OPN4_MOUSE
ID OPN4_MOUSE Reviewed; 521 AA.
AC Q9QXZ9; A4QPG3; B2C712;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Melanopsin;
DE AltName: Full=Opsin-4;
GN Name=Opn4; Synonyms=Mop, Mopn;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Retina;
RX PubMed=10632589; DOI=10.1523/jneurosci.20-02-00600.2000;
RA Provencio I., Rodriguez I.R., Jiang G., Hayes W.P., Moreira E.F.,
RA Rollag M.D.;
RT "A novel human opsin in the inner retina.";
RL J. Neurosci. 20:600-605(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), SYNTHESIS OF 1-15 AND
RP 500-514, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=C3H/He; TISSUE=Retina;
RX PubMed=19793992; DOI=10.1523/jneurosci.2036-09.2009;
RA Pires S.S., Hughes S., Turton M., Melyan Z., Peirson S.N., Zheng L.,
RA Kosmaoglou M., Bellingham J., Cheetham M.E., Lucas R.J., Foster R.G.,
RA Hankins M.W., Halford S.;
RT "Differential expression of two distinct functional isoforms of melanopsin
RT (Opn4) in the mammalian retina.";
RL J. Neurosci. 29:12332-12342(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP SUBCELLULAR LOCATION.
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).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12808468; DOI=10.1038/nature01761;
RA Hattar S., Lucas R.J., Mrosovsky N., Thompson S., Douglas R.H.,
RA Hankins M.W., Lem J., Biel M., Hofmann F., Foster R.G., Yau K.-W.;
RT "Melanopsin and rod-cone photoreceptive systems account for all major
RT accessory visual functions in mice.";
RL Nature 424:76-81(2003).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26392540; DOI=10.1073/pnas.1516259112;
RA Buhr E.D., Yue W.W., Ren X., Jiang Z., Liao H.W., Mei X., Vemaraju S.,
RA Nguyen M.T., Reed R.R., Lang R.A., Yau K.W., Van Gelder R.N.;
RT "Neuropsin (OPN5)-mediated photoentrainment of local circadian oscillators
RT in mammalian retina and cornea.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:13093-13098(2015).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=30240620; DOI=10.1016/j.isci.2018.08.010;
RA Ota W., Nakane Y., Hattar S., Yoshimura T.;
RT "Impaired Circadian Photoentrainment in Opn5-Null Mice.";
RL IScience 6:299-305(2018).
RN [9]
RP TISSUE SPECIFICITY.
RX PubMed=31607531; DOI=10.1016/j.cub.2019.08.063;
RA Buhr E.D., Vemaraju S., Diaz N., Lang R.A., Van Gelder R.N.;
RT "Neuropsin (OPN5) Mediates Local Light-Dependent Induction of Circadian
RT Clock Genes and Circadian Photoentrainment in Exposed Murine Skin.";
RL Curr. Biol. 29:3478-3487.e4(2019).
RN [10]
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=30936473; DOI=10.1038/s41556-019-0301-x;
RA Nguyen M.T., Vemaraju S., Nayak G., Odaka Y., Buhr E.D., Alonzo N.,
RA Tran U., Batie M., Upton B.A., Darvas M., Kozmik Z., Rao S., Hegde R.S.,
RA Iuvone P.M., Van Gelder R.N., Lang R.A.;
RT "An opsin 5-dopamine pathway mediates light-dependent vascular development
RT in the eye.";
RL Nat. Cell Biol. 21:420-429(2019).
CC -!- FUNCTION: Photoreceptor that binds cis-retinaldehydes
CC (PubMed:19793992). Contributes to pupillar reflex, photoentrainment and
CC other non-image forming responses to light (PubMed:12808468). May be
CC involved in the optokinetic visual tracking response (PubMed:26392540).
