OPSD_NEOAU
ID OPSD_NEOAU Reviewed; 347 AA.
AC P79809;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Rhodopsin;
DE Flags: Fragment;
GN Name=rho;
OS Neoniphon aurolineatus (Yellowstriped squirrelfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Holocentriformes; Holocentridae; Neoniphon.
OX NCBI_TaxID=47705;
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; U57541; AAB39522.1; -; mRNA.
DR AlphaFoldDB; P79809; -.
DR SMR; P79809; -.
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_0000197693"
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; 38992 MW; 89F6FD5FD79EA8E5 CRC64;
TEGPDFYIPM VNTSGLVRSP YEYPQYYLVN PAAFAFLGAY MFFLIIIGFP VNFLTLYVTL
EHKKLRTPLN YILLNLAVSD LFMVIGGFTT TMYSSMHGYF VLGRLGCNIE GFFATLGGMI
SLWSLAVLAI ERWVVVCKPI SNFRFGENHA IMGVSMTWLL ALSCTVPPLV GWSRYIPEGM
QCACGIDYYT RAEGYNNESF VIYMFTCHFS VPLFIIFFCY GRLLCAVKEA AAAQQESETT
QRAEREVTRM VVIMVIGFLV CWLPYASVAW FIFTHQGSEF GPLFMAIPSF FAKSSSIYNP
VIYICMNKQF RQCMITTLFC GKNPFEGEEE GSSTKTEASS ASSVSPA
