ID   OPSB_CARAU              Reviewed;         351 AA.
AC   P32310;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Blue-sensitive opsin;
DE   AltName: Full=Blue 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)=441 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}.
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; L11864; AAA49164.1; -; mRNA.
DR   PIR; E45229; E45229.
DR   AlphaFoldDB; P32310; -.
DR   SMR; P32310; -.
DR   Proteomes; UP000515129; Genome assembly.
DR   GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
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; IPR001521; Opsin_blue.
DR   InterPro; IPR027430; Retinal_BS.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00238; OPSIN.
DR   PRINTS; PR00574; OPSINBLUE.
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..351
FT                   /note="Blue-sensitive opsin"
FT                   /id="PRO_0000197756"
FT   TOPO_DOM        1..40
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        41..65
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        66..77
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        78..103
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        104..117
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        118..137
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        138..156
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        157..180
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        181..206
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        207..234
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        235..256
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        257..280
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        281..288
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        289..313
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        314..351
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         300
FT                   /note="N6-(retinylidene)lysine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        21
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        114..191
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   351 AA;  39275 MW;  168282A30551A994 CRC64;
     MKQVPEFHED FYIPIPLDIN NLSAYSPFLV PQDHLGNQGI FMAMSVFMFF IFIGGASINI
     LTILCTIQFK KLRSHLNYIL VNLSIANLFV AIFGSPLSFY SFFNRYFIFG ATACKIEGFL
     ATLGGMVGLW SLAVVAFERW LVICKPLGNF TFKTPHAIAG CILPWISALA ASLPPLFGWS
     RYIPEGLQCS CGPDWYTTNN KYNNESYVMF LFCFCFAVPF GTIVFCYGQL LITLKLAAKA
     QADSASTQKA EREVTKMVVV MVLGFLVCWA PYASFSLWIV SHRGEEFDLR MATIPSCLSK
     ASTVYNPVIY VLMNKQFRSC MMKMVCGKNI EEDEASTSSQ VTQVSSVAPE K