OPSD2_ANGAN
ID OPSD2_ANGAN Reviewed; 352 AA.
AC Q90215;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Rhodopsin, freshwater form;
OS Anguilla anguilla (European freshwater eel) (Muraena anguilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Anguilliformes; Anguillidae;
OC Anguilla.
OX NCBI_TaxID=7936;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Retina;
RX PubMed=8587887; DOI=10.1098/rspb.1995.0208;
RA Archer S.N., Hope A., Partridge J.C.;
RT "The molecular basis for the green-blue sensitivity shift in the rod visual
RT pigments of the European eel.";
RL Proc. R. Soc. B 262:289-295(1995).
CC -!- FUNCTION: Visual pigments such as rhodopsin and porphyropsin are light-
CC absorbing molecules that mediate vision. Rhodopsin consists of an
CC apoprotein, opsin, covalently linked to 11-cis-retinal. This receptor
CC is coupled to the activation of phospholipase C. Porphyropsin consists
CC of opsin covalently linked to 11-cis 3,4-didehydroretinal.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Absorption:
CC Abs(max)=~512 nm;
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Rod shaped photoreceptor cells which mediates
CC vision in dim light.
CC -!- DEVELOPMENTAL STAGE: When eel matures sexually and migrates back to
CC deep sea breeding grounds the visual pigments in its rod photoreceptors
CC change from being maximally sensitive to green light to being maximally
CC sensitive to blue light. In part, this change in sensitivity is due to
CC a change in the opsin component of the visual pigment molecule; this
CC green sensitive rhodopsin is expressed during life in greener inland
CC and coastal waters.
CC -!- PTM: Phosphorylated on some or all of the serine and threonine residues
CC present in the C-terminal region.
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; L78007; AAA99200.1; -; mRNA.
DR AlphaFoldDB; Q90215; -.
DR SMR; Q90215; -.
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; 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 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 Lipoprotein; Membrane; Palmitate; Phosphoprotein; Photoreceptor protein;
KW Receptor; Retinal protein; Sensory transduction; Transducer; Transmembrane;
KW Transmembrane helix; Vision.
FT CHAIN 1..352
FT /note="Rhodopsin, freshwater form"
FT /id="PRO_0000197647"
FT TOPO_DOM 1..36
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 37..61
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 62..73
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 74..98
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 99..113
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 114..133
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 134..152
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 153..176
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 177..202
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..230
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 231..252
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 253..276
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 277..284
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 285..309
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 310..352
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 330..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 296
FT /note="N6-(retinylidene)lysine"
FT /evidence="ECO:0000250"
FT LIPID 323
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 2
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 15
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 200
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; 39468 MW; 6E578919D6679DB4 CRC64;
MNGTEGPNFY VPMSNVTGVV RSPFEYPQYY LAEPWAYSAL AAYMFFLIIA GFPINFLTLY
VTIEHKKLRT PLNYILLNLA VADLFMVFGG FTTTMYTSMH GYFVFGPTGC NIEGFFATLG
GEIALWCLVV LAVERWMVVC KPMSNFRFGE NHAIMGVAFT WVMALACAAP PLFGWSRYIP
EGMQCSCGMD HYAPNPETYN ESFVIYMFIC HFTIPLTVIS FCYGRLVCTV KEATAQQQES
ETTQRAEREV TRMVIIMVIS FLVCWVPYAS VAWYIFTHQG SSFGPIFMTI PAFFAKSSSL
YNPLIYICMN KQSRNCMITT LCCGKNPFEE EEGASTTASK TEASSVSSVS PA
