OPSD_ICTPU
ID OPSD_ICTPU Reviewed; 304 AA.
AC O42268;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Rhodopsin;
DE Flags: Fragment;
GN Name=rho;
OS Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Ictaluridae; Ictalurus.
OX NCBI_TaxID=7998;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9334384; DOI=10.1523/jneurosci.17-21-08083.1997;
RA Blackshaw S., Snyder S.H.;
RT "Parapinopsin, a novel catfish opsin localized to the parapineal organ,
RT defines a new gene family.";
RL J. Neurosci. 17:8083-8092(1997).
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; AF028016; AAB84052.1; -; mRNA.
DR AlphaFoldDB; O42268; -.
DR SMR; O42268; -.
DR PRIDE; O42268; -.
DR Proteomes; UP000221080; Genome assembly.
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 Pfam; PF00001; 7tm_1; 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..>304
FT /note="Rhodopsin"
FT /id="PRO_0000197678"
FT TOPO_DOM 1..13
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 14..38
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT TOPO_DOM 39..50
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 51..73
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT TOPO_DOM 74..87
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 88..110
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT TOPO_DOM 111..129
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 130..150
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT TOPO_DOM 151..179
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 180..201
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT TOPO_DOM 202..229
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 230..251
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT TOPO_DOM 252..263
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 264..285
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT TOPO_DOM 286..304
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT MOTIF 111..113
FT /note="'Ionic lock' involved in activated form
FT stabilization"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT SITE 90
FT /note="Plays an important role in the conformation switch
FT to the active conformation"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT MOD_RES 273
FT /note="N6-(retinylidene)lysine"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT LIPID 299
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT LIPID 300
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 87..164
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT NON_TER 1
FT NON_TER 304
SQ SEQUENCE 304 AA; 34407 MW; B1E9A76977136F46 CRC64;
YEYPQYYLVN PAAYAALGAY MFLLILVGFP INFLTLYVTI EHKKLRTPLN YILLNLAVAN
LFMVFGGFTT TMFTSIRGYF VLGHLGCNLE GFFATLSGEI ALWSLVVLAI ERWVVVCKPI
SNFRFGENHA IMGLAFTWTM AMACAAPPLV GWSRYIPEGM QCSCGIDYYT RAEGFNNESF
VVYMFTCHFM TPLTIVFFCY GRLLCAVKEA AAAQQESETT QRAEREVTRM VVIMVIAFLI
CWCPYAGVAW FIFTHQGSEF GPVFMTIPAF FAKSSSIYNP MIYICLNKQF RHCMITTLCC
GKKA
