ID   OPSD_CATBO              Reviewed;         378 AA.
AC   Q17296;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Rhodopsin;
OS   Cataglyphis bombycinus (Saharan silver ant) (Formica bombycina).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Formicinae; Cataglyphis.
OX   NCBI_TaxID=72790;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Retina;
RX   PubMed=9372150; DOI=10.1007/bf02211912;
RA   Popp M.P., Grisshammer R., Hargrave P.A., Smith W.C.;
RT   "Ant opsins: sequences from the Saharan silver ant and the carpenter ant.";
RL   Invertebr. Neurosci. 1:323-329(1996).
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. {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; U32501; AAC47084.1; -; mRNA.
DR   AlphaFoldDB; Q17296; -.
DR   SMR; Q17296; -.
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   2: Evidence at transcript level;
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..378
FT                   /note="Rhodopsin"
FT                   /id="PRO_0000197641"
FT   TOPO_DOM        1..53
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        54..78
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        79..90
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        91..115
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        116..130
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        131..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..193
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        194..217
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        218..245
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        246..280
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        281..304
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        305..311
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        312..336
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        337..378
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          356..378
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        357..378
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         323
FT                   /note="N6-(retinylidene)lysine"
FT                   /evidence="ECO:0000250"
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   378 AA;  41905 MW;  03D20AE9E1DA5E47 CRC64;
     MMSIASGPSH AAYTWTAQGG GFGNQTVVDK VPPEMLHLVD AHWYQFPPMN PLWHAILGFV
     IGILGMISVI GNGMVIYIFT TTKSLRTPSN LLVINLAISD FLMMLSMSPA MVINCYYETW
     VLGPLVCELY GLTGSLFGCG SIWTMTMIAF DRYNVIVKGL SAKPMTINGA LLRILGIWFF
     SLGWTIAPMF GWNRYVPEGN MTACGTDYLT KDLLSRSYIL VYSFFCYFLP LFLIIYSYFF
     IIQAVAAHEK NMREQAKKMN VASLRSAENQ STSAECKLAK VALMTISLWF MAWTPYLVIN
     YAGIFETVKI NPLFTIWGSL FAKANAVYNP IVYGISHPKY RAALFQRFPS LACSSGPAGA
     DTLSTTTTVT EGTEKPAA