OPN4_BRABE
ID OPN4_BRABE Reviewed; 706 AA.
AC Q4R1I4;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Melanopsin;
DE AltName: Full=Opsin-4;
DE AltName: Full=amphi-MOP;
GN Name=OPN4 {ECO:0000250|UniProtKB:Q1JPS6};
GN Synonyms=MOP {ECO:0000312|EMBL:BAE00065.1};
OS Branchiostoma belcheri (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomidae; Branchiostoma.
OX NCBI_TaxID=7741;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAE00065.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP TISSUE SPECIFICITY.
RX PubMed=15936279; DOI=10.1016/j.cub.2005.04.063;
RA Koyanagi M., Kubokawa K., Tsukamoto H., Shichida Y., Terakita A.;
RT "Cephalochordate melanopsin: evolutionary linkage between invertebrate
RT visual cells and vertebrate photosensitive retinal ganglion cells.";
RL Curr. Biol. 15:1065-1069(2005).
CC -!- FUNCTION: Photoreceptor implicated in non-image-forming responses to
CC light. Photoisomerizes covalently bound all-trans retinal back to 11-
CC cis retinal. Most likely coupled to the G(q) signaling cascade.
CC {ECO:0000269|PubMed:15936279}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Absorption:
CC Abs(max)=485 nm {ECO:0000269|PubMed:15936279};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9QXZ9};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in Joseph cells and photoreceptor cells
CC of the dorsal ocelli. {ECO:0000269|PubMed:15936279}.
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; AB205400; BAE00065.1; -; mRNA.
DR AlphaFoldDB; Q4R1I4; -.
DR SMR; Q4R1I4; -.
DR Proteomes; UP000515135; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0008020; F:G protein-coupled photoreceptor activity; IDA:UniProtKB.
DR GO; GO:0004744; F:retinal isomerase activity; IDA:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0007602; P:phototransduction; TAS:UniProtKB.
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 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.
PE 1: Evidence at protein level;
KW Cell membrane; Chromophore; Disulfide bond; G-protein coupled receptor;
KW Glycoprotein; Membrane; Photoreceptor protein; Receptor;
KW Reference proteome; Retinal protein; Sensory transduction; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..706
FT /note="Melanopsin"
FT /id="PRO_0000270993"
FT TOPO_DOM 1..86
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 108..121
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..142
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 143..159
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..180
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 181..201
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..222
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 223..248
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 249..269
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 270..314
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 315..335
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 336..351
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 352..372
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 373..706
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 393..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 571..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 630..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..445
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..599
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..657
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 358
FT /note="N6-(retinylidene)lysine"
FT /evidence="ECO:0000250"
FT CARBOHYD 12
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 158..236
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 706 AA; 76779 MW; 500A9BF739CA8734 CRC64;
MTEIPSFQPP INATEVEEEN AVFPTALTEW FSEVGNQVGE VALKLLSGEG DGMEVTPTPG
CTGNGSVCNG TDSGGVVWDI PPLAHYIVGT AVFCIGCCGM FGNAVVVYSF IKSKGLRTPA
NFFIINLALS DFLMNLTNMP IFAVNSAFQR WLLSDFACEL YGFAGGLFGC LSINTLMAIS
MDRYLVITKP FLVMRIVTKQ RVMFAILLLW IWSLVWALPP LFGWSAYVSE GFGTSCTFDY
MTPKLSYHIF TYIIFFTMYF IPGGVMIYCY YNIFATVKSG DKQFGKAVKE MAHEDVKNKA
QQERQRKNEI KTAKIAFIVI SLFMSAWTPY AVVSALGTLG YQDLVTPYLQ SIPAMFAKSS
AVYSPIVYAI TYPKFREAVK KHIPCLSGCL PASEEETKTK TRGQSSASAS MSMTQTTAPV
HDPQASVDSG SSVSVDDSSG VSRQDTMMVK VEVDKRMEKA GGGAADAAPQ EGASVSTVSA
QIEVRPSGKV TTKADVISTP QTAHGLSASP VPKVAELGSS ATLESAAIPG KIPTPLPSQP
IAAPIERHMA AMADEPPPKP RGVATTVNVR RTESGYDRSQ DSQRKKVVGD THRSRSFNTT
KDHFASEQPA ALIQPKELYS DDTTKKMARQ SSEKHEYDNP AFDEGITEVD TDSENETEGS
YDMLSVRFQA MAEEPPVETY RKASDLAINL GKASLMLSEA HDETVL
