ID   OPS1_SCHGR              Reviewed;         381 AA.
AC   Q94741;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Opsin-1;
GN   Name=Lo1;
OS   Schistocerca gregaria (Desert locust) (Gryllus gregarius).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Polyneoptera; Orthoptera; Caelifera; Acrididea; Acridomorpha;
OC   Acridoidea; Acrididae; Cyrtacanthacridinae; Schistocerca.
OX   NCBI_TaxID=7010;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9156194; DOI=10.1016/s0042-6989(96)00198-8;
RA   Towner P., Harris P., Wolstenholme A.J., Hill C., Worm K., Gartner W.;
RT   "Primary structure of locust opsins: a speculative model which may account
RT   for ultraviolet wavelength light detection.";
RL   Vision Res. 37:495-503(1997).
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   -!- 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; X80071; CAA56377.1; -; mRNA.
DR   AlphaFoldDB; Q94741; -.
DR   SMR; Q94741; -.
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; IPR001391; Opsin_lateye.
DR   InterPro; IPR027430; Retinal_BS.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00238; OPSIN.
DR   PRINTS; PR00578; OPSINLTRLEYE.
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   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..381
FT                   /note="Opsin-1"
FT                   /id="PRO_0000197635"
FT   TOPO_DOM        1..53
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        54..78
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        79..90
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        91..115
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        116..130
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        131..150
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        151..169
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        170..193
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        194..217
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        218..245
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        246..280
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        281..304
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        305..311
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        312..336
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        337..381
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          354..381
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         323
FT                   /note="N6-(retinylidene)lysine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        24
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        127..204
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   381 AA;  42399 MW;  50D38FF9038D5BA3 CRC64;
     MASASLISEP SFSAYWGGSG GFANQTVVDK VPPEMLYLVD PHWYQFPPMN PLWHGLLGFV
     IGVLGVISVI GNGMVIYIFS TTKSLRTPSN LLVVNLAFSD FLMMFTMSAP MGINCYYETW
     VLGPFMCELY ALFGSLFGCG SIWTMTMIAL DRYNVIVKGL SAKPMTNKTA MLRILFIWAF
     SVAWTIMPLF GWNRYVPEGN MTACGTDYLT KDWVSRSYIL VYSFFVYLLP LGTIIYSYFF
     ILQAVSAHEK QMREQRKKMN VASLRSAEAS QTSAECKLAK VALMTISLWF FGWTPYLIIN
     FTGIFETMKI SPLLTIWGSL FAKANAVFNP IVYGISHPKY RAALEKKFPS LACASSSDDN
     TSVASGATTV SDEKSEKSAS A