OPSCE_BOMMO
ID OPSCE_BOMMO Reviewed; 381 AA.
AC Q95YI3;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Ceropsin;
DE AltName: Full=Cerebral opsin {ECO:0000303|PubMed:11549248};
DE Short=Boceropsin {ECO:0000312|EMBL:BAB63283.1};
GN Name=Bcop {ECO:0000312|EMBL:BAF73627.1};
OS Bombyx mori (Silk moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Bombycidae; Bombycinae; Bombyx.
OX NCBI_TaxID=7091;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAB63283.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Larval brain {ECO:0000269|PubMed:11549248};
RX PubMed=11549248; DOI=10.1006/bbrc.2001.5540;
RA Shimizu I., Yamakawa Y., Shimazaki Y., Iwasa T.;
RT "Molecular cloning of Bombyx cerebral opsin (Boceropsin) and cellular
RT localization of its expression in the silkworm brain.";
RL Biochem. Biophys. Res. Commun. 287:27-34(2001).
RN [2] {ECO:0000312|EMBL:BAF73627.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Atsumi T., Yasukochi Y., Fujiwara Y., Shiomi K.;
RT "Promoter analysis of Boceropsin gene of Bombyx mori.";
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
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:0000269|PubMed:11549248, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed bilaterally in dorsal and ventral
CC anterior protocerebral cells and bilaterally in the dorsal posterior
CC protocerebral and lateral posterior tritocerebral cells (at protein
CC level). Expressed in the larval brain but not in the subesophageal
CC ganglion or thoracic ganglion. {ECO:0000269|PubMed:11549248}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Opsin
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB064496; BAB63283.1; -; mRNA.
DR EMBL; AB184967; BAF73627.1; -; Genomic_DNA.
DR PIR; JC7760; JC7760.
DR RefSeq; NP_001036882.1; NM_001043417.1.
DR RefSeq; XP_012547741.1; XM_012692287.1.
DR AlphaFoldDB; Q95YI3; -.
DR SMR; Q95YI3; -.
DR STRING; 7091.BGIBMGA007787-TA; -.
DR GeneID; 692426; -.
DR KEGG; bmor:692426; -.
DR CTD; 45837; -.
DR eggNOG; KOG3656; Eukaryota.
DR HOGENOM; CLU_009579_3_0_1; -.
DR InParanoid; Q95YI3; -.
DR OrthoDB; 911005at2759; -.
DR Proteomes; UP000005204; Unassembled WGS sequence.
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; Reference proteome;
KW Retinal protein; Sensory transduction; Transducer; Transmembrane;
KW Transmembrane helix; Vision.
FT CHAIN 1..381
FT /note="Ceropsin"
FT /id="PRO_0000389423"
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..96
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..117
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 118..133
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 134..154
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 155..173
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..194
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 195..221
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..242
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 243..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..316
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 317..339
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 340..381
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 131..208
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 381 AA; 42241 MW; 623849C899158FF8 CRC64;
MSISMDAGPG FAALQSWSSQ VAAFGNSNQT VVDRVSPEML HLIDAYWYQF PPMNPLWHAL
LGFTIGVLGF ISMMGNGMVI YIFMTTKNLK TPSNLLVVNL AFSDFLMMCA MSPAMVINCY
NETWVFGPFA CELYGCAGSL FGCASIWTMT MIAFDRYNVI VKGIAAKPMT NNGALLRILG
IWAFSLAWTV APFFGWNRYV PEGNMTACGT DYLTKDWFSR SYIVVYSVFV YFAPLLLIVY
SYYYIVQAVS AHEKAMREQA KKMNVASLRS SEAANTSTEC KLAKVALMTI SLWFMAWTPY
LVINYTGILE SAPISPLATI WGSLFAKANA VYNPIVYGIS HPKYQAALYK RFPVLQCHST
TTDEASSVAS GTTVMEEKPT A
