OPN4B_XENLA
ID OPN4B_XENLA Reviewed; 534 AA.
AC O57422;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Melanopsin-B;
DE AltName: Full=Opsin-4B;
DE Short=xMOP;
GN Name=opn4b {ECO:0000250|UniProtKB:Q804Q2};
GN Synonyms=mop {ECO:0000312|EMBL:AAC41235.1};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAC41235.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Skin {ECO:0000269|PubMed:9419377};
RX PubMed=9419377; DOI=10.1073/pnas.95.1.340;
RA Provencio I., Jiang G., De Grip W.J., Hayes W.P., Rollag M.D.;
RT "Melanopsin: an opsin in melanophores, brain, and eye.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:340-345(1998).
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 iris, high level in the inner
CC nuclear layer, possibly in horizontal cells, and lowest level in
CC retinal pigment epithelium. Expressed in melanophore cells of the skin.
CC {ECO:0000269|PubMed:9419377}.
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; AF014797; AAC41235.1; -; mRNA.
DR RefSeq; NP_001079143.1; NM_001085674.1.
DR RefSeq; XP_018110053.1; XM_018254564.1.
DR AlphaFoldDB; O57422; -.
DR SMR; O57422; -.
DR TCDB; 9.A.14.1.7; the g-protein-coupled receptor (gpcr) family.
DR GeneID; 373689; -.
DR KEGG; xla:373689; -.
DR CTD; 373689; -.
DR Xenbase; XB-GENE-5957217; XB5957215.L.
DR OMA; ILRTHAN; -.
DR Proteomes; UP000186698; Chromosome 1L.
DR Bgee; 373689; Expressed in camera-type eye and 1 other tissue.
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;
KW Reference proteome; Retinal protein; Sensory transduction; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..534
FT /note="Melanopsin-B"
FT /id="PRO_0000271892"
FT TOPO_DOM 1..32
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 33..53
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 54..64
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 65..85
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 86..102
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 103..123
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 124..146
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 147..167
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 168..198
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 199..219
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 220..250
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 251..271
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 272..286
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 287..307
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 308..534
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 478..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 480..501
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 294
FT /note="N6-(retinylidene)lysine"
FT /evidence="ECO:0000250"
FT CARBOHYD 189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 100..178
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 534 AA; 60344 MW; A453F7ED39D1B87E CRC64;
MDLGKTVEYG THRQDAIAQI DVPDQVLYTI GSFILIIGSV GIIGNMLVLY AFYRNKKLRT
APNYFIINLA ISDFLMSATQ APVCFLSSLH REWILGDIGC NVYAFCGALF GITSMMTLLA
ISINRYIVIT KPLQSIQWSS KKRTSQIIVL VWMYSLMWSL APLLGWSSYV PEGLRISCTW
DYVTSTMSNR SYTMMLCCCV FFIPLIVISH CYLFMFLAIR STGRNVQKLG SYGRQSFLSQ
SMKNEWKMAK IAFVIIIVFV LSWSPYACVT LIAWAGHGKS LTPYSKTVPA VIAKASAIYN
PIIYGIIHPK YRETIHKTVP CLRFLIREPK KDIFESSVRG SIYGRQSASR KKNSFISTVS
TAETVSSHIW DNTPNGHWDR KSLSQTMSNL CSPLLQDPNS SHTLEQTLTW PDDPSPKEIL
LPSSLKSVTY PIGLESIVKD EHTNNSCVRN HRVDKSGGLD WIINATLPRI VIIPTSESNI
SETKEEHDNN SEEKSKRTEE EEDFFNFHVD TSLLNLEGLN SSTDLYEVVE RFLS
