OPSB_ASTFA
ID OPSB_ASTFA Reviewed; 355 AA.
AC P51472;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Blue-sensitive opsin;
DE AltName: Full=Blue cone photoreceptor pigment;
GN Name=B23;
OS Astyanax fasciatus (Blind cave fish) (Astyanax mexicanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Characidae; Psalidodon.
OX NCBI_TaxID=223369;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Eye;
RX PubMed=8224220; DOI=10.1016/0014-5793(93)81673-n;
RA Yokoyama R., Yokoyama S.;
RT "Molecular characterization of a blue visual pigment gene in the fish
RT Astyanax fasciatus.";
RL FEBS Lett. 334:27-31(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 -!- 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. {ECO:0000250}.
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; AF134766; AAB28911.1; -; Genomic_DNA.
DR EMBL; AF134762; AAB28911.1; JOINED; Genomic_DNA.
DR EMBL; AF134763; AAB28911.1; JOINED; Genomic_DNA.
DR EMBL; AF134764; AAB28911.1; JOINED; Genomic_DNA.
DR EMBL; AF134765; AAB28911.1; JOINED; Genomic_DNA.
DR PIR; S39028; S39028.
DR AlphaFoldDB; P51472; -.
DR SMR; P51472; -.
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; 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 2: Evidence at transcript 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..355
FT /note="Blue-sensitive opsin"
FT /id="PRO_0000197754"
FT TOPO_DOM 1..41
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..66
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 67..78
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 79..104
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 105..118
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..138
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 139..157
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..181
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 182..207
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 208..235
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 236..257
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..281
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 282..289
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 290..314
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 315..355
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 334..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 301
FT /note="N6-(retinylidene)lysine"
FT /evidence="ECO:0000250"
FT CARBOHYD 22
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 115..192
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 355 AA; 39690 MW; 4179B41F7FEA1843 CRC64;
MKSRPQEFQE DFYIPIPLDT NNITALSPFL VPQDHLGGSG IFMIMTVFML FLFIGGTSIN
VLTIVCTVQY KKLRSHLNYI LVNLAISNLL VSTVGSFTAF VSFLNRYFIF GPTACKIEGF
VATLGGMVSL WSLSVVAFER WLVICKPVGN FSFKGTHAII GCALTWFFAL LASTPPLFGW
SRYIPEGLQC SCGPDWYTTE NKYNNESYVM FLFCFCFGFP FTVILFCYGQ LLFTLKSAAK
AQADSASTQK AEREVTKMVV VMVMGFLVCW LPYASFALWV VFNRGQSFDL RLGTIPSCFS
KASTVYNPVI YVFMNKQFRS CMMKLIFCGK SPFGDDEEAS SSSQVTQVSS VGPEK