OPSD_SMICR
ID OPSD_SMICR Reviewed; 348 AA.
AC Q8HY69;
DT 27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 2.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Rhodopsin;
GN Name=RHO; Synonyms=RH1;
OS Sminthopsis crassicaudata (Fat-tailed dunnart) (Phascogale crassicaudata).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Dasyuromorphia; Dasyuridae; Sminthopsis.
OX NCBI_TaxID=9301;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=14659889; DOI=10.1016/j.gene.2003.09.016;
RA Hunt D.M., Arrese C.A., von Dornum M., Rodger J., Oddy A., Cowing J.A.,
RA Ager E.I., Bowmaker J.K., Beazley L.D., Shand J.;
RT "The rod opsin pigments from two marsupial species, the South American
RT bare-tailed woolly opossum and the Australian fat-tailed dunnart.";
RL Gene 323:157-162(2003).
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 the arrestin SAG and terminates
CC signaling (By similarity). {ECO:0000250|UniProtKB:P02699,
CC ECO:0000250|UniProtKB:P08100}.
CC -!- SUBUNIT: Homodimer (By similarity). May form a complex composed of RHO,
CC GRK1 and RCVRN in a Ca(2+)-dependent manner; RCVRN prevents the
CC interaction between GRK1 and RHO (By similarity). Interacts with GRK1
CC (By similarity). Interacts (phosphorylated form) with SAG. Interacts
CC with GNAT1. Interacts with GNAT3. SAG and G-proteins compete for a
CC common binding site (By similarity). Interacts with PRCD; the
CC interaction promotes PRCD stability. {ECO:0000250|UniProtKB:P02699,
CC ECO:0000250|UniProtKB:P08100}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P02699}; Multi-
CC pass membrane protein {ECO:0000250|UniProtKB:P02699}. Cell projection,
CC cilium, photoreceptor outer segment {ECO:0000250|UniProtKB:P02699}.
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 -!- 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. 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY159786; AAN86046.2; -; mRNA.
DR AlphaFoldDB; Q8HY69; -.
DR SMR; Q8HY69; -.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0097381; C:photoreceptor disc membrane; ISS:UniProtKB.
DR GO; GO:0060342; C:photoreceptor inner segment membrane; ISS:UniProtKB.
DR GO; GO:0042622; C:photoreceptor outer segment 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016038; P:absorption of visible light; ISS:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; 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 SMART; SM01381; 7TM_GPCR_Srsx; 1.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR PROSITE; PS00238; OPSIN; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cell projection; Chromophore; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane;
KW Metal-binding; Palmitate; Phosphoprotein; Photoreceptor protein; Receptor;
KW Retinal protein; Sensory transduction; Transducer; Transmembrane;
KW Transmembrane helix; Vision; Zinc.
FT CHAIN 1..348
FT /note="Rhodopsin"
FT /id="PRO_0000197720"
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..348
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 330..348
FT /note="Interaction with SAG"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT MOTIF 134..136
FT /note="'Ionic lock' involved in activated form
FT stabilization"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT BINDING 201
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT BINDING 279
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
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 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT MOD_RES 296
FT /note="N6-(retinylidene)lysine"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02700"
FT MOD_RES 335
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02700"
FT MOD_RES 336
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02700"
FT MOD_RES 338
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02700"
FT MOD_RES 340
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT MOD_RES 342
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT MOD_RES 343
FT /note="Phosphoserine"
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"
SQ SEQUENCE 348 AA; 39064 MW; C596CD0A56957FF0 CRC64;
MNGTEGPNFY VPYSNKSGVV RSPYEEPQYY LAEPWMFSCL AAYMFMLIVL GFPINFLTLY
VTIQHKKLRT PLNYILLNLA VADLFMVICG FTTTLVTSLN GYFVFGTTGC LVEGFFATTG
GEVALWALVV LAIERYIVVC KPMSNFRFGE NHAIMGVAFT WIMALACSVP PIFGWSRYIP
EGMQCSCGID YYTLNPEFNN ESFVIYMFVV HFIIPLTVIF FCYGQLVFTV KEAAAQQQES
ATTQKAEKEV TRMVIIMVIA FLICWVPYAS VAFYIFTHQG SDFGPIFMTL PAFFAKSSSI
YNPVIYIMMN KQFRNCMITT LCCGKNPLGD DEASTTASKT ETSQVAPA
