ID   OPS2_SCHGR              Reviewed;         380 AA.
AC   Q26495;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Opsin-2;
GN   Name=Lo2;
OS   Schistocerca gregaria (Desert locust) (Gryllus gregarius).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Polyneoptera; Orthoptera; Caelifera; Acrididea; Acridomorpha;
OC   Acridoidea; Acrididae; Cyrtacanthacridinae; Schistocerca.
OX   NCBI_TaxID=7010;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9156194; DOI=10.1016/s0042-6989(96)00198-8;
RA   Towner P., Harris P., Wolstenholme A.J., Hill C., Worm K., Gartner W.;
RT   "Primary structure of locust opsins: a speculative model which may account
RT   for ultraviolet wavelength light detection.";
RL   Vision Res. 37:495-503(1997).
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; X80072; CAA56378.1; -; mRNA.
DR   AlphaFoldDB; Q26495; -.
DR   SMR; Q26495; -.
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   InterPro; IPR027430; Retinal_BS.
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.
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..380
FT                   /note="Opsin-2"
FT                   /id="PRO_0000197636"
FT   TOPO_DOM        1..51
FT                   /note="Extracellular"
FT   TRANSMEM        52..76
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        77..88
FT                   /note="Cytoplasmic"
FT   TRANSMEM        89..115
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        116..128
FT                   /note="Extracellular"
FT   TRANSMEM        129..148
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        149..166
FT                   /note="Cytoplasmic"
FT   TRANSMEM        167..191
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        192..215
FT                   /note="Extracellular"
FT   TRANSMEM        216..243
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        244..279
FT                   /note="Cytoplasmic"
FT   TRANSMEM        280..303
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        304..311
FT                   /note="Extracellular"
FT   TRANSMEM        312..336
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        337..380
FT                   /note="Cytoplasmic"
FT   REGION          358..380
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        360..380
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        3
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        125..202
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   380 AA;  42531 MW;  113504F71027C07A CRC64;
     MVNTTDFYPV PAAMAYESSV GLPLLGWNVP TEHLDLVHPH WRSFQVPNKY WHFGLAFVYF
     MLMCMSSLGN GIVLWIYATT KSIRTPSNMF IVNLALFDVL MLLEMPMLVV SSLFYQRPVG
     WELGCDIYAA LGSVAGIGSA INNAAIAFDR YRTISCPIDG RLTQGQVLAL IAGTWVWTLP
     FTLMPLLRIW SRFTAEGFLT TCSFDYLTDD EDTKVFVGCI FAWSYAFPLC LICCFYYRLI
     GAVREHEKML RDQAKKMNVK SLQSNADTEA QSAEIRIAKV ALTIFFLFLC SWTPYAVVAM
     IGAFGNRAAL TPLSTMIPAV TAKIVSCIDP WVYAINHPRF RAEVQKRMKW LHLGEDARSS
     KSDTSSTATD RTVGNVSASA