OPSR_CHICK
ID OPSR_CHICK Reviewed; 362 AA.
AC P22329;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Red-sensitive opsin;
DE AltName: Full=Iodopsin;
DE AltName: Full=Red cone photoreceptor pigment;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Retina;
RX PubMed=2268324; DOI=10.1016/s0006-291x(05)80915-5;
RA Tokunaga F., Iwasa T., Miyagishi M., Kayada S.;
RT "Cloning of cDNA and amino acid sequence of one of chicken cone visual
RT pigments.";
RL Biochem. Biophys. Res. Commun. 173:1212-1217(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2226824; DOI=10.1016/0014-5793(90)80465-u;
RA Kuwata O., Imamoto Y., Okano T., Kokame K., Kojima D., Matsumoto H.,
RA Morodome A., Fukada Y., Shichida Y., Yasuda K., Shimura Y., Yoshizawa T.;
RT "The primary structure of iodopsin, a chicken red-sensitive cone pigment.";
RL FEBS Lett. 272:128-132(1990).
RN [3]
RP PROTEIN SEQUENCE OF 322-362, AND PHOSPHORYLATION.
RX PubMed=2271641; DOI=10.1021/bi00495a013;
RA Fukada Y., Kokame K., Okano T., Shichida Y., Yoshizawa T., McDowell J.H.,
RA Hargrave P.A., Palczewski K.;
RT "Phosphorylation of iodopsin, chicken red-sensitive cone visual pigment.";
RL Biochemistry 29:10102-10106(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-18.
RX PubMed=7629014; DOI=10.1093/oxfordjournals.jbchem.a124736;
RA Ishihara H., Engel J.D., Yamamoto M.;
RT "Structure and regulation of the chicken GATA-3 gene.";
RL J. Biochem. 117:499-508(1995).
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)=571 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. {ECO:0000269|PubMed:2271641}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Opsin
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M62903; AAA49137.1; -; mRNA.
DR EMBL; X57490; CAA40727.1; -; mRNA.
DR PIR; A37783; A37783.
DR RefSeq; NP_990771.1; NM_205440.1.
DR AlphaFoldDB; P22329; -.
DR SMR; P22329; -.
DR PRIDE; P22329; -.
DR GeneID; 396421; -.
DR KEGG; gga:396421; -.
DR CTD; 5956; -.
DR VEuPathDB; HostDB:geneid_396421; -.
DR OrthoDB; 940057at2759; -.
DR PhylomeDB; P22329; -.
DR PRO; PR:P22329; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0044297; C:cell body; IDA:AgBase.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0060342; C:photoreceptor inner segment membrane; IDA:AgBase.
DR GO; GO:0001750; C:photoreceptor outer segment; IDA:AgBase.
DR GO; GO:0031982; C:vesicle; IDA:AgBase.
DR GO; GO:0031404; F:chloride ion binding; IDA:AgBase.
DR GO; GO:0008020; F:G protein-coupled photoreceptor activity; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:AgBase.
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: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:0016037; P:light absorption; IDA:AgBase.
DR GO; GO:0007602; P:phototransduction; IBA:GO_Central.
DR GO; GO:0070207; P:protein homotrimerization; IDA:AgBase.
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; Direct protein sequencing; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Membrane; Phosphoprotein;
KW Photoreceptor protein; Receptor; Reference proteome; Retinal protein;
KW Sensory transduction; Transducer; Transmembrane; Transmembrane helix;
KW Vision.
FT CHAIN 1..362
FT /note="Red-sensitive opsin"
FT /id="PRO_0000197797"
FT TOPO_DOM 1..49
FT /note="Extracellular"
FT TRANSMEM 50..74
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 75..86
FT /note="Cytoplasmic"
FT TRANSMEM 87..112
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 113..126
FT /note="Extracellular"
FT TRANSMEM 127..146
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 147..165
FT /note="Cytoplasmic"
FT TRANSMEM 166..189
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 190..215
FT /note="Extracellular"
FT TRANSMEM 216..243
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 244..265
FT /note="Cytoplasmic"
FT TRANSMEM 266..289
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 290..297
FT /note="Extracellular"
FT TRANSMEM 298..322
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 323..362
FT /note="Cytoplasmic"
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"
FT CONFLICT 55
FT /note="V -> L (in Ref. 2; CAA40727)"
FT /evidence="ECO:0000305"
FT CONFLICT 240
FT /note="W -> S (in Ref. 2; CAA40727)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 362 AA; 40326 MW; C54426EF63E64B66 CRC64;
MAAWEAAFAA RRRHEEEDTT RDSVFTYTNS NNTRGPFEGP NYHIAPRWVY NLTSVWMIFV
VAASVFTNGL VLVATWKFKK LRHPLNWILV NLAVADLGET VIASTISVIN QISGYFILGH
PMCVVEGYTV SACGITALWS LAIISWERWF VVCKPFGNIK FDGKLAVAGI LFSWLWSCAW
TAPPIFGWSR YWPHGLKTSC GPDVFSGSSD PGVQSYMVVL MVTCCFFPLA IIILCYLQVW
LAIRAVAAQQ KESESTQKAE KEVSRMVVVM IVAYCFCWGP YTFFACFAAA NPGYAFHPLA
AALPAYFAKS ATIYNPIIYV FMNRQFRNCI LQLFGKKVDD GSEVSTSRTE VSSVSNSSVS
PA