OPN3_MOUSE
ID OPN3_MOUSE Reviewed; 400 AA.
AC Q9WUK7; Q3V0X3;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Opsin-3;
DE AltName: Full=Encephalopsin;
DE AltName: Full=Panopsin;
GN Name=Opn3; Synonyms=Ecpn;
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], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=10234000; DOI=10.1523/jneurosci.19-10-03681.1999;
RA Blackshaw S., Snyder S.H.;
RT "Encephalopsin: a novel mammalian extraretinal opsin discretely localized
RT in the brain.";
RL J. Neurosci. 19:3681-3690(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=12242008; DOI=10.1016/s0378-1119(02)00799-0;
RA Kasper G., Taudien S., Staub E., Mennerich D., Rieder M., Hinzmann B.,
RA Dahl E., Schwidetzky U., Rosenthal A., Rump A.;
RT "Different structural organization of the encephalopsin gene in man and
RT mouse.";
RL Gene 295:27-32(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=30284927; DOI=10.1152/ajplung.00135.2018;
RA Yim P.D., Gallos G., Perez-Zoghbi J.F., Zhang Y., Xu D., Wu A.,
RA Berkowitz D.E., Emala C.W.;
RT "Airway smooth muscle photorelaxation via opsin receptor activation.";
RL Am. J. Physiol. 316:L82-L93(2019).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP 136-GLU--TYR-138.
RX PubMed=32040503; DOI=10.1371/journal.pbio.3000630;
RA Sato M., Tsuji T., Yang K., Ren X., Dreyfuss J.M., Huang T.L., Wang C.H.,
RA Shamsi F., Leiria L.O., Lynes M.D., Yau K.W., Tseng Y.H.;
RT "Cell-autonomous light sensitivity via Opsin3 regulates fuel utilization in
RT brown adipocytes.";
RL PLoS Biol. 18:e3000630-e3000630(2020).
CC -!- FUNCTION: G-protein coupled receptor which selectively activates G
CC proteins via ultraviolet A (UVA) light-mediated activation in the skin
CC (PubMed:30284927). Binds both 11-cis retinal and all-trans retinal (By
CC similarity). Regulates melanogenesis in melanocytes via inhibition of
CC alpha-MSH-induced MC1R-mediated cAMP signaling, modulation of calcium
CC flux, regulation of CAMK2 phosphorylation, and subsequently
CC phosphorylation of CREB, p38, ERK and MITF in response to blue light
CC (By similarity). Plays a role in melanocyte survival through regulation
CC of intracellular calcium levels and subsequent BCL2/RAF1 signaling (By
CC similarity). Additionally regulates apoptosis via cytochrome c release
CC and subsequent activation of the caspase cascade (By similarity).
CC Required for TYR and DCT blue light-induced complex formation in
CC melanocytes (By similarity). Involved in keratinocyte differentiation
CC in response to blue-light (By similarity). Required for the UVA-
CC mediated induction of calcium and mitogen-activated protein kinase
CC signaling resulting in the expression of MMP1, MMP2, MMP3, MMP9 and
CC TIMP1 in dermal fibroblasts (By similarity). Plays a role in light-
CC mediated glucose uptake, mitochondrial respiration and fatty acid
CC metabolism in brown adipocyte tissues (PubMed:32040503). May be
CC involved in photorelaxation of airway smooth muscle cells, via blue-
CC light dependent GPCR signaling pathways (PubMed:30284927).
CC {ECO:0000250|UniProtKB:Q9H1Y3, ECO:0000269|PubMed:30284927,
CC ECO:0000269|PubMed:32040503}.
CC -!- SUBUNIT: Interacts with MC1R; the interaction results in a decrease in
CC MC1R-mediated cAMP signaling and ultimately a decrease in melanin
CC production in melanocytes. {ECO:0000250|UniProtKB:Q9H1Y3}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9H1Y3};
CC Multi-pass membrane protein {ECO:0000255}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9H1Y3}.
CC -!- TISSUE SPECIFICITY: Expressed in the eye (at protein level)
CC (PubMed:30284927). Expressed in tracheal airway smooth muscle
CC (PubMed:30284927). Expressed in brown adipocyte tissue; expression
CC becomes more abundant during differentiation (PubMed:32040503).
CC Strongly expressed in brain (PubMed:10234000). Highly expressed in the
CC preoptic area and paraventricular nucleus of the hypothalamus
CC (PubMed:10234000). Shows highly patterned expression in other regions
CC of the brain, being enriched in selected regions of the cerebral
CC cortex, cerebellar Purkinje cells, a subset of striatal neurons,
CC selected thalamic nuclei, and a subset of interneurons in the ventral
CC horn of the spinal cord (PubMed:10234000).
CC {ECO:0000269|PubMed:10234000, ECO:0000269|PubMed:30284927,
CC ECO:0000269|PubMed:32040503}.
CC -!- DEVELOPMENTAL STAGE: Expressed at substantial levels in the dorsal pons
CC at 18.5 dpc (PubMed:10234000). Expressed in Purkinje cells at P4, with
CC expression becoming striped at P20 (PubMed:10234000). Expressed in the
CC cerebral cortex from 18.5 dpc with a rostrocaudal gradient of
CC expression becoming evident at P20 (PubMed:10234000).
