ID   OPN5_HUMAN              Reviewed;         354 AA.
AC   Q6U736; A0AV33; Q5T5B9; Q5T886; Q7Z603; Q86SL5;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 3.
DT   24-JAN-2024, entry version 149.
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;
DE   AltName: Full=Transmembrane protein 13;
GN   Name=OPN5; Synonyms=GPR136, PGR12, TMEM13;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
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   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 119-231.
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 GENOMIC DNA].
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA   Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA   Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA   Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA   Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA   French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA   Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA   Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA   Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA   Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA   Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA   Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA   Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA   Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA   Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA   Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA   Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA   Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA   Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA   West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA   Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA   Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA   Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [6]
RP   FUNCTION.
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).
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 (By similarity). Preferentially binds the chromophore 11-cis
CC       retinal and is a bistable protein that displays emission peaks at 380
CC       nm (UVA light) and 470 nm (blue light) (PubMed:22043319). Required for
CC       the light-response in the inner plexiform layer, and contributes to the
CC       regulation of the light-response in the nerve fiber layer, via
CC       phosphorylated DAT/SLC6A3 dopamine uptake (By similarity). Involved in
CC       local corneal and retinal circadian rhythm photoentrainment via
CC       modulation of the UVA light-induced phase-shift of the retina clock (By
CC       similarity). Acts as a circadian photoreceptor in the outer ear, via
CC       modulation of circadian clock-gene expression in response to violet
CC       light during the light-to-dark transition phase and night phase of the
CC       circadian cycle (By similarity). Required in the retina to negatively
CC       regulate hyaloid vessel regression during postnatal development via
CC       light-dependent OPN5-SLC32A1-DRD2-VEGFR2 signaling (By similarity).
CC       Involved in the light-dependent regulation of retina and vitreous
CC       compartment dopamine levels (By similarity).
CC       {ECO:0000250|UniProtKB:Q6VZZ7, ECO:0000269|PubMed:22043319}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Detected in brain and retina and cell lines derived
CC       from neural retina. {ECO:0000269|PubMed:14623103}.
CC   -!- PTM: It is uncertain whether Cys-315 or Cys-316 is palmitoylated.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Opsin
CC       subfamily. {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAI20454.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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; AY377391; AAR21109.1; -; mRNA.
DR   EMBL; AY288419; AAP72128.1; -; mRNA.
DR   EMBL; AY255615; AAO85127.1; -; mRNA.
DR   EMBL; AL356421; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL161622; CAI20454.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BC126194; AAI26195.1; -; mRNA.
DR   EMBL; BC126198; AAI26199.1; -; mRNA.
DR   CCDS; CCDS4923.1; -.
DR   RefSeq; NP_859528.1; NM_181744.3.
DR   AlphaFoldDB; Q6U736; -.
DR   SMR; Q6U736; -.
DR   BioGRID; 128717; 3.
DR   STRING; 9606.ENSP00000360255; -.
DR   ChEMBL; CHEMBL4523878; -.
DR   GlyCosmos; Q6U736; 1 site, No reported glycans.
DR   GlyGen; Q6U736; 1 site.
DR   iPTMnet; Q6U736; -.
DR   PhosphoSitePlus; Q6U736; -.
DR   BioMuta; OPN5; -.
DR   DMDM; 116242690; -.
DR   PaxDb; 9606-ENSP00000360255; -.
DR   Antibodypedia; 16965; 252 antibodies from 30 providers.
DR   DNASU; 221391; -.
DR   Ensembl; ENST00000371211.7; ENSP00000360255.2; ENSG00000124818.16.
DR   GeneID; 221391; -.
DR   KEGG; hsa:221391; -.
DR   MANE-Select; ENST00000371211.7; ENSP00000360255.2; NM_181744.4; NP_859528.1.
DR   UCSC; uc003ozc.4; human.
DR   AGR; HGNC:19992; -.
DR   CTD; 221391; -.
DR   DisGeNET; 221391; -.
DR   GeneCards; OPN5; -.
DR   HGNC; HGNC:19992; OPN5.
DR   HPA; ENSG00000124818; Tissue enriched (testis).
