MTR1B_RAT
ID MTR1B_RAT Reviewed; 364 AA.
AC P49287; B7X946;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 25-APR-2018, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Melatonin receptor type 1B;
DE Short=Mel-1B-R;
DE Short=Mel1b receptor;
DE Flags: Precursor;
GN Name=Mtnr1b {ECO:0000312|RGD:620798}; Synonyms=Mt2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND FUNCTION.
RC STRAIN=Wistar; TISSUE=Hypothalamus;
RX PubMed=19340560; DOI=10.1007/s12576-008-0003-9;
RA Ishii H., Tanaka N., Kobayashi M., Kato M., Sakuma Y.;
RT "Gene structures, biochemical characterization and distribution of rat
RT melatonin receptors.";
RL J. Physiol. Sci. 59:37-47(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 139-258.
RC STRAIN=Sprague-Dawley;
RX PubMed=7568007; DOI=10.1073/pnas.92.19.8734;
RA Reppert S.M., Godson C., Mahle C.D., Weaver D.R., Slaugenhaupt S.A.,
RA Gusella J.F.;
RT "Molecular characterization of a second melatonin receptor expressed in
RT human retina and brain: the Mel1b melatonin receptor.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:8734-8738(1995).
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.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in the hippocampus, kidney, and ovary.
CC {ECO:0000269|PubMed:19340560}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB377275; BAH03530.1; -; mRNA.
DR EMBL; AABR07069239; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473993; EDL78429.1; -; Genomic_DNA.
DR EMBL; U28218; AAA75003.1; -; Genomic_DNA.
DR RefSeq; NP_001094111.1; NM_001100641.1.
DR AlphaFoldDB; P49287; -.
DR SMR; P49287; -.
DR STRING; 10116.ENSRNOP00000011883; -.
DR BindingDB; P49287; -.
DR ChEMBL; CHEMBL2566; -.
DR PaxDb; P49287; -.
DR Ensembl; ENSRNOT00000011883; ENSRNOP00000011883; ENSRNOG00000008972.
DR GeneID; 192646; -.
DR KEGG; rno:192646; -.
DR UCSC; RGD:620798; rat.
DR CTD; 4544; -.
DR RGD; 620798; Mtnr1b.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00940000162341; -.
DR HOGENOM; CLU_009579_3_3_1; -.
DR InParanoid; P49287; -.
DR OMA; RLFFQDT; -.
DR OrthoDB; 907115at2759; -.
DR TreeFam; TF331693; -.
DR Reactome; R-RNO-373076; Class A/1 (Rhodopsin-like receptors).
DR Reactome; R-RNO-418594; G alpha (i) signalling events.
DR PRO; PR:P49287; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Proteomes; UP000234681; Chromosome 8.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0043010; P:camera-type eye development; IEP:RGD.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0042593; P:glucose homeostasis; ISO:RGD.
DR GO; GO:0010754; P:negative regulation of cGMP-mediated signaling; IMP:RGD.
DR GO; GO:0051481; P:negative regulation of cytosolic calcium ion concentration; IMP:RGD.
DR GO; GO:1902260; P:negative regulation of delayed rectifier potassium channel activity; IDA:RGD.
DR GO; GO:0046676; P:negative regulation of insulin secretion; IMP:RGD.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IDA:RGD.
DR GO; GO:0051970; P:negative regulation of transmission of nerve impulse; IMP:RGD.
DR GO; GO:0045906; P:negative regulation of vasoconstriction; IMP:RGD.
DR GO; GO:0042753; P:positive regulation of circadian rhythm; IDA:RGD.
DR GO; GO:0046010; P:positive regulation of circadian sleep/wake cycle, non-REM sleep; IDA:RGD.
DR GO; GO:0051971; P:positive regulation of transmission of nerve impulse; IDA:RGD.
DR GO; GO:0050796; P:regulation of insulin secretion; ISO:RGD.
DR GO; GO:0098908; P:regulation of neuronal action potential; IMP:RGD.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR000025; Melatonin_rcpt.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
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 Cell membrane; Disulfide bond; G-protein coupled receptor; Membrane;
KW Receptor; Reference proteome; Signal; Transducer; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..364
FT /note="Melatonin receptor type 1B"
FT /evidence="ECO:0000255"
FT /id="PRO_0000069872"
FT TOPO_DOM 29..45
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 46..66
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 67..81
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 82..102
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 103..115
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 116..136
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 137..158
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 159..179
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 180..200
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 201..221
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 222..255
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 256..276
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 277..287
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 288..308
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 309..364
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DISULFID 113..190
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 364 AA; 40194 MW; 3ED047A73D052F55 CRC64;
MPDNSSIANC CAASGLAARP SWPGSAEAEP PETPRAPWVA PMLSTVVIVT TAVDFVGNLL
VILSVLRNRK LRNAGNLFVV NLALADLVVA LYPYPLILVA ILHDGWVLGE IHCKASAFVM
GLSVIGSVFN ITAIAINRYW CICHSATYHR ACSQWHAPLY ISLIWLLTLV ALVPNFFVGS
LEYDPRIYSC TFIQTASTQY TMAVVAIHFL LPIAVVSFCY LRIWILVLQA RRKAKAERKL
RLRPSDLRSF LTMFAVFVVF AICWAPLNCI GLAVAINPEA MALQIPEGLF VTSYFLAYFN
SCLNAIVYGL LNQNFRREYK RILSALWSTG RCFHDASKCH LTEDLQGPVP PAAMATIPVQ
EGAL
