OPSB_CONCO
ID OPSB_CONCO Reviewed; 350 AA.
AC O13227;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Blue-sensitive opsin;
DE AltName: Full=Blue cone photoreceptor pigment;
OS Conger conger (Conger eel) (Muraena conger).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Anguilliformes; Congridae; Conger.
OX NCBI_TaxID=82655;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=8763796; DOI=10.1098/rspb.1996.0114;
RA Archer S., Hirano J.;
RT "Absorbance spectra and molecular structure of the blue-sensitive rod
RT visual pigment in the conger eel (Conger conger).";
RL Proc. R. Soc. B 263:761-767(1996).
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)=~487 nm {ECO:0000269|PubMed:8763796};
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Rod shaped photoreceptor cells which mediates
CC vision in dim light.
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; S82619; AAB37721.1; -; mRNA.
DR AlphaFoldDB; O13227; -.
DR SMR; O13227; -.
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; 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 1: Evidence at protein level;
KW Chromophore; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Phosphoprotein; Photoreceptor protein; Receptor; Retinal protein;
KW Sensory transduction; Transducer; Transmembrane; Transmembrane helix;
KW Vision.
FT CHAIN 1..350
FT /note="Blue-sensitive opsin"
FT /id="PRO_0000197757"
FT TOPO_DOM 1..36
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 37..61
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 62..73
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 74..98
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 99..113
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 114..133
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 134..152
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 153..176
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 177..202
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..230
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 231..252
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 253..276
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 277..284
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 285..309
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 310..350
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 330..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 296
FT /note="N6-(retinylidene)lysine"
FT /evidence="ECO:0000250"
FT CARBOHYD 2
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 15
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 110..187
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 350 AA; 39478 MW; 3F7445C609900358 CRC64;
MNGTEGPNFY VPMSNATGVV RSPFEYPQYY LAEPWAFSIL AAYMFFLIIT GFPINFLTLY
VTIEHKKLRT PLNYILLNLA VADLFMVFGG FTTTMYTSMH GYFVFGETGC NLEGYFATLG
GEISLWSLVV LAIERWVVVC KPISNFRFGE NHAIMGLTLT WVMANACAMP PLFGWSRYIP
EGLQCSCGID YYTLKPEVNN ESFVIYMFLV HFTIPLTIIS FCYGRLVCAV KEAAAQQQES
ETTQRAEREV TRMVVIMVIS FLVCWIPYAS VAWYIFTHQG STFGPIFMTV PSFFAKSSSI
YNPMIYICMN KQFRNCMITT LFCGKNPFEG EEEGSTTKTE ASAVSSVSPA
