OPSR_FELCA
ID OPSR_FELCA Reviewed; 364 AA.
AC O18913; Q9TST7;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Long-wave-sensitive opsin 1;
DE AltName: Full=Red cone photoreceptor pigment;
DE AltName: Full=Red-sensitive opsin;
GN Name=OPN1LW; Synonyms=RCP;
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE
RP SPECIFICITY.
RX PubMed=10511567; DOI=10.1093/genetics/153.2.919;
RA Yokoyama S., Radlwimmer F.B.;
RT "The molecular genetics of red and green color vision in mammals.";
RL Genetics 153:919-932(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 48-320.
RX PubMed=9580985; DOI=10.1093/oxfordjournals.molbev.a025956;
RA Yokoyama S., Radlwimmer F.B.;
RT "The 'five-sites' rule and the evolution of red and green color vision in
RT mammals.";
RL Mol. Biol. Evol. 15:560-567(1998).
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Absorption:
CC Abs(max)=553 nm {ECO:0000269|PubMed:10511567};
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: The three color pigments are found in the cone
CC photoreceptor cells. Expressed in retina (PubMed:10511567).
CC {ECO:0000269|PubMed:10511567}.
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; AF132040; AAD30521.1; -; mRNA.
DR EMBL; AF031532; AAB86632.1; -; mRNA.
DR RefSeq; NP_001009871.1; NM_001009871.1.
DR AlphaFoldDB; O18913; -.
DR SMR; O18913; -.
DR STRING; 9685.ENSFCAP00000010584; -.
DR Ensembl; ENSFCAT00000011393; ENSFCAP00000010584; ENSFCAG00000011390.
DR GeneID; 493959; -.
DR KEGG; fca:493959; -.
DR CTD; 5956; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01030000234549; -.
DR HOGENOM; CLU_009579_3_0_1; -.
DR InParanoid; O18913; -.
DR OMA; EWGKQSF; -.
DR OrthoDB; 940057at2759; -.
DR TreeFam; TF324998; -.
DR Proteomes; UP000011712; Chromosome X.
DR Bgee; ENSFCAG00000011390; Expressed in eyeball of camera-type eye.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0001750; C:photoreceptor outer segment; IBA:GO_Central.
DR GO; GO:0008020; F:G protein-coupled photoreceptor activity; IBA:GO_Central.
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: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 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; Vision.
FT CHAIN 1..364
FT /note="Long-wave-sensitive opsin 1"
FT /id="PRO_0000197800"
FT TOPO_DOM 1..52
FT /note="Extracellular"
FT TRANSMEM 53..77
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 78..89
FT /note="Cytoplasmic"
FT TRANSMEM 90..115
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 116..129
FT /note="Extracellular"
FT TRANSMEM 130..149
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 150..168
FT /note="Cytoplasmic"
FT TRANSMEM 169..192
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 193..218
FT /note="Extracellular"
FT TRANSMEM 219..246
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 247..268
FT /note="Cytoplasmic"
FT TRANSMEM 269..292
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 293..300
FT /note="Extracellular"
FT TRANSMEM 301..325
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 326..364
FT /note="Cytoplasmic"
FT MOD_RES 312
FT /note="N6-(retinylidene)lysine"
FT /evidence="ECO:0000250"
FT CARBOHYD 22
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250|UniProtKB:Q9BGI7"
FT CARBOHYD 34
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 126..203
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 364 AA; 40412 MW; F37C32FF6B1C5B97 CRC64;
MTQRWGPQRL AGGQPHAGLE DSTRASIFTY TNSNATRGPF EGPNYHIAPR WVYHVTSAWM
IFVVIASVFT NGLVLAATMK FKKLRHPLNW ILVNLAVADL AETIIASTIS VVNQIYGYFV
LGHPMCVLEG YTVSLCGITG LWSLAIISWE RWLVVCKPFG NVRFDAKLAI AGIAFSWIWA
AVWTAPPIFG WSRYWPHGLK TSCGPDVFSG SSYPGVQSYM IVLMITCCII PLSVIVLCYL
QVWLAIRAVA KQQKESESTQ KAEKEVTRMV MVMIFAYCVC WGPYTFFACF AAAHPGYAFH
PLVAALPAYF AKSATIYNPI IYVFMNRQFR NCIMQLFGKK VDDGSELSSA SRTEASSVSS
VSPA
