 153..173
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT TOPO_DOM 174..202
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 203..224
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT TOPO_DOM 225..252
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 253..274
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT TOPO_DOM 275..286
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 287..308
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT TOPO_DOM 309..354
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 333..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 134..136
FT /note="'Ionic lock' involved in activated form
FT stabilization"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT SITE 113
FT /note="Plays an important role in the conformation switch
FT to the active conformation"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT MOD_RES 296
FT /note="N6-(retinylidene)lysine"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT CARBOHYD 2
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 15
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 110..187
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 39..40
FT /note="LL -> FV (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 126
FT /note="W -> K (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 235
FT /note="A -> R (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 354 AA; 39706 MW; 6C5D49B51059D238 CRC64;
MNGTEGPAFY VPMSNATGVV RSPYEYPQYY LVAPWAYGLL AAYMFFLIIT GFPVNFLTLY
VTIEHKKLRT PLNYILLNLA IADLFMVFGG FTTTMYTSLH GYFVFGRLGC NLEGFFATLG
GEMGLWSLVV LAIERWMVVC KPVSNFRFGE NHAIMGVAFT WVMACSCAVP PLVGWSRYIP
EGMQCSCGVD YYTRTPGVNN ESFVIYMFIV HFFIPLIVIF FCYGRLVCTV KEAAAQQQES
ETTQRAEREV TRMVIIMVIA FLICWLPYAG VAWYIFTHQG SEFGPVFMTL PAFFAKTSAV
YNPCIYICMN KQFRHCMITT LCCGKNPFEE EEGASTTASK TEASSVSSSS VSPA
