OPSL_CALJA
ID OPSL_CALJA Reviewed; 350 AA.
AC P34989;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Opsin, longwave 563 nm;
DE Flags: Fragment;
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=8447088; DOI=10.1016/0042-6989(93)90153-n;
RA Hunt D.M., Williams A.J., Bowmaker J.K., Mollon J.D.;
RT "Structure and evolution of the polymorphic photopigment gene of the
RT marmoset.";
RL Vision Res. 33:147-154(1993).
RN [2]
RP CHARACTERIZATION.
RX PubMed=1534748; DOI=10.1002/j.1460-2075.1992.tb05261.x;
RA Williams A.J., Hunt D.M., Bowmaker J.K., Mollon J.D.;
RT "The polymorphic photopigments of the marmoset: spectral tuning and genetic
RT basis.";
RL EMBO J. 11:2039-2045(1992).
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)=563 nm;
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: The color pigments are found in the cone
CC photoreceptor cells.
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; Z22218; CAA80221.1; -; mRNA.
DR PIR; S43497; S43497.
DR AlphaFoldDB; P34989; -.
DR SMR; P34989; -.
DR STRING; 9483.ENSCJAP00000026548; -.
DR eggNOG; KOG3656; Eukaryota.
DR Proteomes; UP000008225; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0097381; C:photoreceptor disc membrane; IEA:UniProt.
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; 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 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..>350
FT /note="Opsin, longwave 563 nm"
FT /id="PRO_0000197804"
FT TOPO_DOM <1..45
FT /note="Extracellular"
FT TRANSMEM 46..70
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 71..82
FT /note="Cytoplasmic"
FT TRANSMEM 83..108
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 109..122
FT /note="Extracellular"
FT TRANSMEM 123..142
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 143..161
FT /note="Cytoplasmic"
FT TRANSMEM 162..185
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 186..211
FT /note="Extracellular"
FT TRANSMEM 212..239
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 240..261
FT /note="Cytoplasmic"
FT TRANSMEM 262..285
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 286..293
FT /note="Extracellular"
FT TRANSMEM 294..318
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 319..>350
FT /note="Cytoplasmic"
FT MOD_RES 305
FT /note="N6-(retinylidene)lysine"
FT /evidence="ECO:0000250"
FT CARBOHYD 27
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT DISULFID 119..196
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT NON_TER 1
FT NON_TER 350
SQ SEQUENCE 350 AA; 39138 MW; 45E38949EE81E252 CRC64;
HRLAGRHPQD NYEDSTQSSI FTYTNSNSTR GPFEGPNYHI APRWVYHLTS VWMLFVVVAS
VFTNGLVLAA TMKFKKLRHP LNWILVNLAI ADLAETVIAS TISVVNQVHG YFVLGHPMCV
LEGYTVSLCG ITGLWSLAII SWERWLVVCK PFGNVRFDAK LAIVGVAFSW IWSAVWTAPP
IFGWSRYWPH GLKTSCGPDV FSGSSYPGVQ SYMIVLMITC CFLPLGIIVL CYLQVWLAIR
AVAKQQKESE STQKAEKEVT RMVVVMIVAY CVCWGPYTFF ACFAAANPGY AFHPLMAALP
AYFAKSATIY NPIIYVFMNR QFRNCILQLF GKKVDDGSEL SSASKTEVSS
