OPS1_MANSE
ID OPS1_MANSE Reviewed; 377 AA.
AC O02464;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1999, sequence version 2.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Opsin-1;
DE Short=MANOP1 {ECO:0000303|PubMed:9343857};
DE AltName: Full=Rhodopsin 1, long-wavelength {ECO:0000303|PubMed:9343857};
DE AltName: Full=Rhodopsin P520 {ECO:0000303|PubMed:12939366};
GN Name=OP1;
OS Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Sphingidae; Sphinginae; Sphingini; Manduca.
OX NCBI_TaxID=7130;
RN [1] {ECO:0000312|EMBL:AAD11964.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Retina {ECO:0000312|EMBL:AAD11964.1};
RX PubMed=9343857; DOI=10.1242/jeb.200.18.2469;
RA Chase M.R., Bennett R.R., White R.H.;
RT "Three opsin-encoding cDNAS from the compound eye of Manduca sexta.";
RL J. Exp. Biol. 200:2469-2478(1997).
RN [2] {ECO:0000305}
RP TISSUE SPECIFICITY.
RC TISSUE=Retina {ECO:0000269|PubMed:12939366};
RX PubMed=12939366; DOI=10.1242/jeb.00571;
RA White R.H., Xu H., Munch T.A., Bennett R.R., Grable E.A.;
RT "The retina of Manduca sexta: rhodopsin expression, the mosaic of green-,
RT blue- and UV-sensitive photoreceptors, and regional specialization.";
RL J. Exp. Biol. 206:3337-3348(2003).
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. May play a role in photoperiodic photoreception.
CC {ECO:0000250|UniProtKB:Q95YI3, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: In the retina, expression is abundant and uniform
CC in the anterior-posterior and oblique cells of the retinulae, with some
CC expression in the proximal cells. There is no expression in the dorsal
CC rim retinulae (at protein level). {ECO:0000269|PubMed:12939366}.
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; L78080; AAD11964.1; -; mRNA.
DR AlphaFoldDB; O02464; -.
DR SMR; O02464; -.
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 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; Photoreceptor protein; Receptor; Retinal protein;
KW Sensory transduction; Transducer; Transmembrane; Transmembrane helix;
KW Vision.
FT CHAIN 1..377
FT /note="Opsin-1"
FT /id="PRO_0000389622"
FT TOPO_DOM 1..58
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 59..79
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 80..92
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..113
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 114..129
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 130..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..190
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 191..220
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 221..241
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 242..280
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 281..301
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 302..312
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 313..335
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 336..377
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 357..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 377 AA; 41432 MW; 43B202E558105E74 CRC64;
MDPGPGLAAL QAWAAKSPAY GAANQTVVDK VPPDMMHMID PHWYQFPPMN PLWHALLGFT
IGVLGFVSIS GNGMVIYIFM STKSLKTPSN LLVVNLAFSD FLMMCAMSPA MVVNCYYETW
VWGPFACELY ACAGSLFGCA SIWTMTMIAF DRYNVIVKGI AAKPMTSNGA LLRILGIWVF
SLAWTLLPFF GWNRYVPEGN MTACGTDYLS KSWVSRSYIL IYSVFVYFLP LLLIIYSYFF
IVQAVAAHEK AMREQAKKMN VASLRSSEAA NTSAECKLAK VALMTISLWF MAWTPYLVIN
YTGVFESAPI SPLATIWGSL FAKANAVYNP IVYGISHPKY QAALYAKFPS LQCQSAPEDA
GSVASGTTAV SEEKPAA