CC May be involved in the regulation of retinal hyaloid vessel growth and
CC regression (PubMed:30936473). {ECO:0000269|PubMed:12808468,
CC ECO:0000269|PubMed:19793992, ECO:0000269|PubMed:26392540,
CC ECO:0000269|PubMed:30936473}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19793992};
CC Multi-pass membrane protein {ECO:0000255}. Cell projection, axon
CC {ECO:0000269|PubMed:11834834}. Cell projection, dendrite
CC {ECO:0000269|PubMed:11834834}. Perikaryon
CC {ECO:0000269|PubMed:11834834}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Opn4L;
CC IsoId=Q9QXZ9-1; Sequence=Displayed;
CC Name=2; Synonyms=Opn4S;
CC IsoId=Q9QXZ9-2; Sequence=VSP_045928;
CC -!- TISSUE SPECIFICITY: Expressed in the retinal pigment epithelium and
CC ganglion cell layer (at protein level) (PubMed:10632589,
CC PubMed:30240620, PubMed:31607531). Also expressed in amacrine cell
CC layers of the retina (PubMed:10632589). Weakly expressed in vibrissae,
CC and tail (PubMed:31607531). {ECO:0000269|PubMed:10632589,
CC ECO:0000269|PubMed:30240620, ECO:0000269|PubMed:31607531}.
CC -!- TISSUE SPECIFICITY: [Isoform 1]: Observed with processes in the outer
CC strata of inner plexiform layer (IPL) close to the inner nuclear layer
CC (INL) or is found to be bistratified with processes located both in the
CC inner (ON) or outer (OFF) layers of the IPL (at protein level)
CC (PubMed:19793992). A second population of isoform 1 is identified in
CC processes which are confined to the inner layer of the IPL near to the
CC ganglion cell layer (GCL) (at protein level) (PubMed:19793992).
CC {ECO:0000269|PubMed:19793992}.
CC -!- TISSUE SPECIFICITY: [Isoform 2]: About 40 times more abundant than
CC isoform 1 in the retina (at protein level) (PubMed:19793992). Isoform 2
CC is involved in processes localized to the outer IPL or is bistratified
CC with processes in both the inner and outer layers of the IPL (at
CC protein level) (PubMed:19793992). Isoform 2 is absent in the processes
CC confined only to the inner layer of the IPL (at protein level)
CC (PubMed:19793992). {ECO:0000269|PubMed:19793992}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the inner retina at postnatal day 5
CC (P5), and expressed in retinal ganglion cells at P12.
CC {ECO:0000269|PubMed:30936473}.
CC -!- DISRUPTION PHENOTYPE: Mice fail to show a pupillar reflex,
CC photoentrainment of the circadian clock and other non-image forming
CC responses to light (PubMed:12808468). Newborn mice show normal hyaloid
CC vessel numbers and normal vessel cellularity, however vessel numbers
CC are increased by P8 (PubMed:30936473). In Opn4 and Pde6b double
CC knockout mice optokinetic visual tracking response is abolished
CC (PubMed:26392540). {ECO:0000269|PubMed:12808468,
CC ECO:0000269|PubMed:26392540, ECO:0000269|PubMed:30936473}.
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; AF147789; AAF24979.1; -; mRNA.
DR EMBL; EU303117; ACA01962.1; -; mRNA.
DR EMBL; EU303118; ACA01963.1; -; mRNA.
DR EMBL; AC114543; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC139827; AAI39828.1; -; mRNA.
DR CCDS; CCDS26943.1; -. [Q9QXZ9-1]
DR CCDS; CCDS49446.1; -. [Q9QXZ9-2]
DR RefSeq; NP_001122071.1; NM_001128599.1. [Q9QXZ9-2]
DR RefSeq; NP_038915.1; NM_013887.2. [Q9QXZ9-1]
DR AlphaFoldDB; Q9QXZ9; -.
DR SMR; Q9QXZ9; -.
DR IntAct; Q9QXZ9; 4.
DR STRING; 10090.ENSMUSP00000022331; -.
DR GlyGen; Q9QXZ9; 2 sites.
DR iPTMnet; Q9QXZ9; -.
DR PhosphoSitePlus; Q9QXZ9; -.
DR PaxDb; Q9QXZ9; -.
DR PRIDE; Q9QXZ9; -.
DR Antibodypedia; 30087; 95 antibodies from 23 providers.
DR DNASU; 30044; -.
DR Ensembl; ENSMUST00000022331; ENSMUSP00000022331; ENSMUSG00000021799. [Q9QXZ9-1]
DR Ensembl; ENSMUST00000168444; ENSMUSP00000126136; ENSMUSG00000021799. [Q9QXZ9-2]
DR GeneID; 30044; -.
