ID   OPS1_CALVI              Reviewed;         371 AA.
AC   P22269;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Opsin Rh1;
DE   AltName: Full=Outer R1-R6 photoreceptor cells opsin;
GN   Name=NINAE; Synonyms=RH1;
OS   Calliphora vicina (Blue blowfly) (Calliphora erythrocephala).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Oestroidea;
OC   Calliphoridae; Calliphorinae; Calliphora.
OX   NCBI_TaxID=7373;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1698782; DOI=10.1016/s0021-9258(18)38249-8;
RA   Huber A., Smith D.P., Zuker C.S., Paulsen R.;
RT   "Opsin of Calliphora peripheral photoreceptors R1-6. Homology with
RT   Drosophila Rh1 and posttranslational processing.";
RL   J. Biol. Chem. 265:17906-17910(1990).
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)=480 nm;
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.
CC   -!- MISCELLANEOUS: Each eye is composed of 800 facets or ommatidia. Each
CC       ommatidium contains 8 photoreceptor cells (R1-R8), the R1 to R6 cells
CC       are outer cells, while R7 and R8 are inner cells.
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; M58334; AAA62725.1; -; mRNA.
DR   PIR; A39234; A39234.
DR   AlphaFoldDB; P22269; -.
DR   SMR; P22269; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008020; F:G protein-coupled photoreceptor activity; IEA:UniProt.
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; IPR001735; Opsin_RH1/RH2.
DR   InterPro; IPR027430; Retinal_BS.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00238; OPSIN.
DR   PRINTS; PR00576; OPSINRH1RH2.
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..371
FT                   /note="Opsin Rh1"
FT                   /id="PRO_0000197624"
FT   TOPO_DOM        1..47
FT                   /note="Extracellular"
FT   TRANSMEM        48..72
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        73..84
FT                   /note="Cytoplasmic"
FT   TRANSMEM        85..110
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        111..124
FT                   /note="Extracellular"
FT   TRANSMEM        125..144
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        145..163
FT                   /note="Cytoplasmic"
FT   TRANSMEM        164..187
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        188..211
FT                   /note="Extracellular"
FT   TRANSMEM        212..239
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        240..274
FT                   /note="Cytoplasmic"
FT   TRANSMEM        275..298
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        299..305
FT                   /note="Extracellular"
FT   TRANSMEM        306..330
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        331..371
FT                   /note="Cytoplasmic"
FT   MOD_RES         317
FT                   /note="N6-(retinylidene)lysine"
FT   CARBOHYD        18
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000305"
FT   DISULFID        121..198
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   371 AA;  41289 MW;  163C685E991B6D99 CRC64;
     MERYSTPLIG PSFAALTNGS VTDKVTPDMA HLVHPYWNQF PAMEPKWAKF LAAYMVLIAT
     ISWCGNGVVI YIFSTTKSLR TPANLLVINL AISDFGIMIT NTPMMGINLF YETWVLGPLM
     CDIYGGLGSA FGCSSILSMC MISLDRYNVI VKGMAGQPMT IKLAIMKIAL IWFMASIWTL
     APVFGWSRYV PEGNLTSCGI DYLERDWNPR SYLIFYSIFV YYLPLFLICY SYWFIIAAVS
     AHEKAMREQA KKMNVKSLRS SEDADKSAEG KLAKVALVTI SLWFMAWTPY TIINTLGLFK
     YEGLTPLNTI WGACFAKSAA CYNPIVYGIS HPKYGIALKE KCPCCVFGKV DDGKASDATS
     QATNNESETK A