MR1BA_DANRE
ID MR1BA_DANRE Reviewed; 287 AA.
AC Q90456; Q804J1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Melatonin receptor type 1B-A;
DE Short=Mel-1B-R-A;
DE Short=Mel1b receptor A;
DE AltName: Full=Melatonin receptor Mel1b Z6.2;
DE AltName: Full=Melatonin receptor Mel1b-19;
DE AltName: Full=zMel1b-2;
DE Flags: Fragment;
GN Name=mtnr1ba; Synonyms=mel1b, mtnr1b;
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 [MRNA] OF 1-240.
RA Danilova N.P.;
RT "Zebrafish melatonin receptors.";
RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 131-287.
RX PubMed=8647286; DOI=10.1016/0014-5793(96)00437-1;
RA Reppert S.M., Weaver D.R., Ebisawa T., Mahle C.D., Kolakowski L.F. Jr.;
RT "Cloning of a melatonin-related receptor from human pituitary.";
RL FEBS Lett. 386:219-224(1996).
RN [3]
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; AY166823; AAO23294.1; -; mRNA.
DR EMBL; U52220; AAC59913.1; -; mRNA.
DR AlphaFoldDB; Q90456; -.
DR SMR; Q90456; -.
DR STRING; 7955.ENSDARP00000070419; -.
DR PaxDb; Q90456; -.
DR ZFIN; ZDB-GENE-990415-157; mtnr1ba.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; Q90456; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
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..>287
FT /note="Melatonin receptor type 1B-A"
FT /id="PRO_0000069746"
FT TOPO_DOM 1..28
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 29..49
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 50..69
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..90
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 91..107
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 108..128
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 129..149
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 171..192
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..213
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 214..245
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 246..266
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 267..275
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 276..>287
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT CARBOHYD 4
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 10
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 105..182
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT NON_TER 287
SQ SEQUENCE 287 AA; 31693 MW; 37FD8A35AD746D40 CRC64;
MPENVSLIRN RTEVGQGRAW GSGAGARPAW VVMVLAGVLI FTSVVDVLGN VLVIISVLRN
RKLRNAGNAF VVSLAFADLL VVCYPYPLVL HAMLHAGWLP GEMECKVSGF LMGASVIGSI
FNITAIAINR YCFICQANTY EKIYGRAGTL VLLTLVWVLT AIAILPNLSL GSLTYDPRVY
SCTFSQTTSA GYTIAVVTVH FLLPIAVVTF CYLRIWVLVL RVRRRVTTDV RPRLRPSELR
HFLTMFVVFV LFAVCWAPLN LIGLAVAVDP PRVGPLVPDW LFVMSYF
