OPSD_XENLA
ID OPSD_XENLA Reviewed; 354 AA.
AC P29403;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Rhodopsin;
GN Name=rho;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8510503; DOI=10.1016/0169-328x(93)90016-i;
RA Saha M.S., Grainger R.M.;
RT "Early opsin expression in Xenopus embryos precedes photoreceptor
RT differentiation.";
RL Brain Res. Mol. Brain Res. 17:307-318(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=8621718; DOI=10.1074/jbc.271.6.3179;
RA Batni S., Scalzetti L.C., Moody S.A., Knox B.E.;
RT "Characterization of the Xenopus rhodopsin gene.";
RL J. Biol. Chem. 271:3179-3186(1996).
RN [3]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF PRO-23.
RX PubMed=22276148; DOI=10.1371/journal.pone.0030101;
RA Haeri M., Knox B.E.;
RT "Rhodopsin mutant P23H destabilizes rod photoreceptor disk membranes.";
RL PLoS ONE 7:E30101-E30101(2012).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=26492040; DOI=10.1371/journal.pone.0141114;
RA Rakshit T., Senapati S., Sinha S., Whited A.M., Park P.S.;
RT "Rhodopsin Forms Nanodomains in Rod Outer Segment Disc Membranes of the
RT Cold-Blooded Xenopus laevis.";
RL PLoS ONE 10:E0141114-E0141114(2015).
CC -!- FUNCTION: Photoreceptor required for image-forming vision at low light
CC intensity. Required for photoreceptor cell viability after birth (By
CC similarity). Light-induced isomerization of 11-cis to all-trans retinal
CC triggers a conformational change that activates signaling via G-
CC proteins. Subsequent receptor phosphorylation mediates displacement of
CC the bound G-protein alpha subunit by arrestin and terminates signaling
CC (By similarity). {ECO:0000250|UniProtKB:P02699,
CC ECO:0000250|UniProtKB:P08100}.
CC -!- INTERACTION:
CC P29403; P51644: arf4; NbExp=2; IntAct=EBI-7490990, EBI-7491013;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:26492040}; Multi-
CC pass membrane protein {ECO:0000250|UniProtKB:P08100}. Cell projection,
CC cilium, photoreceptor outer segment {ECO:0000269|PubMed:22276148,
CC ECO:0000269|PubMed:26492040}. Note=Synthesized in the inner segment
CC (IS) of rod photoreceptor cells before vectorial transport to disk
CC membranes in the rod outer segment (OS) photosensory cilia.
CC {ECO:0000269|PubMed:22276148}.
CC -!- PTM: Contains one covalently linked retinal chromophore. Upon light
CC absorption, the covalently bound 11-cis-retinal is converted to all-
CC trans-retinal. After hydrolysis of the Schiff base and release of the
CC covalently bound all-trans-retinal, active rhodopsin is regenerated by
CC binding of a fresh molecule of 11-cis-retinal.
CC {ECO:0000250|UniProtKB:P02699}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Opsin
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; S62229; AAB27128.2; -; mRNA.
DR EMBL; L04692; AAB59950.1; -; mRNA.
DR EMBL; L07770; AAC42232.1; -; mRNA.
DR EMBL; U23808; AAC59901.1; -; Genomic_DNA.
DR PIR; I51200; I51200.
DR RefSeq; XP_018114543.1; XM_018259054.1.
DR AlphaFoldDB; P29403; -.
DR SMR; P29403; -.
DR IntAct; P29403; 2.
DR MINT; P29403; -.
DR GeneID; 108714644; -.
DR KEGG; xla:108714644; -.
DR CTD; 108714644; -.
DR Xenbase; XB-GENE-18034123; rho.2.L.
DR OrthoDB; 940057at2759; -.
DR Proteomes; UP000186698; Chromosome 4L.
DR Bgee; 108714644; Expressed in camera-type eye and 7 other tissues.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0097381; C:photoreceptor disc membrane; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0016038; P:absorption of visible light; ISS:UniProtKB.
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; Lipoprotein; Membrane; Palmitate; Phosphoprotein;
KW Photoreceptor protein; Receptor; Reference proteome; Retinal protein;
KW Sensory transduction; Transducer; Transmembrane; Transmembrane helix;
KW Vision.
FT CHAIN 1..354
FT /note="Rhodopsin"
FT /id="PRO_0000197727"
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 331..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 COMPBIAS 332..354
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 LIPID 322
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT LIPID 323
FT /note="S-palmitoyl cysteine"
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 DISULFID 110..187
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT MUTAGEN 23
FT /note="P->H: Near loss of rhodopsin accumulation in rod
FT outer segments."
FT /evidence="ECO:0000269|PubMed:22276148"
FT CONFLICT 107
FT /note="P -> Q (in Ref. 2; AAC42232/AAC59901)"
FT /evidence="ECO:0000305"
FT CONFLICT 137
FT /note="I -> M (in Ref. 2; AAC42232/AAC59901)"
FT /evidence="ECO:0000305"
FT CONFLICT 241
FT /note="L -> A (in Ref. 2; AAC42232/AAC59901)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 354 AA; 39787 MW; CD18F49EC63D8FFE CRC64;
MNGTEGPNFY VPMSNKTGVV RSPFDYPQYY LAEPWQYSAL AAYMFLLILL GLPINFMTLF
VTIQHKKLRT PLNYILLNLV FANHFMVLCG FTVTMYTSMH GYFIFGPTGC YIEGFFATLG
GEVALWSLVV LAVERYIVVC KPMANFRFGE NHAIMGVAFT WIMALSCAAP PLFGWSRYIP
EGMQCSCGVD YYTLKPEVNN ESFVIYMFIV HFTIPLIVIF FCYGRLLCTV KEAAAQQQES
LTTQKAEKEV TRMVVIMVVF FLICWVPYAY VAFYIFTHQG SNFGPVFMTV PAFFAKSSAI
YNPVIYIVLN KQFRNCLITT LCCGKNPFGD EDGSSAATSK TEASSVSSSQ VSPA
