ID   OPSG_MOUSE              Reviewed;         359 AA.
AC   O35599; Q548Z4;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   24-JAN-2024, entry version 159.
DE   RecName: Full=Medium-wave-sensitive opsin 1;
DE   AltName: Full=Green cone photoreceptor pigment;
DE   AltName: Full=Green-sensitive opsin;
DE            Short=M opsin;
DE   AltName: Full=Medium wavelength-sensitive cone opsin;
GN   Name=Opn1mw; Synonyms=Gcp;
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].
RX   PubMed=9238068; DOI=10.1073/pnas.94.16.8860;
RA   Sun H., Macke J.P., Nathans J.;
RT   "Mechanisms of spectral tuning in the mouse green cone pigment.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:8860-8865(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC   STRAIN=BALB/cJ, and C57BL/10;
RX   PubMed=11055434; DOI=10.1016/s0896-6273(00)00062-3;
RA   Applebury M.L., Antoch M.P., Baxter L.C., Chun L.Y., Falk J.D.,
RA   Farhangfar F., Kage K., Krzystolik M.G., Lyass L.A., Robbins J.T.;
RT   "The murine cone photoreceptor: a single cone type expresses both S and M
RT   opsins with retinal spatial patterning.";
RL   Neuron 27:513-523(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Retina;
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   [4]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=23001562; DOI=10.1093/hmg/dds398;
RA   Alves C.H., Sanz A.S., Park B., Pellissier L.P., Tanimoto N., Beck S.C.,
RA   Huber G., Murtaza M., Richard F., Sridevi Gurubaran I., Garcia Garrido M.,
RA   Levelt C.N., Rashbass P., Le Bivic A., Seeliger M.W., Wijnholds J.;
RT   "Loss of CRB2 in the mouse retina mimics human retinitis pigmentosa due to
RT   mutations in the CRB1 gene.";
RL   Hum. Mol. Genet. 22:35-50(2013).
RN   [5]
RP   TISSUE SPECIFICITY, AND GLYCOSYLATION.
RX   PubMed=30948514; DOI=10.1074/jbc.ra118.006835;
RA   Salom D., Jin H., Gerken T.A., Yu C., Huang L., Palczewski K.;
RT   "Human red and green cone opsins are O-glycosylated at an N-terminal
RT   Ser/Thr-rich domain conserved in vertebrates.";
RL   J. Biol. Chem. 294:8123-8133(2019).
CC   -!- FUNCTION: Visual pigments are the light-absorbing molecules that
CC       mediate vision. They consist of an apoprotein, opsin, covalently linked
CC       to cis-retinal. May increase spectral sensitivity in dim light.
CC       {ECO:0000269|PubMed:11055434}.
CC   -!- SUBUNIT: Monomer. Homodimer. Homotetramer.
CC       {ECO:0000250|UniProtKB:P04001}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P04001};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Expressed in retina (at protein level)
CC       (PubMed:30948514). Expressed in cone photoreceptor cells (at protein
CC       level) (PubMed:11055434). {ECO:0000269|PubMed:11055434,
CC       ECO:0000269|PubMed:30948514}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the retinal outer nuclear layer and
CC       the inner nuclear layer at postnatal day 10.
CC       {ECO:0000269|PubMed:23001562}.
CC   -!- PTM: N-glycosylated (PubMed:30948514). O-glycosylated
CC       (PubMed:30948514). {ECO:0000269|PubMed:30948514}.
CC   -!- PTM: Phosphorylated on some or all of the serine and threonine residues
CC       present in the C-terminal region. {ECO:0000250}.
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; AF011389; AAB64302.1; -; mRNA.
DR   EMBL; AF190672; AAG17991.1; -; mRNA.
DR   EMBL; AF191085; AAG17992.1; -; Genomic_DNA.
DR   EMBL; AF191080; AAG17992.1; JOINED; Genomic_DNA.
DR   EMBL; AF191081; AAG17992.1; JOINED; Genomic_DNA.
DR   EMBL; AF191082; AAG17992.1; JOINED; Genomic_DNA.
DR   EMBL; AF191083; AAG17992.1; JOINED; Genomic_DNA.
DR   EMBL; AF191084; AAG17992.1; JOINED; Genomic_DNA.
DR   EMBL; BC014826; AAH14826.1; -; mRNA.
DR   CCDS; CCDS30220.1; -.
DR   RefSeq; NP_032132.1; NM_008106.2.
DR   AlphaFoldDB; O35599; -.
DR   SMR; O35599; -.
DR   STRING; 10090.ENSMUSP00000033771; -.
