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OPSD_SPHSP
ID   OPSD_SPHSP              Reviewed;         376 AA.
AC   P35362;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Rhodopsin;
DE            Short=Opsin;
OS   Sphodromantis sp. (Mantis).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Polyneoptera; Dictyoptera; Mantodea; Eumantodea; Mantoidea;
OC   Mantidae; Mantinae; Paramantini; Sphodromantis; unclassified Sphodromantis.
OX   NCBI_TaxID=27433;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8206378; DOI=10.1016/0378-1119(94)90101-5;
RA   Towner P., Gaertner W.;
RT   "The primary structure of mantid opsin.";
RL   Gene 143:227-231(1994).
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; X71665; CAA50658.1; -; mRNA.
DR   PIR; S34335; S34335.
DR   AlphaFoldDB; P35362; -.
DR   SMR; P35362; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
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   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..376
FT                   /note="Rhodopsin"
FT                   /id="PRO_0000197642"
FT   TOPO_DOM        1..51
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        52..76
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        77..88
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        89..113
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        114..128
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        129..148
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        149..167
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        168..191
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        192..215
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        216..243
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        244..278
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        279..302
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        303..309
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        310..334
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        335..376
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          353..376
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        354..376
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         321
FT                   /note="N6-(retinylidene)lysine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        22
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        198
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        125..202
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   376 AA;  41883 MW;  4D0A271CC1F7B82B CRC64;
     MSLINEPSYS AYSWGGQGGY GNQTVVDKVL PEMLHLIDPH WYQFPPMNPL WHGLLGFVIG
     CLGFVSVVGN GMVIYIFSTT KGLRTPSNLL VVNLAFSDFL MMLSMSPPMV INCYYETWVL
     GPFMCELYAL LGSLFGCGSI WTMVMIALDR YNVIVKGLAA KPMTNKTAML RILGIWAMSI
     AWTVFPLFGW NRYVPEGNMT ACGTDYLNKE WVSRSYILVY SVFVYFLPLA TIIYSYWFIV
     QAVSAHEKQM REQAKKMNVA SLRSAENANT SAECKLAKVA LMTISLWFFA WTPYLVTDFS
     GIFEWGKISP LATIWCSLFA KANAVYNPIV YGISHPKYRA ALNKKFPSLA CASEPDDTAS
     QASGATTVSD EKSASA
 
 
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