ID OPN4_RUTRU Reviewed; 500 AA.
AC Q6XL69;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 22-FEB-2023, entry version 59.
DE RecName: Full=Melanopsin;
DE AltName: Full=Opsin-4;
GN Name=opn4;
OS Rutilus rutilus (Roach).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Leuciscidae; Leuciscinae; Rutilus.
OX NCBI_TaxID=48668;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAO38857.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Retina {ECO:0000312|EMBL:AAO38857.1};
RX PubMed=12906786; DOI=10.1016/s0960-9822(03)00509-8;
RA Jenkins A., Munoz M., Tarttelin E.E., Bellingham J., Foster R.G.,
RA Hankins M.W.;
RT "VA opsin, melanopsin, and an inherent light response within retinal
RT interneurons.";
RL Curr. Biol. 13:1269-1278(2003).
CC -!- FUNCTION: Photoreceptor implicated in non-image-forming responses to
CC light. {ECO:0000250|UniProtKB:Q9QXZ9}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9QXZ9};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in a subset of retinal horizontal cells
CC as well as in retinal ganglion cells. {ECO:0000269|PubMed:12906786}.
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; AY226847; AAO38857.1; -; mRNA.
DR AlphaFoldDB; Q6XL69; -.
DR SMR; Q6XL69; -.
DR GlyCosmos; Q6XL69; 1 site, No reported glycans.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
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:InterPro.
DR CDD; cd15336; 7tmA_Melanopsin; 1.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR001760; Opsin.
DR InterPro; IPR027430; Retinal_BS.
DR PANTHER; PTHR24240:SF144; MELANOPSIN-LIKE; 1.
DR PANTHER; PTHR24240; OPSIN; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00238; OPSIN.
DR SMART; SM01381; 7TM_GPCR_Srsx; 1.
DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 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 2: Evidence at transcript level;
KW Cell membrane; Chromophore; Disulfide bond; G-protein coupled receptor;
KW Glycoprotein; Membrane; Photoreceptor protein; Receptor; Retinal protein;
KW Sensory transduction; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..500
FT /note="Melanopsin"
FT /id="PRO_0000270992"
FT TOPO_DOM 1..65
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 66..86
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 87..101
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..122
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 123..138
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..159
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 160..182
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 204..232
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 233..253
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 254..286
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 287..307
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 308..322
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 323..343
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 344..500
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 406..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 448..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 481..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..465
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 330
FT /note="N6-(retinylidene)lysine"
FT /evidence="ECO:0000250"
FT CARBOHYD 18
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 137..215
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 500 AA; 54523 MW; 86B0D626B48DF427 CRC64;
MSHHSSWRGH HCAPGDNNCT AGFKESLGSK NYKLLHVPFH GPTHSHHHEP PHPFPTVDVP
DHAHYIIGAV ILIVGITGVI GNALVIYVFC RSRTLRTAGN MFVVNLAVAD FFMSLTQSPV
FFAASLHRRW IFGERICELY AFCGALFGIC SMMTLTAIAA DRCLAITQPL ALVGNVSRRK
AGAVLAVVWL YSLGWSLPPF FGWSAYVPEG LQTSCSWDYM TFTPSVRAYT ILLFIFVFFI
PLGIIVSCYV GIFQAIRAMG KEIRELDCGE TQKVYERMQN EWKMAKIALL VILLFVISWS
PYSVVALTAT AGYSHLLTPY MNSVPAVIAK ASAIHNPIIY AITHPKYRAA IARYIPVLRT
ILRVKEKELR SSFSSGSVSS RRPTLSSQCS LGVSIGNAAR ANGRWGKKRL SSASDSDSCW
TESEADGSSV SSLTFGRRVS TEISTDTVIL SPGSSNSTAS GQKSEKAHKV VSVPVPSITF
ETDSADESLS DGKALLLGGN
//
