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OPSD_SARSP
ID   OPSD_SARSP              Reviewed;         347 AA.
AC   P79903;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Rhodopsin;
DE   Flags: Fragment;
GN   Name=rho;
OS   Sargocentron spiniferum (Sabre squirrelfish) (Adioryx spinifer).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Holocentriformes; Holocentridae; Sargocentron.
OX   NCBI_TaxID=47712;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Eye;
RA   Toller W.W., Moses K., McFall-Ngai M.J.;
RT   "Molecular phylogeny of 11 holocentrid fishes (Order Beryciformes) inferred
RT   from rhodopsin cDNA and cytochrome b.";
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:P35359}.
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.
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; U57544; AAB39532.1; -; mRNA.
DR   AlphaFoldDB; P79903; -.
DR   SMR; P79903; -.
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   2: Evidence at transcript level;
KW   Cell projection; Chromophore; Disulfide bond; G-protein coupled receptor;
KW   Glycoprotein; Lipoprotein; Membrane; Palmitate; Phosphoprotein;
KW   Photoreceptor protein; Receptor; Retinal protein; Sensory transduction;
KW   Transducer; Transmembrane; Transmembrane helix; Vision.
FT   CHAIN           <1..347
FT                   /note="Rhodopsin"
FT                   /id="PRO_0000197715"
FT   TOPO_DOM        <1..33
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        34..58
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000250|UniProtKB:P02699"
FT   TOPO_DOM        59..70
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        71..93
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000250|UniProtKB:P02699"
FT   TOPO_DOM        94..107
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        108..130
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000250|UniProtKB:P02699"
FT   TOPO_DOM        131..149
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        150..170
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000250|UniProtKB:P02699"
FT   TOPO_DOM        171..199
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        200..221
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000250|UniProtKB:P02699"
FT   TOPO_DOM        222..249
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        250..271
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000250|UniProtKB:P02699"
FT   TOPO_DOM        272..283
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        284..305
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000250|UniProtKB:P02699"
FT   TOPO_DOM        306..347
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   REGION          326..347
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           131..133
FT                   /note="'Ionic lock' involved in activated form
FT                   stabilization"
FT                   /evidence="ECO:0000250|UniProtKB:P02699"
FT   SITE            110
FT                   /note="Plays an important role in the conformation switch
FT                   to the active conformation"
FT                   /evidence="ECO:0000250|UniProtKB:P02699"
FT   MOD_RES         293
FT                   /note="N6-(retinylidene)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P02699"
FT   LIPID           320
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P02699"
FT   CARBOHYD        12
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        197
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        107..184
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   NON_TER         1
SQ   SEQUENCE   347 AA;  39137 MW;  091ECDA403E90FE9 CRC64;
     TEGPDFYIPM VNTTGVVRSP YEYPQYYLVN PAAYAVLGAY MFFLIIVGFP INFLTLYVTL
     EHKKLRTPLN YILLNLAVAD LFMVIGGFTT TMYSSMHGYF VLGRLGCNIE GFFATLGGMI
     SLWSLAVLAI ERWVVVCKPI SNFRFGENHA IMGVSLTWVM ALACTVPPLV GWSRYIPEGM
     QCACGIDYYT RAEGYNNESF VIYMFTFHFL FPMFIIFFCY GRLLCAVKEA AAAQQESETT
     QRAEREVTRM VILMVIGYLV CWLPYASVAW FIFTHKGSEF GPLFMAVPSF FAKSSSIYNP
     IIYICMNKQF RQCMITTLFC GKNPFEGQEE DSSTKTEASS ASSVSPA
 
 
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