OPSUV_MELUD
ID OPSUV_MELUD Reviewed; 347 AA.
AC O57605;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Ultraviolet-sensitive opsin;
DE AltName: Full=Ultraviolet cone photoreceptor pigment;
OS Melopsittacus undulatus (Budgerigar) (Psittacus undulatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Psittaciformes; Psittaculidae;
OC Melopsittacus.
OX NCBI_TaxID=13146;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC TISSUE=Retina;
RX PubMed=9461554; DOI=10.1042/bj3300541;
RA Wilkie S.E., Vissers P.M.A.M., Das D., DeGrip W.J., Bowmaker J.K.,
RA Hunt D.M.;
RT "The molecular basis for UV vision in birds: spectral characteristics, cDNA
RT sequence and retinal localization of the UV-sensitive visual pigment of the
RT budgerigar (Melopsittacus undulatus).";
RL Biochem. J. 330:541-547(1998).
RN [2]
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Retina;
RX PubMed=9578901; DOI=10.1016/s0042-6989(97)00026-6;
RA Bowmaker J.K., Heath L.A., Wilkie S.E., Hunt D.M.;
RT "Visual pigments and oil droplets from six classes of photoreceptor in the
RT retinas of birds.";
RL Vision Res. 37:2183-2194(1997).
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)=371 nm {ECO:0000269|PubMed:9461554,
CC ECO:0000269|PubMed:9578901};
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Cone photoreceptor cells.
CC {ECO:0000269|PubMed:9461554}.
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; Y11787; CAA72483.1; -; mRNA.
DR RefSeq; NP_001298010.1; NM_001311081.1.
DR AlphaFoldDB; O57605; -.
DR SMR; O57605; -.
DR GeneID; 101869469; -.
DR OrthoDB; 940057at2759; -.
DR Proteomes; UP000694405; Unplaced.
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:0016038; P:absorption of visible light; ISS: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; IPR001521; Opsin_blue.
DR InterPro; IPR027430; Retinal_BS.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00238; OPSIN.
DR PRINTS; PR00574; OPSINBLUE.
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; Reference proteome; Retinal protein; Sensory transduction;
KW Transducer; Transmembrane; Transmembrane helix; Vision.
FT CHAIN 1..347
FT /note="Ultraviolet-sensitive opsin"
FT /id="PRO_0000197769"
FT TOPO_DOM 1..37
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 38..58
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 59..69
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 70..90
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 91..106
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 107..127
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 128..147
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 148..168
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 169..197
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 198..218
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 219..247
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 248..268
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 269..282
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 283..303
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 304..347
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 324..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 291
FT /note="N6-(retinylidene)lysine"
FT /evidence="ECO:0000250"
FT LIPID 317
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 12
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 105..182
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 347 AA; 38791 MW; C272A8690F228E4A CRC64;
MSGEEEFYLF KNGSIGGPWD GPQYHIAPPW AFYLQTAFMG FVFMVGTPLN AIVLVVTIKY
KKLRQPLNYI LVNISFCGFL ACIICIFTVF VSSSQGYFVF GKHVCAFEGF MGATAGLVTG
WSLAFLAFER YIVICKPLGN FRFTAKHALV VVVATWVIGI GVAIPPFFGW SRYVPEGLQC
SCGPDWYTVG TKYRSEYYTW FLFIFCFIVP LSLIIFSYSQ LLSALRAVAA QQQESATTQK
AEREVSRMVV VMVGSFCVCY VPYAALAMYM VNNREHGIDL RLVTIPAFFS KSSCVYNPII
YCFMNKQFRG CIMEMVCGKP MTDDSDMSSS AQRTEVSSVS SSQVSPS