DR   GlyCosmos; O35599; 1 site, No reported glycans.
DR   GlyGen; O35599; 1 site.
DR   PhosphoSitePlus; O35599; -.
DR   PaxDb; 10090-ENSMUSP00000033771; -.
DR   ProteomicsDB; 294394; -.
DR   DNASU; 14539; -.
DR   Ensembl; ENSMUST00000033771.11; ENSMUSP00000033771.5; ENSMUSG00000031394.12.
DR   GeneID; 14539; -.
DR   KEGG; mmu:14539; -.
DR   UCSC; uc009tnv.1; mouse.
DR   AGR; MGI:1097692; -.
DR   CTD; 2652; -.
DR   MGI; MGI:1097692; Opn1mw.
DR   VEuPathDB; HostDB:ENSMUSG00000031394; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT01030000234549; -.
DR   HOGENOM; CLU_009579_3_0_1; -.
DR   InParanoid; O35599; -.
DR   OMA; EWGKQSF; -.
DR   OrthoDB; 5350930at2759; -.
DR   PhylomeDB; O35599; -.
DR   TreeFam; TF324998; -.
DR   Reactome; R-MMU-2187335; The retinoid cycle in cones (daylight vision).
DR   Reactome; R-MMU-418594; G alpha (i) signalling events.
DR   Reactome; R-MMU-419771; Opsins.
DR   BioGRID-ORCS; 14539; 2 hits in 77 CRISPR screens.
DR   PRO; PR:O35599; -.
DR   Proteomes; UP000000589; Chromosome X.
DR   RNAct; O35599; Protein.
DR   Bgee; ENSMUSG00000031394; Expressed in retinal neural layer and 12 other cell types or tissues.
DR   ExpressionAtlas; O35599; baseline and differential.
DR   GO; GO:0001750; C:photoreceptor outer segment; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0008020; F:G protein-coupled photoreceptor activity; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR   GO; GO:0009881; F:photoreceptor activity; ISO:MGI.
DR   GO; GO:0071482; P:cellular response to light stimulus; IBA:GO_Central.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0007602; P:phototransduction; IBA:GO_Central.
DR   GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
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; IPR001760; Opsin.
DR   InterPro; IPR000378; Opsin_red/grn.
DR   InterPro; IPR027430; Retinal_BS.
DR   PANTHER; PTHR24240:SF17; MEDIUM-WAVE-SENSITIVE OPSIN 1-RELATED; 1.
DR   PANTHER; PTHR24240; OPSIN; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00238; OPSIN.
DR   PRINTS; PR00575; OPSINREDGRN.
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; O35599; MM.
PE   1: Evidence at protein level;
KW   Cell membrane; Chromophore; Disulfide bond; G-protein coupled receptor;
KW   Glycoprotein; Membrane; Phosphoprotein; Photoreceptor protein; Receptor;
KW   Reference proteome; Retinal protein; Sensory transduction; Transducer;
KW   Transmembrane; Transmembrane helix; Vision.
FT   CHAIN           1..359
FT                   /note="Medium-wave-sensitive opsin 1"
FT                   /id="PRO_0000197786"
FT   TOPO_DOM        1..47
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        48..72
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        73..84
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        85..110
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        111..124
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        125..144
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        145..163
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        164..187
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        188..213
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        214..241
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        242..263
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        264..287
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        288..295
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        296..320
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        321..359
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          12..38
FT                   /note="Required for 11-cis-retinal regeneration"
FT                   /evidence="ECO:0000250|UniProtKB:P04001"
FT   MOD_RES         307
FT                   /note="N6-(retinylidene)lysine"
FT   CARBOHYD        29
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        121..198
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   359 AA;  40218 MW;  1BB5F531A6FAE357 CRC64;
     MAQRLTGEQT LDHYEDSTHA SIFTYTNSNS TKGPFEGPNY HIAPRWVYHL TSTWMILVVV
     ASVFTNGLVL AATMRFKKLR HPLNWILVNL AVADLAETII ASTISVVNQI YGYFVLGHPL
     CVIEGYIVSL CGITGLWSLA IISWERWLVV CKPFGNVRFD AKLATVGIVF SWVWAAIWTA
     PPIFGWSRYW PYGLKTSCGP DVFSGTSYPG VQSYMMVLMV TCCIFPLSII VLCYLQVWLA
     IRAVAKQQKE SESTQKAEKE VTRMVVVMVF AYCLCWGPYT FFACFATAHP GYAFHPLVAS
     LPSYFAKSAT IYNPIIYVFM NRQFRNCILH LFGKKVDDSS ELSSTSKTEV SSVSSVSPA
//