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Database: UniProt/SWISS-PROT
Entry: OPN4_FELCA
LinkDB: OPN4_FELCA
Original site: OPN4_FELCA 
ID   OPN4_FELCA              Reviewed;         487 AA.
AC   Q5YKK9;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   27-MAR-2024, entry version 98.
DE   RecName: Full=Melanopsin;
DE   AltName: Full=Opsin-4;
GN   Name=OPN4;
OS   Felis catus (Cat) (Felis silvestris catus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX   NCBI_TaxID=9685;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   PubMed=15842746; DOI=10.1017/s0952523805001069;
RA   Semo M., Munoz Llamosas M., Foster R.G., Jeffery G.;
RT   "Melanopsin (Opn4) positive cells in the cat retina are randomly
RT   distributed across the ganglion cell layer.";
RL   Vis. Neurosci. 22:111-116(2005).
CC   -!- FUNCTION: Photoreceptor that binds cis-retinaldehydes (By similarity).
CC       Contributes to pupillar reflex, photoentrainment and other non-image
CC       forming responses to light (By similarity). May be involved in the
CC       optokinetic visual tracking response (By similarity). May be involved
CC       in the regulation of retinal hyaloid vessel growth and regression (By
CC       similarity). {ECO:0000250|UniProtKB:Q9QXZ9}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9QXZ9};
CC       Multi-pass membrane protein {ECO:0000255}. Cell projection, axon
CC       {ECO:0000250|UniProtKB:Q9QXZ9}. Cell projection, dendrite
CC       {ECO:0000250|UniProtKB:Q9QXZ9}. Perikaryon
CC       {ECO:0000250|UniProtKB:Q9QXZ9}.
CC   -!- TISSUE SPECIFICITY: Eye. Expression is restricted within the ganglion
CC       cell layer. {ECO:0000269|PubMed:15842746}.
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; AY382594; AAR36861.1; -; mRNA.
DR   RefSeq; NP_001009325.1; NM_001009325.2.
DR   AlphaFoldDB; Q5YKK9; -.
DR   SMR; Q5YKK9; -.
DR   STRING; 9685.ENSFCAP00000051489; -.
DR   PaxDb; 9685-ENSFCAP00000013930; -.
DR   Ensembl; ENSFCAT00000057256.2; ENSFCAP00000051489.2; ENSFCAG00000015018.6.
DR   GeneID; 493921; -.
DR   KEGG; fca:493921; -.
DR   VGNC; VGNC:103737; OPN4.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT01100000263502; -.
DR   HOGENOM; CLU_009579_3_12_1; -.
DR   InParanoid; Q5YKK9; -.
DR   OrthoDB; 3432893at2759; -.
DR   Proteomes; UP000011712; Chromosome D2.
DR   GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR   GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; TAS:UniProtKB.
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; IEA:Ensembl.
DR   GO; GO:0005502; F:11-cis retinal binding; ISS:UniProtKB.
DR   GO; GO:0008020; F:G protein-coupled photoreceptor activity; ISS: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; IEA:Ensembl.
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:0007634; P:optokinetic behavior; ISS:UniProtKB.
DR   GO; GO:0007602; P:phototransduction; ISS:UniProtKB.
DR   GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
DR   GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl.
DR   GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR   GO; GO:0043052; P:thermotaxis; IEA:Ensembl.
DR   GO; GO:0007601; P:visual perception; IEA:InterPro.
DR   CDD; cd15336; 7tmA_Melanopsin; 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; IPR001760; Opsin.
DR   InterPro; IPR027430; Retinal_BS.
DR   PANTHER; PTHR24240:SF72; MELANOPSIN; 1.
DR   PANTHER; PTHR24240; OPSIN; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00238; OPSIN.
DR   SMART; SM01381; 7TM_GPCR_Srsx; 1.
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.
PE   2: Evidence at transcript level;
KW   Biological rhythms; Cell membrane; Cell projection; Chromophore;
KW   Disulfide bond; G-protein coupled receptor; Membrane;
KW   Photoreceptor protein; Receptor; Reference proteome; Retinal protein;
KW   Sensory transduction; Transducer; Transmembrane; Transmembrane helix.
FT   CHAIN           1..487
FT                   /note="Melanopsin"
FT                   /id="PRO_0000226728"
FT   TOPO_DOM        1..67
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        68..88
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        89..102
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        103..123
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        124..139
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        140..160
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        161..183
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        184..204
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        205..233
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        234..254
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        255..291
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        292..312
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        313..327
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        328..348
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        349..487
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          436..459
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..37
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         335
FT                   /note="N6-(retinylidene)lysine"
FT                   /evidence="ECO:0000250"
FT   DISULFID        138..216
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   487 AA;  53681 MW;  B867E24B4D322D57 CRC64;
     MNPPSGPRTQ EPSCVATPAS PSRWDGYRSS TSSLDQPLPI SPTAARAQAA AWIPFPTVDV
     PDHAHYTLGT VILLVGLTGI LGNLMVIYTF CRSRGLRTPA NMFIINLAVS DFFMSFTQAP
     VFFASSLHKR WLFGEAGCEF YAFCGALFGI TSMITLMAIA LDRYLVITHP LATIGVVSKR
     RAALVLLGVW LYALAWSLPP FFGWSAYVPE GLLTSCSWDY MSFTPSVRAY TMLLFCFVFF
     LPLLVIVYCY IFIFRAIRET GQALQTFRAC EGGGRSPRQR QRLQREWKMA KIELLVILLF
     VLSWAPYSIV ALMAFAGYAH VLTPYMNSVP AVIAKASAIH NPIIYAITHP KYRMAIAQHL
     PCLGVLLGVS GQHTGPYASY RSTHRSTLSS QASDLSWISG RRRQASLGSE SEVGWMDTEA
     AAVWGAAQQV SGRFPCSQGL EDREAKAPVR PQGREAETPG QAMTMAMAPW DTPANCELPL
     HPGWAFH
//
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