OPSB_ORYLA
ID OPSB_ORYLA Reviewed; 352 AA.
AC P87365;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Blue-sensitive opsin;
DE AltName: Full=Blue cone photoreceptor pigment;
DE AltName: Full=KFH-B;
OS Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=8090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Retina;
RA Hisatomi O., Satoh T., Tokunaga F.;
RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; AB001602; BAA19419.1; -; mRNA.
DR RefSeq; NP_001098124.1; NM_001104654.1.
DR AlphaFoldDB; P87365; -.
DR SMR; P87365; -.
DR Ensembl; ENSORLT00000017628; ENSORLP00000017627; ENSORLG00000028370.
DR GeneID; 100049179; -.
DR KEGG; ola:100049179; -.
DR CTD; 100049179; -.
DR GeneTree; ENSGT01030000234549; -.
DR OrthoDB; 940057at2759; -.
DR Proteomes; UP000001038; Chromosome 5.
DR Proteomes; UP000265180; Unplaced.
DR Proteomes; UP000265200; Unplaced.
DR Bgee; ENSORLG00000028370; Expressed in gastrula and 10 other tissues.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0001750; C:photoreceptor outer segment; IBA:GO_Central.
DR GO; GO:0008020; F:G protein-coupled photoreceptor activity; IBA:GO_Central.
DR GO; GO:0071482; P:cellular response to light stimulus; IBA:GO_Central.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007602; P:phototransduction; IBA:GO_Central.
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;
KW Reference proteome; Retinal protein; Sensory transduction; Transducer;
KW Transmembrane; Transmembrane helix; Vision.
FT CHAIN 1..352
FT /note="Blue-sensitive opsin"
FT /id="PRO_0000197758"
FT TOPO_DOM 1..42
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 43..67
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 68..79
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..105
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 106..119
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 120..139
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 140..158
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..182
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 183..208
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 209..236
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 237..258
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 259..282
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 283..290
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 291..315
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 316..352
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 332..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 302
FT /note="N6-(retinylidene)lysine"
FT /evidence="ECO:0000250"
FT CARBOHYD 23
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 116..193
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 352 AA; 38906 MW; 68BC44A44F54057D CRC64;
MRGNRLVEFP DDFWIPIPLD TNNVTALSPF LVPQDHLGSP TIFYSMSALM FVLFVAGTAI
NLLTIACTLQ YKKLRSHLNY ILVNMAVANL IVASTGSSTC FVCFAFKYMV LGPLGCKIEG
FTAALGGMVS LWSLAVIAFE RWLVICKPLG NFVFKSEHAL LCCALTWVCG LCASVPPLVG
WSRYIPEGMQ CSCGPDWYTT GNKFNNESFV MFLFCFCFAV PFSIIVFCYS QLLFTLKMAA
KAQADSASTQ KAEKEVTRMV VVMVVAFLVC YVPYASFALW VINNRGQTFD LRLATIPSCV
SKASTVYNPV IYVLLNKQFR LCMKKMLGMS ADEDEESSTS QSTTEVSKVG PS
