OPN5_MOUSE
ID OPN5_MOUSE Reviewed; 377 AA.
AC Q6VZZ7; Q059L5; Q7TQP1; Q80T51; Q8BYI2;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Opsin-5;
DE AltName: Full=G-protein coupled receptor 136;
DE AltName: Full=G-protein coupled receptor PGR12;
DE AltName: Full=Neuropsin;
GN Name=Opn5; Synonyms=Gpr136, Pgr12;
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 2).
RX PubMed=14623098; DOI=10.1016/s0014-5793(03)01196-7;
RA Fredriksson R., Hoeglund P.J., Gloriam D.E.I., Lagerstroem M.C.,
RA Schioeth H.B.;
RT "Seven evolutionarily conserved human rhodopsin G protein-coupled receptors
RT lacking close relatives.";
RL FEBS Lett. 554:381-388(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 154-228.
RX PubMed=12679517; DOI=10.1073/pnas.0230374100;
RA Vassilatis D.K., Hohmann J.G., Zeng H., Li F., Ranchalis J.E.,
RA Mortrud M.T., Brown A., Rodriguez S.S., Weller J.R., Wright A.C.,
RA Bergmann J.E., Gaitanaris G.A.;
RT "The G protein-coupled receptor repertoires of human and mouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:4903-4908(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 270-377 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Spinal cord;
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 [5]
RP IDENTIFICATION (ISOFORM 1), AND TISSUE SPECIFICITY.
RC STRAIN=C3H/HeJ;
RX PubMed=14623103; DOI=10.1016/s0014-5793(03)01212-2;
RA Tarttelin E.E., Bellingham J., Hankins M.W., Foster R.G., Lucas R.J.;
RT "Neuropsin (Opn5): a novel opsin identified in mammalian neural tissue.";
RL FEBS Lett. 554:410-416(2003).
RN [6]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=22043319; DOI=10.1371/journal.pone.0026388;
RA Kojima D., Mori S., Torii M., Wada A., Morishita R., Fukada Y.;
RT "UV-sensitive photoreceptor protein OPN5 in humans and mice.";
RL PLoS ONE 6:e26388-e26388(2011).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, 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 FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
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 FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
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: G-protein coupled receptor which selectively activates G(i)
CC type G proteins via ultraviolet A (UVA) light-mediated activation in
CC the retina (PubMed:22043319). Preferentially binds the chromophore 11-
CC cis retinal and is a bistable protein that displays emission peaks at
CC 380 nm (UVA light) and 470 nm (blue light) (PubMed:22043319,
CC PubMed:31607531). Required for the light-response in the inner
CC plexiform layer, and contributes to the regulation of the light-
CC response in the nerve fiber layer, via phosphorylated DAT/SLC6A3
CC dopamine uptake (PubMed:30936473). Involved in local corneal and
CC retinal circadian rhythm photoentrainment via modulation of the UVA
CC light-induced phase-shift of the retina clock (PubMed:26392540,
CC PubMed:30240620). Acts as a circadian photoreceptor in the outer ear
CC and vibrissal pads, via modulation of circadian clock-gene expression
CC in response to violet light during the light-to-dark transition phase
CC and night phase of the circadian cycle (PubMed:31607531). Required in
CC the retina to negatively regulate hyaloid vessel regression during
CC postnatal development via light-dependent OPN5-SLC32A1-DRD2-VEGFR2
CC signaling (PubMed:30936473). Involved in the light-dependent regulation
CC of retina and vitreous compartment dopamine levels (PubMed:30936473).
CC {ECO:0000269|PubMed:22043319, ECO:0000269|PubMed:26392540,
CC ECO:0000269|PubMed:30240620, ECO:0000269|PubMed:30936473,
CC ECO:0000269|PubMed:31607531}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6VZZ7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6VZZ7-2; Sequence=VSP_014041, VSP_014042;
CC -!- TISSUE SPECIFICITY: Expressed in the brain (at protein level)
CC (PubMed:14623103, PubMed:22043319). Weakly expressed in the skin and
CC liver (at protein level) (PubMed:22043319). Abundantly expressed in
CC striated muscle cells (PubMed:22043319). Expressed in Math7/Atok7-
CC dependent retinal ganglion cells in the ganglion cell layer (at protein
CC level) (PubMed:14623103, PubMed:22043319, PubMed:26392540,
CC PubMed:30240620, PubMed:31607531). Additionally expressed in horizontal
CC and amacrine cells in the inner nuclear layer of the retina (at protein
CC level) (PubMed:22043319). Expressed around the base of hair follicles
CC and in epidermal and sebaceous gland cells of the outer ear (at protein
CC level) (PubMed:22043319, PubMed:31607531). Abundantly expressed in
CC vibrissae hair follicles and weakly expressed in the vibrissae skin
CC pad, dorsal back skin, and tail (PubMed:31607531).
