ID   OPSO_LIMPO              Reviewed;         376 AA.
AC   P35361;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Ocellar opsin;
OS   Limulus polyphemus (Atlantic horseshoe crab).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Merostomata;
OC   Xiphosura; Limulidae; Limulus.
OX   NCBI_TaxID=6850;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Median ocelli;
RX   PubMed=8327495; DOI=10.1073/pnas.90.13.6150;
RA   Smith W.C., Price D.A., Greenberg R.M., Battelle B.-A.;
RT   "Opsins from the lateral eyes and ocelli of the horseshoe crab, Limulus
RT   polyphemus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:6150-6154(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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Absorption:
CC         Abs(max)=530 nm;
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Ocellar cells; median ocelli.
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; L03792; AAA28274.1; -; mRNA.
DR   EMBL; L03782; AAA02499.1; -; mRNA.
DR   PIR; A48197; A48197.
DR   RefSeq; NP_001301089.1; NM_001314160.1.
DR   AlphaFoldDB; P35361; -.
DR   SMR; P35361; -.
DR   GeneID; 106470356; -.
DR   OrthoDB; 911005at2759; -.
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   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..376
FT                   /note="Ocellar opsin"
FT                   /id="PRO_0000197752"
FT   TOPO_DOM        1..46
FT                   /note="Extracellular"
FT   TRANSMEM        47..71
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        72..83
FT                   /note="Cytoplasmic"
FT   TRANSMEM        84..108
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        109..123
FT                   /note="Extracellular"
FT   TRANSMEM        124..143
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        144..162
FT                   /note="Cytoplasmic"
FT   TRANSMEM        163..186
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        187..210
FT                   /note="Extracellular"
FT   TRANSMEM        211..238
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        239..274
FT                   /note="Cytoplasmic"
FT   TRANSMEM        275..298
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        299..306
FT                   /note="Extracellular"
FT   TRANSMEM        307..331
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        332..376
FT                   /note="Cytoplasmic"
FT   REGION          349..376
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         318
FT                   /note="N6-(retinylidene)lysine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        17
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        193
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        120..197
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   376 AA;  42112 MW;  FA9647C40531CBF8 CRC64;
     MANQLSYSSL GWPYQPNASV VDTMPKEMLY MIHEHWYAFP PMNPLWYSIL GVAMIILGII
     CVLGNGMVIY LMMTTKSLRT PTNLLVVNLA FSDFCMMAFM MPTMASNCFA ETWILGPFMC
     EVYGMAGSLF GCASIWSMVM ITLDRYNVIV RGMAAAPLTH KKATLLLLFV WIWSGGWTIL
     PFFGWSRYVP EGNLTSCTVD YLTKDWSSAS YVIIYGLAVY FLPLITMIYC YFFIVHAVAE
     HEKQLREQAK KMNVASLRAN ADQQKQSAEC RLAKVAMMTV GLWFMAWTPY LIIAWAGVFS
     SGTRLTPLAT IWGSVFAKAN SCYNPIVYGI SHPRYKAALY QRFPSLACGS GESGSDVKSE
     ASATMTMEEK PKSPEA