OPSR_XENLA
ID OPSR_XENLA Reviewed; 365 AA.
AC O12948; Q66IX0;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Red-sensitive opsin;
DE AltName: Full=Red cone photoreceptor pigment;
GN Name=opn1lw1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9622007;
RX DOI=10.1002/(sici)1097-4695(19980605)35:3<227::aid-neu1>3.0.co;2-0;
RA Chang W.S., Harris W.A.;
RT "Sequential genesis and determination of cone and rod photoreceptors in
RT Xenopus.";
RL J. Neurobiol. 35:227-244(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
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.
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.
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; U90895; AAC60374.1; -; mRNA.
DR EMBL; BC081156; AAH81156.1; -; mRNA.
DR RefSeq; NP_001084114.1; NM_001090645.1.
DR AlphaFoldDB; O12948; -.
DR SMR; O12948; -.
DR DNASU; 399310; -.
DR GeneID; 399310; -.
DR KEGG; xla:399310; -.
DR CTD; 399310; -.
DR Xenbase; XB-GENE-955013; opn1lw.L.
DR OrthoDB; 940057at2759; -.
DR Proteomes; UP000186698; Chromosome 8L.
DR Bgee; 399310; Expressed in camera-type eye and 5 other tissues.
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:0016039; P:absorption of UV light; IDA:AgBase.
DR GO; GO:0016038; P:absorption of visible light; IDA:AgBase.
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; IPR000378; Opsin_red/grn.
DR InterPro; IPR027430; Retinal_BS.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00238; OPSIN.
DR PRINTS; PR00575; OPSINREDGRN.
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;
KW Reference proteome; Retinal protein; Sensory transduction; Transducer;
KW Transmembrane; Transmembrane helix; Vision.
FT CHAIN 1..365
FT /note="Red-sensitive opsin"
FT /id="PRO_0000197803"
FT TOPO_DOM 1..51
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 52..76
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 77..88
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 89..113
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 114..128
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 129..148
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 149..167
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..191
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 192..217
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..245
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 246..267
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 268..291
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 292..299
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 300..324
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 325..365
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 342..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 311
FT /note="N6-(retinylidene)lysine"
FT /evidence="ECO:0000250"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 125..202
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 365 AA; 41094 MW; 96EA4D31D4D80473 CRC64;
MASQLNEAIF AARRRNDDDD TTRSSVFTYT NSNNTRGPFE GPNYHIAPRW VYNLTSIWMI
FVVFASVFTN GLVIVATLKF KKLRHPLNWI LVNMAIADLG ETVIASTISV FNQIFGYFIL
GHPMCVLEGF TVSTCGITAL WSLTVIAWER WFVVCKPFGN IKFDEKLAAT GIIFSWVWSA
GWCAPPMFGW SRFWPHGLKT SCGPDVFSGS SDPGVQSYML VLMITCCIIP LAIIILCYLH
VWWTIRQVAQ QQKESESTQK AEREVSRMVV VMIVAYIFCW GPYTFFACFA AFSPGYSFHP
LAAALPAYFA KSATIYNPII YVFMNRQFRN CIYQMFGKKV DDGSEVSSTS RTEVSSVSNS
SVSPA