CC {ECO:0000269|PubMed:10234000}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype (PubMed:32040503). Increased
CC weight gain on a high fat diet, as a result of increased fat mass and
CC increased insulin resistance (PubMed:32040503). Increased basal glucose
CC uptake in brown adipocytes, potentially as a result of decreased GLUT1
CC expression (PubMed:32040503). Significantly reduced lipocytic rate,
CC mitochondrial DNA expression and cytochrome C oxidase activity in brown
CC adipocyte tissues (PubMed:32040503). Loss of light-mediated increase in
CC glucose uptake, mitochondrial respiration, thermogenic capacity and
CC lipid metabolism-related gene expression in brown adipocyte tissues
CC (PubMed:32040503). Impaired maximum thermogenic capacity with reduced
CC heat production and reduced oxygen consumption in response to
CC norepinephrine treatment in brown adipocytes (PubMed:32040503).
CC {ECO:0000269|PubMed:32040503}.
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; AF140241; AAD32670.1; -; mRNA.
DR EMBL; AF482427; AAO15719.1; -; Genomic_DNA.
DR EMBL; AK043135; BAC31471.1; -; mRNA.
DR EMBL; AK132822; BAE21380.1; -; mRNA.
DR CCDS; CCDS15549.1; -.
DR RefSeq; NP_034228.1; NM_010098.3.
DR AlphaFoldDB; Q9WUK7; -.
DR SMR; Q9WUK7; -.
DR STRING; 10090.ENSMUSP00000027809; -.
DR GlyGen; Q9WUK7; 2 sites.
DR PhosphoSitePlus; Q9WUK7; -.
DR PaxDb; Q9WUK7; -.
DR PRIDE; Q9WUK7; -.
DR ProteomicsDB; 293518; -.
DR Antibodypedia; 34703; 247 antibodies from 29 providers.
DR DNASU; 13603; -.
DR Ensembl; ENSMUST00000027809; ENSMUSP00000027809; ENSMUSG00000026525.
DR GeneID; 13603; -.
DR KEGG; mmu:13603; -.
DR UCSC; uc007dtq.2; mouse.
DR CTD; 23596; -.
DR MGI; MGI:1338022; Opn3.
DR VEuPathDB; HostDB:ENSMUSG00000026525; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01030000234631; -.
DR HOGENOM; CLU_009579_3_0_1; -.
DR InParanoid; Q9WUK7; -.
DR OMA; KMCFLMV; -.
DR OrthoDB; 940057at2759; -.
DR PhylomeDB; Q9WUK7; -.
DR TreeFam; TF324998; -.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR Reactome; R-MMU-419771; Opsins.
DR BioGRID-ORCS; 13603; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Opn3; mouse.
DR PRO; PR:Q9WUK7; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9WUK7; protein.
DR Bgee; ENSMUSG00000026525; Expressed in epididymal fat pad and 178 other tissues.
DR Genevisible; Q9WUK7; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0001750; C:photoreceptor outer segment; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005502; F:11-cis retinal binding; ISS:UniProtKB.
DR GO; GO:0005503; F:all-trans retinal binding; ISS:UniProtKB.
DR GO; GO:0008020; F:G protein-coupled photoreceptor activity; IBA:GO_Central.
DR GO; GO:0071482; P:cellular response to light stimulus; IBA:GO_Central.
DR GO; GO:0071492; P:cellular response to UV-A; ISO:MGI.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0030216; P:keratinocyte differentiation; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0048022; P:negative regulation of melanin biosynthetic process; ISS:UniProtKB.
DR GO; GO:0007602; P:phototransduction; IBA:GO_Central.
DR GO; GO:1901857; P:positive regulation of cellular respiration; IMP:UniProtKB.
DR GO; GO:0046326; P:positive regulation of glucose import; IMP:UniProtKB.
DR GO; GO:0048023; P:positive regulation of melanin biosynthetic process; ISS:UniProtKB.
DR GO; GO:0009637; P:response to blue light; IMP:UniProtKB.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR027430; Retinal_BS.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
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 Cell membrane; Chromophore; Cytoplasm; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane; Palmitate;
KW Photoreceptor protein; Receptor; Reference proteome; Retinal protein;
KW Sensory transduction; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..400
FT /note="Opsin-3"
FT /id="PRO_0000197814"
FT TOPO_DOM 1..38
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 39..63
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 64..75
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 76..100
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 101..115
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..135
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 136..151
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..175
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 176..199
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..227
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 228..253
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 254..277
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 278..285
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 286..310
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 311..400
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 297
FT /note="N6-(retinylidene)lysine"
FT LIPID 323
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 5
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 112..186
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT MUTAGEN 136..138
FT /note="ERY->RDR: Reduced basal glucose uptake and glucose-
FT dependent mitochondrial respiration."
FT /evidence="ECO:0000269|PubMed:32040503"
SQ SEQUENCE 400 AA; 44947 MW; AAFA81386C48BDB5 CRC64;
MYSGNRSGDQ GYWEDGAGAE GAAPAGTRSP APLFSPTAYE RLALLLGCLA LLGVGGNLLV
LLLYSKFPRL RTPTHLFLVN LSLGDLLVSL FGVTFTFASC LRNGWVWDAV GCAWDGFSGS
LFGFVSITTL TVLAYERYIR VVHARVINFS WAWRAITYIW LYSLAWAGAP LLGWNRYILD
IHGLGCTVDW RSKDANDSSF VLFLFLGCLV VPVGIIAHCY GHILYSVRML RCVEDLQTIQ
VIKMLRYEKK VAKMCFLMAF VFLTCWMPYI VTRFLVVNGY GHLVTPTVSI VSYLFAKSST
VYNPVIYIFM NRKFRRSLLQ LLCFRLLRCQ RPAKNLPAAE SEMHIRPIVM SQKDGDRPKK
KVTFNSSSII FIITSDESLS VEDSDRSSAS KVDVIQVRPL
