OPS4_DROVI
ID OPS4_DROVI Reviewed; 383 AA.
AC P17646;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 2.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Opsin Rh4;
DE AltName: Full=Inner R7 photoreceptor cells opsin;
GN Name=Rh4;
OS Drosophila virilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7244;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1946441; DOI=10.1073/pnas.88.22.10203;
RA Neufeld T.P., Carthew R.W., Rubin G.M.;
RT "Evolution of gene position: chromosomal arrangement and sequence
RT comparison of the Drosophila melanogaster and Drosophila virilis sina and
RT Rh4 genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:10203-10207(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29.
RX PubMed=2140105; DOI=10.1101/gad.4.3.444;
RA Fortini M.E., Rubin G.M.;
RT "Analysis of cis-acting requirements of the Rh3 and Rh4 genes reveals a
RT bipartite organization to rhodopsin promoters in Drosophila melanogaster.";
RL Genes Dev. 4:444-463(1990).
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.
CC -!- MISCELLANEOUS: Each Drosophila eye is composed of 800 facets or
CC ommatidia. Each ommatidium contains 8 photoreceptor cells (R1-R8), the
CC R1 to R6 cells are outer cells, while R7 and R8 are inner cells.
CC -!- MISCELLANEOUS: Opsin Rh4 is sensitive to UV light.
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; M77281; AAA28855.1; -; Genomic_DNA.
DR EMBL; X51351; CAA35743.1; -; Genomic_DNA.
DR PIR; B41544; B41544.
DR AlphaFoldDB; P17646; -.
DR SMR; P17646; -.
DR STRING; 7244.FBpp0225756; -.
DR eggNOG; KOG3656; Eukaryota.
DR ChiTaRS; Rh4; fly.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008020; F:G protein-coupled photoreceptor activity; IEA:UniProt.
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 InterPro; IPR027430; Retinal_BS.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00577; OPSINRH3RH4.
DR SMART; SM01381; 7TM_GPCR_Srsx; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR PROSITE; PS00238; OPSIN; 1.
PE 3: Inferred from homology;
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..383
FT /note="Opsin Rh4"
FT /id="PRO_0000197632"
FT TOPO_DOM 1..57
FT /note="Extracellular"
FT TRANSMEM 58..82
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 83..94
FT /note="Cytoplasmic"
FT TRANSMEM 95..117
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 118..133
FT /note="Extracellular"
FT TRANSMEM 134..153
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 154..171
FT /note="Cytoplasmic"
FT TRANSMEM 172..196
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 197..220
FT /note="Extracellular"
FT TRANSMEM 221..248
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 249..284
FT /note="Cytoplasmic"
FT TRANSMEM 285..308
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 309..316
FT /note="Extracellular"
FT TRANSMEM 317..341
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 342..383
FT /note="Cytoplasmic"
FT REGION 361..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..383
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 328
FT /note="N6-(retinylidene)lysine"
FT /evidence="ECO:0000250"
FT CARBOHYD 9
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT DISULFID 130..207
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 383 AA; 42846 MW; 3D8F4833946E4956 CRC64;
MDIAGSLCNA SEGPVLRPEA RVSGNGDLQF LGWNVPPDQI QHIPEHWLTQ LEPPASMHYM
LGVFYIFLFC ASTVGNGMVI WIFSTSKALR TPSNMFVLNL AVFDFIMCLK APIFIYNSFH
RGFALGNTGC QIFAAIGSYS GIGAGMTNAA IGYDRLNVIT KPMNRNMTFT KAIIMNVIIW
LYCTPWVVLP LTQFWDRFVP EGYLTSCTFD YLTDNFDTRL FVGTIFFFSF VCPTLMIIYY
YSQIVGHVFS HEKALREQAK KMNVESLRSN VDKSKDTAEI RIAKAAITIC FLFFVSWTPY
GVMSLIGAFG DKSLLTPGAT MIPACTCKLV ACIDPFVYAI SHPRYRMELQ KRCPWLAIDE
KAPESSSAAS TTTTQEQQQT TAA
