OPSD_ANOCA
ID OPSD_ANOCA Reviewed; 352 AA.
AC P41591;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Rhodopsin;
GN Name=RHO;
OS Anolis carolinensis (Green anole) (American chameleon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Iguania; Dactyloidae; Anolis.
OX NCBI_TaxID=28377;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7959000; DOI=10.1016/0378-1119(94)90159-7;
RA Kawamura S., Yokoyama S.;
RT "Cloning of the rhodopsin-encoding gene from the rod-less lizard Anolis
RT carolinensis.";
RL Gene 149:267-270(1994).
CC -!- FUNCTION: Photoreceptor. Light-induced isomerization of 11-cis to all-
CC trans retinal triggers a conformational change that activates signaling
CC via G-proteins. {ECO:0000250|UniProtKB:P02699}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P08100}; Multi-
CC pass membrane protein {ECO:0000250|UniProtKB:P08100}.
CC -!- TISSUE SPECIFICITY: Pineal gland. Instead of the rod where rhodopsin is
CC generally located. {ECO:0000303|PubMed:7959000}.
CC -!- PTM: Contains one covalently linked retinal chromophore. Upon light
CC absorption, the covalently bound 11-cis-retinal is converted to all-
CC trans-retinal. After hydrolysis of the Schiff base and release of the
CC covalently bound all-trans-retinal, active rhodopsin is regenerated by
CC binding of a fresh molecule of 11-cis-retinal.
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; L31503; AAA62614.1; -; Genomic_DNA.
DR PIR; I50081; I50081.
DR AlphaFoldDB; P41591; -.
DR SMR; P41591; -.
DR STRING; 28377.ENSACAP00000014023; -.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; P41591; -.
DR Proteomes; UP000001646; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0097381; C:photoreceptor disc membrane; ISS:UniProtKB.
DR GO; GO:0001750; C:photoreceptor outer segment; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005502; F:11-cis retinal binding; ISS:UniProtKB.
DR GO; GO:0008020; F:G protein-coupled photoreceptor activity; ISS:UniProtKB.
DR GO; GO:0016038; P:absorption of visible light; ISS:UniProtKB.
DR GO; GO:0071482; P:cellular response to light stimulus; IBA:GO_Central.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007602; P:phototransduction; IBA:GO_Central.
DR GO; GO:0016056; P:rhodopsin mediated signaling pathway; ISS:UniProtKB.
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; IPR027430; Retinal_BS.
DR InterPro; IPR000732; Rhodopsin.
DR InterPro; IPR019477; Rhodopsin_N.
DR Pfam; PF00001; 7tm_1; 1.
DR Pfam; PF10413; Rhodopsin_N; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00238; OPSIN.
DR PRINTS; PR00579; RHODOPSIN.
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 3: Inferred from homology;
KW Chromophore; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Lipoprotein; Membrane; Palmitate; Phosphoprotein; Photoreceptor protein;
KW Receptor; Reference proteome; Retinal protein; Sensory transduction;
KW Transducer; Transmembrane; Transmembrane helix; Vision.
FT CHAIN 1..352
FT /note="Rhodopsin"
FT /id="PRO_0000197648"
FT TOPO_DOM 1..36
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 37..61
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT TOPO_DOM 62..73
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 74..96
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT TOPO_DOM 97..110
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 111..133
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT TOPO_DOM 134..152
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 153..173
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT TOPO_DOM 174..202
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 203..224
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT TOPO_DOM 225..252
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 253..274
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT TOPO_DOM 275..286
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 287..308
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT TOPO_DOM 309..352
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 332..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 134..136
FT /note="'Ionic lock' involved in activated form
FT stabilization"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT SITE 113
FT /note="Plays an important role in the conformation switch
FT to the active conformation"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT MOD_RES 296
FT /note="N6-(retinylidene)lysine"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT LIPID 322
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT LIPID 323
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT CARBOHYD 2
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 15
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 110..187
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 352 AA; 39350 MW; D80365535CCE159B CRC64;
MNGTEGQNFY VPMSNKTGVV RNPFEYPQYY LADPWQFSAL AAYMFLLILL GFPINFLTLF
VTIQHKKLRT PLNYILLNLA VANLFMVLMG FTTTMYTSMN GYFIFGTVGC NIEGFFATLG
GEMGLWSLVV LAVERYVVIC KPMSNFRFGE THALIGVSCT WIMALACAGP PLLGWSRYIP
EGMQCSCGVD YYTPTPEVHN ESFVIYMFLV HFVTPLTIIF FCYGRLVCTV KAAAAQQQES
ATTQKAEREV TRMVVIMVIS FLVCWVPYAS VAFYIFTHQG SDFGPVFMTI PAFFAKSSAI
YNPVIYILMN KQFRNCMIMT LCCGKNPLGD EETSAGTKTE TSTVSTSQVS PA
