OPN4_RAT
ID OPN4_RAT Reviewed; 474 AA.
AC Q8R456;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Melanopsin;
DE AltName: Full=Opsin-4;
GN Name=Opn4 {ECO:0000312|RGD:621701};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAL61854.1}
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley {ECO:0000312|EMBL:AAL61854.1};
RC TISSUE=Retina {ECO:0000312|EMBL:AAL61854.1};
RX PubMed=11834834; DOI=10.1126/science.1069609;
RA Hattar S., Liao H.-W., Takao M., Berson D.M., Yau K.-W.;
RT "Melanopsin-containing retinal ganglion cells: architecture, projections,
RT and intrinsic photosensitivity.";
RL Science 295:1065-1070(2002).
CC -!- FUNCTION: Photoreceptor that binds cis-retinaldehydes (By similarity).
CC Contributes to pupillar reflex, photoentrainment and other non-image
CC forming responses to light (By similarity). May be involved in the
CC optokinetic visual tracking response (By similarity). May be involved
CC in the regulation of retinal hyaloid vessel growth and regression (By
CC similarity). {ECO:0000250|UniProtKB:Q9QXZ9}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11834834};
CC Multi-pass membrane protein {ECO:0000255}. Cell projection, axon
CC {ECO:0000250|UniProtKB:Q9QXZ9}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:Q9QXZ9}. Perikaryon
CC {ECO:0000250|UniProtKB:Q9QXZ9}.
CC -!- TISSUE SPECIFICITY: Eye; expressed in a photosensitive subset of
CC retinal ganglion cells (at protein level).
CC {ECO:0000269|PubMed:11834834}.
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; AY072689; AAL61854.1; -; mRNA.
DR RefSeq; NP_620215.1; NM_138860.1.
DR RefSeq; XP_017455477.1; XM_017599988.1.
DR RefSeq; XP_017455478.1; XM_017599989.1.
DR AlphaFoldDB; Q8R456; -.
DR SMR; Q8R456; -.
DR STRING; 10116.ENSRNOP00000015642; -.
DR GlyGen; Q8R456; 2 sites.
DR iPTMnet; Q8R456; -.
DR PhosphoSitePlus; Q8R456; -.
DR PaxDb; Q8R456; -.
DR PRIDE; Q8R456; -.
DR Ensembl; ENSRNOT00000091315; ENSRNOP00000069548; ENSRNOG00000053893.
DR GeneID; 192223; -.
DR KEGG; rno:192223; -.
DR UCSC; RGD:621701; rat.
DR CTD; 94233; -.
DR RGD; 621701; Opn4.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01030000234631; -.
DR HOGENOM; CLU_009579_3_12_1; -.
DR InParanoid; Q8R456; -.
DR OMA; HYTIGTV; -.
DR OrthoDB; 911005at2759; -.
DR PhylomeDB; Q8R456; -.
DR TreeFam; TF324998; -.
DR Reactome; R-RNO-416476; G alpha (q) signalling events.
DR Reactome; R-RNO-419771; Opsins.
DR PRO; PR:Q8R456; -.
DR Proteomes; UP000002494; Chromosome 16.
DR Bgee; ENSRNOG00000053893; Expressed in skeletal muscle tissue and 4 other tissues.
DR Genevisible; Q8R456; RN.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; TAS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:1990913; C:sperm head plasma membrane; ISO:RGD.
DR GO; GO:0005502; F:11-cis retinal binding; ISS:UniProtKB.
DR GO; GO:0008020; F:G protein-coupled photoreceptor activity; IDA:RGD.
DR GO; GO:0071482; P:cellular response to light stimulus; IBA:GO_Central.
DR GO; GO:0050960; P:detection of temperature stimulus involved in thermoception; ISO:RGD.
DR GO; GO:0043153; P:entrainment of circadian clock by photoperiod; ISO:RGD.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:1990384; P:hyaloid vascular plexus regression; ISS:UniProtKB.
DR GO; GO:0007634; P:optokinetic behavior; ISS:UniProtKB.
DR GO; GO:0007602; P:phototransduction; IDA:RGD.
DR GO; GO:0045938; P:positive regulation of circadian sleep/wake cycle, sleep; ISO:RGD.
DR GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
DR GO; GO:0016056; P:rhodopsin mediated signaling pathway; ISO:RGD.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR GO; GO:0043052; P:thermotaxis; ISO:RGD.
DR GO; GO:0007601; P:visual perception; IEA:InterPro.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR001760; Opsin.
DR InterPro; IPR027430; Retinal_BS.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00238; OPSIN.
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 Biological rhythms; Cell membrane; Cell projection; Chromophore;
KW Disulfide bond; G-protein coupled receptor; Glycoprotein; Membrane;
KW Photoreceptor protein; Receptor; Reference proteome; Retinal protein;
KW Sensory transduction; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..474
FT /note="Melanopsin"
FT /id="PRO_0000233062"
FT TOPO_DOM 1..72
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 73..93
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 94..107
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 108..128
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 129..144
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..165
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 166..188
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..209
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 210..238
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..259
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 260..293
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 294..314
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 315..355
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 356..372
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 373..474
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 428..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..474
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 337
FT /note="N6-(retinylidene)lysine"
FT /evidence="ECO:0000250"
FT CARBOHYD 31
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 35
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 143..221
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 474 AA; 52407 MW; 33C302113D41E5EC CRC64;
MNSPSESRVP SSLTQDPSFT ASPALLQGIW NSTQNISVRV QLLSVSPTTP GLQAAAWVPF
PTVDVPDHAH YTLGTVILLV GLTGMLGNLT VIYTFCRNRG LRTPANMLII NLAVSDFLMS
FTQAPVFFAS SLYKKWLFGE TGCKFYAFCG AVFGIVSMIT LTAIAMDRYL VITRPLATIG
MRSKRRTALV LLGVWLYALA WSLPPFFGWS AYVPEGLLTS CSWDYVTFTP LVRAYTMLLF
CFVFFLPLLI IIFCYIFIFR AIRETGRACE GCGESPLRRR QWQRLQSEWK MAKVALIVIL
LFVLSWAPYS TVALVGFAGY SHILTPYMSS VPAVIAKASA IHNPIIYAIT HPKYRAAIAQ
HLPCLGVLLG VSGQRSHPSL SYRSTHRSTL SSQSSDLSWI SGQKRQESLG SESEVGWTDT
ETTAAWGAAQ QASGQSFCSH DLEDGEVKAP SSPQEQKSKT PKTKRHLPSL DRRM
