OPSR_ASTFA
ID OPSR_ASTFA Reviewed; 357 AA.
AC P22332;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 2.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Red-sensitive opsin;
DE AltName: Full=Red cone photoreceptor pigment;
GN Name=R007;
OS Astyanax fasciatus (Blind cave fish) (Astyanax mexicanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Characidae; Psalidodon.
OX NCBI_TaxID=223369;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8336542; DOI=10.1093/oxfordjournals.molbev.a040024;
RA Yokoyama R., Yokoyama S.;
RT "Paralogous origin of the red- and green-sensitive visual pigment genes in
RT vertebrates.";
RL Mol. Biol. Evol. 10:527-538(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Pineal gland;
RX PubMed=2123554; DOI=10.1073/pnas.87.23.9315;
RA Yokoyama R., Yokoyama S.;
RT "Convergent evolution of the red- and green-like visual pigment genes in
RT fish, Astyanax fasciatus, and human.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:9315-9318(1990).
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 -!- 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. {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; M90075; AAA02766.1; -; Genomic_DNA.
DR EMBL; M38630; AAA62672.1; -; Genomic_DNA.
DR EMBL; M38625; AAA62672.1; JOINED; Genomic_DNA.
DR EMBL; M38626; AAA62672.1; JOINED; Genomic_DNA.
DR EMBL; M38627; AAA62672.1; JOINED; Genomic_DNA.
DR EMBL; M38628; AAA62672.1; JOINED; Genomic_DNA.
DR EMBL; M38629; AAA62672.1; JOINED; Genomic_DNA.
DR PIR; A37440; A37440.
DR AlphaFoldDB; P22332; -.
DR SMR; P22332; -.
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: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 1: Evidence at protein level;
KW Chromophore; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Phosphoprotein; Photoreceptor protein; Receptor; Retinal protein;
KW Sensory transduction; Transducer; Transmembrane; Transmembrane helix;
KW Vision.
FT CHAIN 1..357
FT /note="Red-sensitive opsin"
FT /id="PRO_0000197792"
FT TOPO_DOM 1..49
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 50..74
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 75..86
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..112
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 113..126
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..146
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 147..165
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 166..189
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 190..215
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..243
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 244..265
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..289
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 290..297
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 298..322
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 323..357
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 309
FT /note="N6-(retinylidene)lysine"
FT CARBOHYD 31
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 123..200
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 357 AA; 39837 MW; 41CA340478816DD4 CRC64;
MGDQWGDAVF AARRRGDDTT REAAFTYTNS NNTKDPFEGP NYHIAPRWVY NLATCWMFFV
VVASTVTNGL VLVASAKFKK LRHPLNWILV NLAIADLLET LLASTISVCN QFFGYFILGH
PMCVFEGFTV ATCGIAGLWS LTVISWERWV VVCKPFGNVK FDGKMATAGI VFTWVWSAVW
CAPPIFGWSR YWPHGLKTSC GPDVFSGSED PGVQSYMIVL MITCCFIPLG IIILCYIAVW
WAIRTVAQQQ KDSESTQKAE KEVSRMVVVM IMAYCFCWGP YTFFACFAAA NPGYAFHPLA
AAMPAYFAKS ATIYNPVIYV FMNRQFRVCI MQLFGKKVDD GSEVSTSKTE VSSVAPA
