OPSD_PROCL
ID OPSD_PROCL Reviewed; 376 AA.
AC P35356;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Rhodopsin;
GN Name=RHO;
OS Procambarus clarkii (Red swamp crayfish).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Astacidea;
OC Astacoidea; Cambaridae; Procambarus.
OX NCBI_TaxID=6728;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Retina;
RX PubMed=8422920; DOI=10.1016/0014-5793(93)81180-8;
RA Hariyama T., Ozaki K., Tokunaga F., Tsukahara Y.;
RT "Primary structure of crayfish visual pigment deduced from cDNA.";
RL FEBS Lett. 315:287-292(1993).
RN [2]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP INTERACTION WITH GNAQ.
RX PubMed=8365491; DOI=10.1016/0014-5793(93)80272-v;
RA Terakita A., Hariyama T., Tsukahara Y., Katsukura Y., Tashiro H.;
RT "Interaction of GTP-binding protein Gq with photoactivated rhodopsin in the
RT photoreceptor membranes of crayfish.";
RL FEBS Lett. 330:197-200(1993).
RN [3]
RP FUNCTION.
RX PubMed=8485084; DOI=10.1017/s0952523800003606;
RA Zeiger J., Goldsmith T.H.;
RT "Packaging of rhodopsin and porphyropsin in the compound eye of the
RT crayfish.";
RL Vis. Neurosci. 10:193-202(1993).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=8249320; DOI=10.1016/0042-6989(93)90120-l;
RA Terakita A., Tsukahara Y., Hariyama T., Seki T., Tashiro H.;
RT "Light-induced binding of proteins to rhabdomeric membranes in the retina
RT of crayfish (Procambarus clarkii).";
RL Vision Res. 33:2421-2426(1993).
CC -!- FUNCTION: Photoreceptor required for image-forming vision at low light
CC intensity (PubMed:8249320). Can use both retinal and 3-dehydroretinal
CC as visual pigment (PubMed:8485084). Light-induced isomerization of 11-
CC cis to all-trans retinal triggers a conformational change that
CC activates signaling via G-proteins (PubMed:8365491, PubMed:8249320).
CC Signaling via GNAQ probably mediates the activation of phospholipase C
CC (PubMed:8365491). {ECO:0000305|PubMed:8249320,
CC ECO:0000305|PubMed:8365491, ECO:0000305|PubMed:8485084}.
CC -!- SUBUNIT: Homodimer. Interacts with GNAQ. {ECO:0000269|PubMed:8365491}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:8365491}; Multi-pass
CC membrane protein {ECO:0000250|UniProtKB:P31356}. Note=Detected on the
CC rhabdomere membrane in the photoreceptor outer segment.
CC {ECO:0000269|PubMed:8249320}.
CC -!- TISSUE SPECIFICITY: Detected on rhabdomere membranes on photoreceptor
CC cells in the retina (at protein level). {ECO:0000269|PubMed:8249320}.
CC -!- PTM: Contains one covalently linked retinal chromophore.
CC {ECO:0000250|UniProtKB:P02699}.
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; S53494; AAB25036.1; -; mRNA.
DR PIR; S28853; S28853.
DR AlphaFoldDB; P35356; -.
DR SMR; P35356; -.
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; Retinal protein;
KW Sensory transduction; Transducer; Transmembrane; Transmembrane helix;
KW Vision.
FT CHAIN 1..376
FT /note="Rhodopsin"
FT /id="PRO_0000197743"
FT TOPO_DOM 1..52
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 53..77
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT TOPO_DOM 78..89
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 90..112
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT TOPO_DOM 113..126
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 127..149
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT TOPO_DOM 150..168
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 169..189
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT TOPO_DOM 190..216
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 217..237
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT TOPO_DOM 238..278
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 279..300
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT TOPO_DOM 301..311
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 312..333
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT TOPO_DOM 334..376
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 353..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 150..152
FT /note="'Ionic lock' involved in activated form
FT stabilization"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT COMPBIAS 354..376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 321
FT /note="N6-(retinylidene)lysine"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT CARBOHYD 23
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 199
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 126..203
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 376 AA; 42762 MW; A9F0BA71081A430D CRC64;
MSSWSNQPAM DDYGLPSSNP YGNFTVVDMA PKDILHMIHP HWYQYPPMNP MMYPLLLIFM
LFTGILCLAG NFVTIWVFMN TKSLRTPANL LVVNLAMSDF LMMFTMFPPM MVTCYYHTWT
LGPTFCQVYA FLGNLCGCAS IWTMVFITFD RYNVIVKGVA GEPLSTKKAS LWILTIWVLS
ITWCIAPFFG WNRYVPEGNL TGCGTDYLSE DILSRSYLYD YSTWVYYLPL LPIYCYVSII
KAVAAHEKGM RDQAKKMGIK SLRNEEAQKT SAECRLAKIA MTTVALWFIA WTPYLLINWV
GMFARSYLSP VYTIWGYVFA KANAVYNPIV YAISHPKYRA AMEKKLPCLS CKTESDDVSE
SASTTTSSAE EKAESA
