OPSD_APIME
ID OPSD_APIME Reviewed; 377 AA.
AC Q17053;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Rhodopsin, long-wavelength;
DE AltName: Full=Opsin, green-sensitive;
OS Apis mellifera (Honeybee).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea; Apidae;
OC Apis.
OX NCBI_TaxID=7460;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8964502; DOI=10.1016/0378-1119(96)00165-5;
RA Chang B.S.W., Ayers D., Smith W.C., Pierce N.E.;
RT "Cloning of the gene encoding honeybee long-wavelength rhodopsin: a new
RT class of insect visual pigments.";
RL Gene 173:215-219(1996).
CC -!- FUNCTION: Visual pigments are the light-absorbing molecules that
CC mediate vision. They consist of an apoprotein, opsin, covalently linked
CC to 11-cis-retinal.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Absorption:
CC Abs(max)=526 nm;
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; U26026; AAA69069.1; -; mRNA.
DR PIR; JC4933; JC4933.
DR RefSeq; NP_001011639.2; NM_001011639.2.
DR AlphaFoldDB; Q17053; -.
DR SMR; Q17053; -.
DR STRING; 7460.GB50196-PA; -.
DR PaxDb; Q17053; -.
DR GeneID; 413961; -.
DR KEGG; ame:413961; -.
DR CTD; 100122456; -.
DR eggNOG; KOG3656; Eukaryota.
DR OrthoDB; 911005at2759; -.
DR Proteomes; UP000005203; Unplaced.
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 1: Evidence at protein level;
KW Chromophore; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Phosphoprotein; Photoreceptor protein; Receptor;
KW Reference proteome; Retinal protein; Sensory transduction; Transducer;
KW Transmembrane; Transmembrane helix; Vision.
FT CHAIN 1..377
FT /note="Rhodopsin, long-wavelength"
FT /id="PRO_0000197637"
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..377
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 357..377
FT /note="Disordered"
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 377 AA; 42016 MW; 31F944F9CE5869DB CRC64;
MIAVSGPSYE AFSYGGQARF NNQTVVDKVP PDMLHLIDAN WYQYPPLNPM WHGILGFVIG
MLGFVSAMGN GMVVYIFLST KSLRTPSNLF VINLAISNFL MMFCMSPPMV INCYYETWVL
GPLFCQIYAM LGSLFGCGSI WTMTMIAFDR YNVIVKGLSG KPLSINGALI RIIAIWLFSL
GWTIAPMFGW NRYVPEGNMT ACGTDYFNRG LLSASYLVCY GIWVYFVPLF LIIYSYWFII
QAVAAHEKNM REQAKKMNVA SLRSSENQNT SAECKLAKVA LMTISLWFMA WTPYLVINFS
GIFNLVKISP LFTIWGSLFA KANAVYNPIV YGISHPKYRA ALFAKFPSLA CAAEPSSDAV
STTSGTTTVT DNEKSNA
