OPN4_PHOSU
ID OPN4_PHOSU Reviewed; 469 AA.
AC Q5XXP2;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Melanopsin;
DE AltName: Full=Opsin-4;
GN Name=OPN4;
OS Phodopus sungorus (Striped hairy-footed hamster) (Djungarian hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Phodopus.
OX NCBI_TaxID=10044;
RN [1] {ECO:0000312|EMBL:AAU11506.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Retina {ECO:0000269|PubMed:15698924};
RX PubMed=15698924; DOI=10.1016/j.neulet.2004.11.029;
RA Hermann R., Poppe L., Pilbak S., Boden C., Maurer J., Weber S., Lerchl A.;
RT "Predicted 3D-structure of melanopsin, the non-rod, non-cone photopigment
RT of the mammalian circadian clock, from Djungarian hamsters (Phodopus
RT sungorus).";
RL Neurosci. Lett. 376:76-80(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 -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Opsin
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AY726733; AAU11506.1; -; mRNA.
DR AlphaFoldDB; Q5XXP2; -.
DR SMR; Q5XXP2; -.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; TAS:UniProtKB.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
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: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:0048511; P:rhythmic process; 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 Biological rhythms; Cell membrane; Cell projection; Chromophore;
KW Disulfide bond; G-protein coupled receptor; Glycoprotein; Membrane;
KW Photoreceptor protein; Receptor; Retinal protein; Sensory transduction;
KW Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..469
FT /note="Melanopsin"
FT /id="PRO_0000233061"
FT TOPO_DOM 1..71
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..92
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 93..106
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 107..127
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 128..143
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 144..164
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 165..187
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 188..208
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 209..237
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..258
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 259..295
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 296..316
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 317..328
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 329..349
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 350..469
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 409..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 336
FT /note="N6-(retinylidene)lysine"
FT /evidence="ECO:0000250"
FT CARBOHYD 30
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 142..220
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 469 AA; 51202 MW; BFE6B54A50A9C9BC CRC64;
MDSPPGPTAP PGLTQGPSFM ASTTLHSHWN STQKVSTRAQ LLAVSPTASG PEAAAWVPFP
TVDVPDHAHY ILGTVILLVG LTGMLGNLTV IYTFCRSRSL RTPANMLIIN LAVSDFLMSF
TQAPVFFASS LYKKWLFGET GCEFYAFCGA VLGITSMITL TAIALDRYLV ITRPLATIGM
GSKRRTALVL LGIWLYALAW SLPPFFGWSA YVPEGLLTSC SWDYVTFTPQ VRAYTMLLFC
FVFFLPLLVI IFCYISIFRA IRETGRACEG WSESPQRRRQ WHRLQSEWKM AKVALIVILL
FVLSWAPYST VALVAFAGYS HILTPYMSSV PAVIAKASAI HNPIVYAITH PKYRAAIAQH
LPCLGVLLGV SSQRNRPSLS YRSTHRSTLS SQSSDLSWIS APKRQESLGS ESEVGWTDTE
ATAVWGAAQP ASGQSSCGQN LEDGMVKAPS SPQAKGQLPS LDLGMQDAP