CC {ECO:0000269|PubMed:14623103, ECO:0000269|PubMed:22043319,
CC ECO:0000269|PubMed:26392540, ECO:0000269|PubMed:30240620,
CC ECO:0000269|PubMed:31607531}.
CC -!- DEVELOPMENTAL STAGE: Expressed weakly in the inner retina at postnatal
CC day 5 (P5), with expression becoming abundant in retinal ganglion cells
CC at P8 (PubMed:30936473). Expressed throughout the retinal sublaminae
CC layers, with abundant expression in the ganglion cell layer and nerve
CC fiber layer at P12 (PubMed:30936473). Expressed in ganglion cells in
CC the optic tracts, superior colliculus and lateral geniculate nucleus of
CC the brain at P28 (PubMed:30936473). Expressed around the base of hair
CC follicles in the dorsal ear skin, in the vibrissal nose pad, and weakly
CC expressed below the epidermis in the vibrissal nose pad at P8
CC (PubMed:31607531). {ECO:0000269|PubMed:30936473,
CC ECO:0000269|PubMed:31607531}.
CC -!- PTM: It is uncertain whether Cys-315 or Cys-316 is palmitoylated.
CC {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Ultrastructure of the retina is normal
CC (PubMed:30936473, PubMed:30240620, PubMed:26392540). Newborn mice show
CC normal hyaloid vessel numbers and normal vessel cellularity
CC (PubMed:30936473). Retinas show normal expression patterns of rod and
CC cone opsins including Opn4 (PubMed:26392540, PubMed:30240620).
CC Decreased activated Vegfr2 in the hyaloid vessels and increased
CC activated Akt1 at P5 (PubMed:30936473). Reduced levels of dopamine in
CC the retina, however increased levels in the vitreous at P6
CC (PubMed:30936473). Reduced number of hyaloid blood vessels due to
CC precocious regression, however no change in abundance of Vegfa or Flt1
CC at P8 (PubMed:30936473). Expression of tyrosine hydroxylase Th in
CC retinal cell processes at P8, with increased expression in developed
CC dopaminergic amacrine cells at P15 (PubMed:30936473). Loss of retinal
CC and corneal circadian rhythm photoentrainment (PubMed:26392540,
CC PubMed:30240620). Reduced UVA-induced phase-shift response and Fos
CC expression in the suprachiasmatic nuclei (SCN) in the brain
CC (PubMed:30240620). Abolishes retinaldehyde-dependent photoentrainment
CC in the dermal tissues of the outer ear and vibrissal pad
CC (PubMed:31607531). Loss of phase shifting activity in response to
CC violet light and expression of circadian clock-genes in the skin of the
CC outer ear during light-to-dark cycle, including Per1, Per2, Cry2, Dbp
CC and Nr1d2 (PubMed:31607531). Pde6b and Opn5 double knockout mice also
CC show loss of retinal ultrastructures and a more severe reduction in the
CC rate of circadian photoentrainment, light-induced phase-shift response
CC and Fos expression in the SCN (PubMed:30240620).
CC {ECO:0000269|PubMed:26392540, ECO:0000269|PubMed:30240620,
CC ECO:0000269|PubMed:30936473, ECO:0000269|PubMed:31607531}.
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; AY288426; AAP72135.1; -; mRNA.
DR EMBL; BC125611; AAI25612.1; -; mRNA.
DR EMBL; BC132010; AAI32011.1; -; mRNA.
DR EMBL; AY255592; AAO85104.1; -; mRNA.
DR EMBL; AK039525; BAC30373.1; -; mRNA.
DR EMBL; AY318865; AAR08201.1; -; mRNA.
DR EMBL; BK001605; DAA01972.1; -; Genomic_DNA.
