ID   OPS3_MANSE              Reviewed;         384 AA.
AC   O96107;
DT   15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Opsin-3;
DE            Short=MANOP3 {ECO:0000303|PubMed:9343857};
DE   AltName: Full=Rhodopsin 3, short-wavelength {ECO:0000303|PubMed:9343857};
DE   AltName: Full=Rhodopsin P450 {ECO:0000303|PubMed:12939366};
GN   Name=OP3;
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:AAD11966.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Retina {ECO:0000312|EMBL:AAD11966.1};
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 essentially uniformly
CC       distributed but a higher level is seen in the ventral region where the
CC       B-cells are localized. {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; AD001674; AAD11966.1; -; mRNA.
DR   AlphaFoldDB; O96107; -.
DR   SMR; O96107; -.
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; IPR000856; Opsin_RH3/RH4.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00577; OPSINRH3RH4.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   2: Evidence at transcript 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..384
FT                   /note="Opsin-3"
FT                   /id="PRO_0000389624"
FT   TOPO_DOM        1..62
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        63..83
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        84..94
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        95..115
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        116..132
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        133..153
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        154..171
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        172..192
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        193..219
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        220..240
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        241..284
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        285..305
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        306..312
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        313..333
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        334..384
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        4
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        130..207
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   384 AA;  43543 MW;  787C477C539E2A02 CRC64;
     MATNFTQELY EIGPMAYPLK MISKDVAEHM LGWNIPEEHQ DLVHDHWRNF PAVSKYWHYV
     LALIYTMLMV TSLTGNGIVI WIFSTSKSLR SASNMFVINL AVFDLMMMLE MPLLIMNSFY
     QRLVGYQLGC DVYAVLGSLS GIGGAITNAV IAFDRYKTIS SPLDGRINTV QAGLLIAFTW
     FWALPFTILP AFRIWGRFVP EGFLTTCSFD YFTEDQDTEV FVACIFVWSY CIPMALICYF
     YSQLFGAVRL HERMLQEQAK KMNVKSLASN KEDNSRSVEI RIAKVAFTIF FLFICAWTPY
     AFVTMTGAFG DRTLLTPIAT MIPAVCCKVV SCIDPWVYAI NHPRYRAELQ KRLPWMGVRE
     QDPDAVSTTT SVATAGFQPP AAEA