ID   OPSC2_HEMSA             Reviewed;         377 AA.
AC   Q25158;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Compound eye opsin BCRH2;
OS   Hemigrapsus sanguineus (Asian shore crab).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC   Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Brachyura;
OC   Eubrachyura; Grapsoidea; Varunidae; Hemigrapsus.
OX   NCBI_TaxID=40176;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Eye;
RX   PubMed=9318091; DOI=10.1242/jeb.199.2.441;
RA   Sakamoto K., Hisatomi O., Tokunaga F., Eguchi E.;
RT   "Two opsins from the compound eye of the crab Hemigrapsus sanguineus.";
RL   J. Exp. Biol. 199:441-450(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. This opsin produces visual pigments with maximal
CC       absorption in the blue-green region of the spectrum.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Expressed in all of the seven retinular cells (R1-
CC       R7) forming the main rhabdom in each ommatidium.
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; D50584; BAA09133.1; -; mRNA.
DR   AlphaFoldDB; Q25158; -.
DR   SMR; Q25158; -.
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; IPR000856; Opsin_RH3/RH4.
DR   InterPro; IPR027430; Retinal_BS.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00238; OPSIN.
DR   PRINTS; PR00577; OPSINRH3RH4.
DR   SMART; SM01381; 7TM_GPCR_Srsx; 1.
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..377
FT                   /note="Compound eye opsin BCRH2"
FT                   /id="PRO_0000197750"
FT   TOPO_DOM        1..53
FT                   /note="Extracellular"
FT   TRANSMEM        54..78
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        79..90
FT                   /note="Cytoplasmic"
FT   TRANSMEM        91..115
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        116..131
FT                   /note="Extracellular"
FT   TRANSMEM        132..151
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        152..170
FT                   /note="Cytoplasmic"
FT   TRANSMEM        171..194
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        195..218
FT                   /note="Extracellular"
FT   TRANSMEM        219..246
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        247..281
FT                   /note="Cytoplasmic"
FT   TRANSMEM        282..305
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        306..313
FT                   /note="Extracellular"
FT   TRANSMEM        314..338
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        339..377
FT                   /note="Cytoplasmic"
FT   MOD_RES         325
FT                   /note="N6-(retinylidene)lysine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        3
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        128..205
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   377 AA;  42114 MW;  FD6CC2E0E199A256 CRC64;
     MTNATGPQMA YYGAASMDFG YPEGVSIVDF VRPEIKPYVH QHWYNYPPVN PMWHYLLGVI
     YLFLGTVSIF GNGLVIYLFN KSAALRTPAN ILVVNLALSD LIMLTTNVPF FTYNCFSGGV
     WMFSPQYCEI YACLGAITGV CSIWLLCMIS FDRYNIICNG FNGPKLTTGK AVVFALISWV
     IAIGCALPPF FGWGNYILEG ILDSCSYDYL TQDFNTFSYN IFIFVFDYFL PAAIIVFSYV
     FIVKAIFAHE AAMRAQAKKM NVSTLRSNEA DAQRAEIRIA KTALVNVSLW FICWTPYALI
     SLKGVMGDTS GITPLVSTLP ALLAKSCSCY NPFVYAISHP KYRLAITQHL PWFCVHETET
     KSNDDSQSNS TVAQDKA