DR CCDS; CCDS37619.1; -. [Q6VZZ7-1]
DR RefSeq; NP_861418.2; NM_181753.4. [Q6VZZ7-1]
DR AlphaFoldDB; Q6VZZ7; -.
DR SMR; Q6VZZ7; -.
DR STRING; 10090.ENSMUSP00000063542; -.
DR GlyGen; Q6VZZ7; 1 site.
DR PhosphoSitePlus; Q6VZZ7; -.
DR PaxDb; Q6VZZ7; -.
DR PRIDE; Q6VZZ7; -.
DR Antibodypedia; 16965; 234 antibodies from 30 providers.
DR DNASU; 353344; -.
DR Ensembl; ENSMUST00000068355; ENSMUSP00000063542; ENSMUSG00000043972. [Q6VZZ7-1]
DR GeneID; 353344; -.
DR KEGG; mmu:353344; -.
DR UCSC; uc008coq.1; mouse. [Q6VZZ7-1]
DR CTD; 221391; -.
DR MGI; MGI:2662912; Opn5.
DR VEuPathDB; HostDB:ENSMUSG00000043972; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01020000230391; -.
DR HOGENOM; CLU_009579_3_0_1; -.
DR InParanoid; Q6VZZ7; -.
DR OMA; WAYAAFW; -.
DR OrthoDB; 704940at2759; -.
DR PhylomeDB; Q6VZZ7; -.
DR TreeFam; TF324998; -.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR Reactome; R-MMU-419771; Opsins.
DR BioGRID-ORCS; 353344; 2 hits in 70 CRISPR screens.
DR ChiTaRS; Opn5; mouse.
DR PRO; PR:Q6VZZ7; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q6VZZ7; protein.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005502; F:11-cis retinal binding; IDA:MGI.
DR GO; GO:0008020; F:G protein-coupled photoreceptor activity; IMP:UniProtKB.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IDA:MGI.
DR GO; GO:0071482; P:cellular response to light stimulus; IMP:UniProtKB.
DR GO; GO:0071492; P:cellular response to UV-A; ISO:MGI.
DR GO; GO:0043153; P:entrainment of circadian clock by photoperiod; IMP:UniProtKB.
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:0007602; P:phototransduction; IMP:UniProtKB.
DR GO; GO:0007604; P:phototransduction, UV; IMP:UniProtKB.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR002962; Peropsin.
DR InterPro; IPR027430; Retinal_BS.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR01244; PEROPSIN.
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; Cell membrane; Chromophore; 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;
KW Vision.
FT CHAIN 1..377
FT /note="Opsin-5"
FT /id="PRO_0000197818"
FT TOPO_DOM 1..33
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 34..54
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 55..74
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..95
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 96..108
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 109..129
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 130..150
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 151..171
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 172..197
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 198..218
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 219..252
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 253..273
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 274..288
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 289..309
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 310..377
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 357..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 296
FT /note="N6-(retinylidene)lysine"
FT LIPID 315
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT LIPID 316
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 106..183
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT VAR_SEQ 353
FT /note="S -> V (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14623098"
FT /id="VSP_014041"
FT VAR_SEQ 354..377
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14623098"
FT /id="VSP_014042"
FT CONFLICT 84..86
FT /note="Missing (in Ref. 1; AAP72135)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 377 AA; 42018 MW; 26036DC9248B1596 CRC64;
MALNHTALPQ DERLPHYLRD EDPFASKLSW EADLVAGFYL TIIGILSTFG NGYVLYMSSR
RKKKLRPAEI MTINLAVCDL GISVVGKPFT IISCFCHRWV FGWFGCRWYG WAGFFFGCGS
LITMTAVSLD RYLKICYLSY GVWLKRKHAY ICLAVIWAYA SFWTTMPLVG LGDYAPEPFG
TSCTLDWWLA QASGGGQVFI LSILFFCLLL PTAVIVFSYA KIIAKVKSSS KEVAHFDSRI
HSSHVLEVKL TKVAMLICAG FLIAWIPYAV VSVWSAFGRP DSIPIQLSVV PTLLAKSAAM
YNPIIYQVID YRFACCQAGG LRGTKKKSLE DFRLHTVTAV RKSSAVLEIH PESSSRFTSA
HVMDGESHSN DGDCGKK
