ID   OPSR_CARAU              Reviewed;         357 AA.
AC   P32313;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Red-sensitive opsin;
DE   AltName: Full=Red cone photoreceptor pigment;
OS   Carassius auratus (Goldfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Cyprininae; Carassius.
OX   NCBI_TaxID=7957;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8418840; DOI=10.1021/bi00052a027;
RA   Johnson R.L., Grant K.B., Zankel T.C., Boehm M.F., Merbs S.L., Nathans J.,
RA   Nakanishi K.;
RT   "Cloning and expression of goldfish opsin sequences.";
RL   Biochemistry 32:208-214(1993).
CC   -!- FUNCTION: Visual pigments are the light-absorbing molecules that
CC       mediate vision. They consist of an apoprotein, opsin, covalently linked
CC       to cis-retinal.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Absorption:
CC         Abs(max)=525 nm;
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: The color pigments are found in the cone
CC       photoreceptor cells.
CC   -!- PTM: Phosphorylated on some or all of the serine and threonine residues
CC       present in the C-terminal region.
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; L11867; AAA49190.1; -; mRNA.
DR   PIR; D45229; D45229.
DR   AlphaFoldDB; P32313; -.
DR   SMR; P32313; -.
DR   Proteomes; UP000515129; Genome assembly.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0009881; F:photoreceptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0007602; P:phototransduction; IEA:UniProtKB-KW.
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; IPR000378; Opsin_red/grn.
DR   InterPro; IPR027430; Retinal_BS.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00238; OPSIN.
DR   PRINTS; PR00575; OPSINREDGRN.
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   1: Evidence at protein level;
KW   Chromophore; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW   Membrane; Phosphoprotein; Photoreceptor protein; Receptor;
KW   Reference proteome; Retinal protein; Sensory transduction; Transducer;
KW   Transmembrane; Transmembrane helix; Vision.
FT   CHAIN           1..357
FT                   /note="Red-sensitive opsin"
FT                   /id="PRO_0000197795"
FT   TOPO_DOM        1..49
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        50..74
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        75..86
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        87..112
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        113..126
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        127..146
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        147..165
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        166..189
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        190..215
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        216..243
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        244..265
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        266..289
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        290..297
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        298..322
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        323..357
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         309
FT                   /note="N6-(retinylidene)lysine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        31
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        123..200
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   357 AA;  39970 MW;  3B0C3948A182A08E CRC64;
     MAEQWGDAIF AARRRGDETT RESMFVYTNS NNTRDPFEGP NYHIAPRWVY NLATVWMFFV
     VVASTFTNGL VLVATAKFKK LRHPLNWILV NLAVADLAET LLASTISVTN QFFGYFILGH
     PMCIFEGFTV SVCGIAGLWS LTVISWERWV VVCKPFGNVK FDAKWASAGI IFSWVWSAIW
     CAPPIFGWSR FWPHGLKTSC GPDVFSGSED PGVQSYMIVL MITCCIIPLA IIILCYIAVW
     LAIRTVAQQQ KDSESTQKAE KEVSRMVVVM IFAYCFCWGP YTFCACFAAA NPGYAFHPLA
     AAMPAYFAKS ATIYNPIIYV FMNRQFRVCI MQLFGKKVDD GSEVSTSKTE VSSVAPA