OPSO_SALSA
ID OPSO_SALSA Reviewed; 323 AA.
AC O13018;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Vertebrate ancient opsin;
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Eye;
RX PubMed=9136902; DOI=10.1016/s0014-5793(97)00287-1;
RA Soni B.G., Foster R.G.;
RT "A novel and ancient vertebrate opsin.";
RL FEBS Lett. 406:279-283(1997).
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; AF001499; AAC60124.1; -; mRNA.
DR RefSeq; NP_001117098.1; NM_001123626.1.
DR AlphaFoldDB; O13018; -.
DR SMR; O13018; -.
DR GeneID; 100136521; -.
DR KEGG; sasa:100136521; -.
DR Proteomes; UP000087266; Chromosome ssa18.
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; IDA:AgBase.
DR GO; GO:0007603; P:phototransduction, visible light; IDA:AgBase.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR027430; Retinal_BS.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR PROSITE; PS00238; OPSIN; 2.
PE 1: Evidence at protein level;
KW Chromophore; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Phosphoprotein; Photoreceptor protein; Receptor;
KW Reference proteome; Retinal protein; Sensory transduction; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..323
FT /note="Vertebrate ancient opsin"
FT /id="PRO_0000197811"
FT TOPO_DOM 1..38
FT /note="Extracellular"
FT TRANSMEM 39..63
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 64..75
FT /note="Cytoplasmic"
FT TRANSMEM 76..100
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 101..115
FT /note="Extracellular"
FT TRANSMEM 116..135
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 136..154
FT /note="Cytoplasmic"
FT TRANSMEM 155..178
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 179..202
FT /note="Extracellular"
FT TRANSMEM 203..230
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 231..250
FT /note="Cytoplasmic"
FT TRANSMEM 251..274
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 275..282
FT /note="Extracellular"
FT TRANSMEM 283..307
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 308..323
FT /note="Cytoplasmic"
FT MOD_RES 294
FT /note="N6-(retinylidene)lysine"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 112..189
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 323 AA; 36668 MW; D1FD813EC599D0C3 CRC64;
MDTLRIAVNG VSYNEASEIY KPHADPFTGP ITNLAPWNFA VLATLMFVIT SLSLFENFTV
MLATYKFKQL RQPLNYIIVN LSLADFLVSL TGGTISFLTN ARGYFFLGNW ACVLEGFAVT
YFGIVAMWSL AVLSFERYFV ICRPLGNVRL RGKHAALGLL FVWTFSFIWT IPPVFGWCSY
TVSKIGTTCE PNWYSNNIWN HTYIITFFVT CFIMPLGMII YCYGKLLQKL RKVSHDRLGN
AKKPERQVSR MVVVMIVAYL VGWTPYAAFS IIVTACPTIY LDPRLAAAPA FFSKTAAVYN
PVIYVFMNKQ VSTQLNWGFW SRA