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 27-MAR-2024, entry version 88.
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 EnsemblMetazoa; NM_001314160.1; NP_001301089.1; LOC106470356.
DR GeneID; 106470356; -.
DR KEGG; lpol:106470356; -.
DR OrthoDB; 3432893at2759; -.
DR Proteomes; UP000694941; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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 CDD; cd15079; 7tmA_photoreceptors_insect; 1.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
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 PANTHER; PTHR24240; OPSIN; 1.
DR PANTHER; PTHR24240:SF85; OPSIN RH1-RELATED; 1.
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 SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 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
//
