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MR1BB_DANRE
ID   MR1BB_DANRE             Reviewed;         347 AA.
AC   P51049; Q5RGH4; Q804I8;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 2.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=Melatonin receptor type 1B-B;
DE            Short=Mel-1B-R-B;
DE            Short=Mel1b receptor B;
DE   AltName: Full=Melatonin receptor Mel1b Z2.6-4;
DE   AltName: Full=zMel1b-1;
GN   Name=mtnr1bb; Synonyms=mel1br, mtnr1br, mtnr1br-2;
GN   ORFNames=si:ch211-214k5.4, si:ch211-224h1.2;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-233.
RA   Danilova N.P.;
RT   "Zebrafish melatonin receptors.";
RL   Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 134-286.
RX   PubMed=7576645; DOI=10.1016/0896-6273(95)90090-x;
RA   Reppert S.M., Weaver D.R., Cassone V.M., Godson C., Kolakowski L.F. Jr.;
RT   "Melatonin receptors are for the birds: molecular analysis of two receptor
RT   subtypes differentially expressed in chick brain.";
RL   Neuron 15:1003-1015(1995).
RN   [4]
RP   INDUCTION.
RX   PubMed=17622340; DOI=10.1371/journal.pone.0000587;
RA   Shang E.H., Zhdanova I.V.;
RT   "The circadian system is a target and modulator of prenatal cocaine
RT   effects.";
RL   PLoS ONE 2:E587-E587(2007).
CC   -!- FUNCTION: High affinity receptor for melatonin. The activity of this
CC       receptor is mediated by pertussis toxin sensitive G proteins that
CC       inhibits adenylate cyclase activity (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- INDUCTION: By cocaine, which increases the levels of day-time
CC       expression. {ECO:0000269|PubMed:17622340}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; BX897671; CAI11795.1; -; Genomic_DNA.
DR   EMBL; CR933018; CAM14076.1; -; Genomic_DNA.
DR   EMBL; AY166826; AAO23297.1; -; mRNA.
DR   EMBL; U31824; AAA92496.1; -; mRNA.
DR   RefSeq; NP_571469.1; NM_131394.1.
DR   AlphaFoldDB; P51049; -.
DR   SMR; P51049; -.
DR   STRING; 7955.ENSDARP00000072688; -.
DR   PaxDb; P51049; -.
DR   Ensembl; ENSDART00000078226; ENSDARP00000072688; ENSDARG00000086493.
DR   Ensembl; ENSDART00000181941; ENSDARP00000147236; ENSDARG00000086493.
DR   GeneID; 30668; -.
DR   KEGG; dre:30668; -.
DR   CTD; 30668; -.
DR   ZFIN; ZDB-GENE-990415-156; mtnr1bb.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT00940000166267; -.
DR   HOGENOM; CLU_009579_3_3_1; -.
DR   InParanoid; P51049; -.
DR   OMA; RLFFQDT; -.
DR   OrthoDB; 907115at2759; -.
DR   PhylomeDB; P51049; -.
DR   TreeFam; TF331693; -.
DR   PRO; PR:P51049; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 10.
DR   Bgee; ENSDARG00000086493; Expressed in dorsal caudal thalamic nucleus and 7 other tissues.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR   GO; GO:0008502; F:melatonin receptor activity; IEA:InterPro.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   InterPro; IPR002278; Mel_1A/1B_rcpt.
DR   InterPro; IPR000025; Melatonin_rcpt.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR01149; MELATONIN1AR.
DR   PRINTS; PR00857; MELATONINR.
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   2: Evidence at transcript level;
KW   Biological rhythms; Cell membrane; Disulfide bond;
KW   G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW   Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT   CHAIN           1..347
FT                   /note="Melatonin receptor type 1B-B"
FT                   /id="PRO_0000069745"
FT   TOPO_DOM        1..36
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        37..57
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        58..72
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        73..93
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        94..105
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        106..126
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        127..148
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        149..169
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        170..191
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        192..212
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        213..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..278
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        279..299
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        300..347
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        10
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        104..181
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   CONFLICT        25
FT                   /note="A -> P (in Ref. 2; AAO23297)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        63
FT                   /note="R -> K (in Ref. 2; AAO23297)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        143
FT                   /note="Y -> C (in Ref. 3; AAA92496)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   347 AA;  38979 MW;  5BB93B61AE83D563 CRC64;
     MPENIAFLTN STDLGHVGRA LGSSARPAWA IAVLASVLIF TTVVDVLGNL LVIISVFRNR
     KLRNAGNVFV VSLAFADLVV AFYPYPLVLY AIFHDGWSLG ETQCKISGFL MGLSVIGSVF
     NITGIAINRY CYICHSFAYG RLYSFRNTLL LVALIWALTV LAILPNFFVG SLSYDPRVYS
     CTFTQTASSS YTVVVVVVHF LVPIAVVTFC YLRIWVLVIQ VRRKVKSEER SRVRPSDLRN
     FVTMFVVFVL FAICWAPLNL IGLVVAINPE VMAPRVPEWL FVVSYFMAYF NSCLNAIIYG
     LLNRNFRKEY VRIMTAVWIP RRFVTETSRA ATDGMRSKPS PAINNNE
 
 
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