DR KEGG; mmu:30044; -.
DR UCSC; uc007tbh.2; mouse. [Q9QXZ9-1]
DR UCSC; uc011ziw.1; mouse. [Q9QXZ9-2]
DR CTD; 94233; -.
DR MGI; MGI:1353425; Opn4.
DR VEuPathDB; HostDB:ENSMUSG00000021799; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01030000234631; -.
DR HOGENOM; CLU_009579_3_12_1; -.
DR InParanoid; Q9QXZ9; -.
DR OMA; HYTIGTV; -.
DR OrthoDB; 911005at2759; -.
DR PhylomeDB; Q9QXZ9; -.
DR TreeFam; TF324998; -.
DR Reactome; R-MMU-416476; G alpha (q) signalling events.
DR Reactome; R-MMU-419771; Opsins.
DR BioGRID-ORCS; 30044; 5 hits in 73 CRISPR screens.
DR PRO; PR:Q9QXZ9; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q9QXZ9; protein.
DR Bgee; ENSMUSG00000021799; Expressed in iris and 38 other tissues.
DR Genevisible; Q9QXZ9; MM.
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; IDA:MGI.
DR GO; GO:0005502; F:11-cis retinal binding; ISS:UniProtKB.
DR GO; GO:0008020; F:G protein-coupled photoreceptor activity; IMP:UniProtKB.
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; IGI:MGI.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:1990384; P:hyaloid vascular plexus regression; IMP:UniProtKB.
DR GO; GO:0007634; P:optokinetic behavior; IMP:UniProtKB.
DR GO; GO:0007602; P:phototransduction; IMP:UniProtKB.
DR GO; GO:0042752; P:regulation of circadian rhythm; IMP:UniProtKB.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR GO; GO:0043052; P:thermotaxis; IGI:MGI.
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 Alternative splicing; Biological rhythms; Cell membrane; Cell projection;
KW Chromophore; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Photoreceptor protein; Receptor; Reference proteome;
KW Retinal protein; Sensory transduction; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..521
FT /note="Melanopsin"
FT /id="PRO_0000197816"
FT TOPO_DOM 1..71
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..92
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 93..106
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 107..127
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 128..143
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 144..164
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 165..187
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 188..208
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 209..237
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..258
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 259..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..329
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 330..350
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 351..521
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 445..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..463
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 337
FT /note="N6-(retinylidene)lysine"
FT CARBOHYD 30
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 34
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 142..220
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT VAR_SEQ 455..521
FT /note="VQRSKTPKVPGPSTCRPMKGQGARPSSLRGDQKGRLAVCTGLSECPHPHTSQ
FT FPLAFLEDDVTLRHL -> TKGHLPSLDLGM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19793992"
FT /id="VSP_045928"
SQ SEQUENCE 521 AA; 57231 MW; 50FD1CBB05669DA9 CRC64;
MDSPSGPRVL SSLTQDPSFT TSPALQGIWN GTQNVSVRAQ LLSVSPTTSA HQAAAWVPFP
TVDVPDHAHY TLGTVILLVG LTGMLGNLTV IYTFCRNRGL RTPANMFIIN LAVSDFLMSV
TQAPVFFASS LYKKWLFGET GCEFYAFCGA VFGITSMITL TAIAMDRYLV ITRPLATIGR
GSKRRTALVL LGVWLYALAW SLPPFFGWSA YVPEGLLTSC SWDYMTFTPQ VRAYTMLLFC
FVFFLPLLII IFCYIFIFRA IRETGRACEG CGESPLRQRR QWQRLQSEWK MAKVALIVIL
LFVLSWAPYS TVALVAFAGY SHILTPYMSS VPAVIAKASA IHNPIIYAIT HPKYRVAIAQ
HLPCLGVLLG VSGQRSHPSL SYRSTHRSTL SSQSSDLSWI SGRKRQESLG SESEVGWTDT
ETTAAWGAAQ QASGQSFCSQ NLEDGELKAS SSPQVQRSKT PKVPGPSTCR PMKGQGARPS
SLRGDQKGRL AVCTGLSECP HPHTSQFPLA FLEDDVTLRH L