DR   MIM; 609042; gene.
DR   neXtProt; NX_Q6U736; -.
DR   OpenTargets; ENSG00000124818; -.
DR   PharmGKB; PA134942887; -.
DR   VEuPathDB; HostDB:ENSG00000124818; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT01100000263524; -.
DR   InParanoid; Q6U736; -.
DR   OrthoDB; 3044063at2759; -.
DR   PhylomeDB; Q6U736; -.
DR   TreeFam; TF324998; -.
DR   PathwayCommons; Q6U736; -.
DR   Reactome; R-HSA-418594; G alpha (i) signalling events.
DR   Reactome; R-HSA-419771; Opsins.
DR   BioGRID-ORCS; 221391; 15 hits in 1141 CRISPR screens.
DR   ChiTaRS; OPN5; human.
DR   GeneWiki; OPN5; -.
DR   GenomeRNAi; 221391; -.
DR   Pharos; Q6U736; Tbio.
DR   PRO; PR:Q6U736; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; Q6U736; Protein.
DR   Bgee; ENSG00000124818; Expressed in male germ line stem cell (sensu Vertebrata) in testis and 42 other cell types or tissues.
DR   ExpressionAtlas; Q6U736; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0005502; F:11-cis retinal binding; IMP:UniProtKB.
DR   GO; GO:0008020; F:G protein-coupled photoreceptor activity; ISS:UniProtKB.
DR   GO; GO:0071482; P:cellular response to light stimulus; ISS:UniProtKB.
DR   GO; GO:0071492; P:cellular response to UV-A; IDA:UniProtKB.
DR   GO; GO:0043153; P:entrainment of circadian clock by photoperiod; ISS:UniProtKB.
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:0007602; P:phototransduction; ISS:UniProtKB.
DR   GO; GO:0007604; P:phototransduction, UV; IMP:UniProtKB.
DR   GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR   CDD; cd15074; 7tmA_Opsin5_neuropsin; 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; IPR002962; Peropsin.
DR   InterPro; IPR027430; Retinal_BS.
DR   PANTHER; PTHR24240; OPSIN; 1.
DR   PANTHER; PTHR24240:SF0; OPSIN-5; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR01244; PEROPSIN.
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.
DR   Genevisible; Q6U736; HS.
PE   1: Evidence at protein level;
KW   Cell membrane; Chromophore; Disulfide bond; G-protein coupled receptor;
KW   Glycoprotein; Lipoprotein; Membrane; Palmitate; Photoreceptor protein;
KW   Receptor; Reference proteome; Retinal protein; Sensory transduction;
KW   Transducer; Transmembrane; Transmembrane helix; Vision.
FT   CHAIN           1..354
FT                   /note="Opsin-5"
FT                   /id="PRO_0000197817"
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..353
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
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   CONFLICT        84..86
FT                   /note="Missing (in Ref. 2; AAP72128)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        133..145
FT                   /note="Missing (in Ref. 3; AAO85127)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        353..354
FT                   /note="WE -> V (in Ref. 2; AAP72128 and 4; CAI20454)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   354 AA;  39727 MW;  BBF03FA2C0741005 CRC64;
     MALNHTALPQ DERLPHYLRD GDPFASKLSW EADLVAGFYL TIIGILSTFG NGYVLYMSSR
     RKKKLRPAEI MTINLAVCDL GISVVGKPFT IISCFCHRWV FGWIGCRWYG WAGFFFGCGS
     LITMTAVSLD RYLKICYLSY GVWLKRKHAY ICLAAIWAYA SFWTTMPLVG LGDYVPEPFG
     TSCTLDWWLA QASVGGQVFI LNILFFCLLL PTAVIVFSYV KIIAKVKSSS KEVAHFDSRI
     HSSHVLEMKL TKVAMLICAG FLIAWIPYAV VSVWSAFGRP DSIPIQLSVV PTLLAKSAAM
     YNPIIYQVID YKFACCQTGG LKATKKKSLE GFRLHTVTTV RKSSAVLEIH EEWE
//