OPN4_PODSI
ID OPN4_PODSI Reviewed; 475 AA.
AC Q4U4D2;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 2.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Melanopsin;
DE AltName: Full=Opsin-4;
GN Name=OPN4;
OS Podarcis siculus (Italian wall lizard).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Laterata;
OC Lacertibaenia; Lacertidae; Podarcis.
OX NCBI_TaxID=65484;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAY34941.2}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=16688437; DOI=10.1007/s00114-006-0119-9;
RA Frigato E., Vallone D., Bertolucci C., Foulkes N.S.;
RT "Isolation and characterization of melanopsin and pinopsin expression
RT within photoreceptive sites of reptiles.";
RL Naturwissenschaften 93:379-385(2006).
CC -!- FUNCTION: Photoreceptor implicated in non-image-forming responses to
CC light. May be able to isomerize covalently bound all-trans retinal back
CC to 11-cis retinal (By similarity). {ECO:0000250|UniProtKB:Q9QXZ9}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9QXZ9};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Highest level in the lateral eye. Low level in the
CC brain. {ECO:0000269|PubMed:16688437}.
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; DQ013043; AAY34941.2; -; mRNA.
DR AlphaFoldDB; Q4U4D2; -.
DR SMR; Q4U4D2; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0009881; F:photoreceptor activity; IEA:UniProtKB-KW.
DR GO; GO:0007602; P:phototransduction; IEA:UniProtKB-KW.
DR GO; GO:0007601; P:visual perception; IEA:InterPro.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR001760; Opsin.
DR InterPro; IPR027430; Retinal_BS.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00238; OPSIN.
DR SMART; SM01381; 7TM_GPCR_Srsx; 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 Cell membrane; Chromophore; Disulfide bond; G-protein coupled receptor;
KW Glycoprotein; Membrane; Photoreceptor protein; Receptor; Retinal protein;
KW Sensory transduction; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..475
FT /note="Melanopsin"
FT /id="PRO_0000271893"
FT TOPO_DOM 1..21
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 22..42
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 43..53
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 54..74
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 75..90
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 91..111
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 112..134
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 135..155
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 156..187
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 188..208
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 209..240
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 241..261
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 262..276
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 277..297
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 298..475
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 370..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 445..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..388
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 284
FT /note="N6-(retinylidene)lysine"
FT /evidence="ECO:0000250"
FT CARBOHYD 178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 89..167
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 475 AA; 53068 MW; 6382B0BC171B7D16 CRC64;
MGTQHRIKVD VPDRVLYTVG SCVLVIGSIG ITGNLLVLYA FYSNKRLRTP ANYFIMNLAA
SDFLMSATQA PICFLNSMHT EWILGDIGCN FYVFCGALFG ITSMMTLLAI SVDRYCVITK
PLQSIKRSSK KRSCIIIAFV WLYSLGWSVC PLFGWSSYIP EGLMISCTWD YVSYSPANRS
YTMMLCCFVF FIPLIIIFHC YLFMFLAIRS TGRNVQKLGS TYNRKSNVSQ SVKSEWKLAK
IAFVAIVVFV LSWSPYACVT LIAWAGYAKT LNPYSKSVPA VIAKASAIYN PIIYAIIHPR
YRRTIRSAVP CLRFLIRISP SDLSTSSVNE SSFRASMSSR HSFAARNKSS CVSSISAAET
TWSDMELEPV EAARKKQQPH RSRSFSKQAE EETGLLLKTQ SCNVLTGEKV AVSSISLHDP
FERSFGENAP ELLLRPSCLR TSSLPFGLNS SSTEENADTS DMEVQEQHQM EASSH
