OPN4B_GADMO
ID OPN4B_GADMO Reviewed; 615 AA.
AC Q804Q2;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Melanopsin-B;
DE AltName: Full=Opsin-4B;
GN Name=opn4b;
OS Gadus morhua (Atlantic cod).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Zeiogadaria; Gadariae; Gadiformes; Gadoidei; Gadidae; Gadus.
OX NCBI_TaxID=8049;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAM95160.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=12508316; DOI=10.1002/cne.10523;
RA Drivenes O., Soviknes A.M., Ebbesson L.O., Fjose A., Seo H.C., Helvik J.V.;
RT "Isolation and characterization of two teleost melanopsin genes and their
RT differential expression within the inner retina and brain.";
RL J. Comp. Neurol. 456:84-93(2003).
CC -!- FUNCTION: Photoreceptor implicated in non-image-forming responses to
CC light. {ECO:0000250|UniProtKB:Q9QXZ9}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9QXZ9};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in the inner nuclear layer of the retina,
CC possibly in amacrine and ganglion cells. Expressed in a subpopulation
CC of neurons in the dorsal habenula. {ECO:0000269|PubMed:12508316}.
CC -!- DEVELOPMENTAL STAGE: Expressed in horizontal cell layer of the retina
CC at early larval stages declining to undetectable levels later in
CC development. {ECO:0000269|PubMed:12508316}.
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; AY126448; AAM95160.1; -; mRNA.
DR AlphaFoldDB; Q804Q2; -.
DR SMR; Q804Q2; -.
DR Proteomes; UP000694546; Unplaced.
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 Membrane; Photoreceptor protein; Receptor; Reference proteome;
KW Retinal protein; Sensory transduction; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..615
FT /note="Melanopsin-B"
FT /id="PRO_0000270991"
FT TOPO_DOM 1..19
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 20..40
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 41..56
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 57..77
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 78..93
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 94..114
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 115..136
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..157
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 158..189
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..210
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 211..244
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 245..265
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 266..279
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 280..300
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 301..615
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 390..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 465..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..502
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 287
FT /note="N6-(retinylidene)lysine"
FT /evidence="ECO:0000250"
FT DISULFID 91..169
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 615 AA; 69473 MW; 392D9756C407BAD2 CRC64;
MDMDRGFYRK VDVPDHAHYV IAFFVLIIGV VGVTGNALVM YAFLCNKKLR TPPNYFIMNL
AVSDFLMAIT QSPIFFINSL FKEWIFGETG CRMYAFCGAL FGITSMINLL AISLDRYIVI
TKPPQAIRWV SGRRTMVVIL LVWLYSLAWS LAPLLGWSSY IPEGLMTSCT WDYVTSTPAN
KGYTLMLCCF VFFIPLGIIS YCYLCMFLAI RSAGREIERL GTQVRKSTLM QQQTIKTEWK
LTKVAFVVII VYVHSWSPYA CVTLIAWAGY GSHLSPYSKA VPAVIAKASA IYNPFIYAII
HSKYRDTLAE HVPCLYFLRQ PPRKVSMSRA QSECSFRDSM VSRQSSASKT KFHRVSSTST
ADTQVWSDVE LDPMNHEGQS LRTSHSLGVL GRSKEHRGPP AQQNRQTRSS DTLEQATVAD
WRPPLTALRC DRNFLPQPTH PPYKMAAATP LQATTVDNVT PEHWNKHPNN NHKNHNNRHN
GNNNNEEHEY SGKGGRHCQN HPHHIDVKNS ISNCKKTCEK DTFSKEPVPC NAADDVRFSP
RSAHTIQHAM GTPFRYMPEG DIACQERLST DRSQRGDPLP DSKSLNCTGD VPVSAQRCSF
PHETSRNLEE SFMAL
