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MTR1B_MOUSE
ID   MTR1B_MOUSE             Reviewed;         364 AA.
AC   Q8CIQ6; Q80T38; Q8K3K0;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 117.
DE   RecName: Full=Melatonin receptor type 1B;
DE            Short=Mel-1B-R;
DE            Short=Mel1b receptor;
GN   Name=Mtnr1b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=129/Sv;
RA   Jin X., von Gall C., Pieschl R.L., Gribkoff V.K., Stehle J.H.,
RA   Reppert S.M., Weaver D.R.;
RT   "Targeted disruption of the mouse Mel1b melatonin receptor.";
RL   Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 142-364.
RC   STRAIN=C57BL/6 X C3H;
RA   Resuehr D., Olcese J.;
RL   Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 143-253.
RX   PubMed=12679517; DOI=10.1073/pnas.0230374100;
RA   Vassilatis D.K., Hohmann J.G., Zeng H., Li F., Ranchalis J.E.,
RA   Mortrud M.T., Brown A., Rodriguez S.S., Weller J.R., Wright A.C.,
RA   Bergmann J.E., Gaitanaris G.A.;
RT   "The G protein-coupled receptor repertoires of human and mouse.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:4903-4908(2003).
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   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; AY145850; AAN46105.1; -; mRNA.
DR   EMBL; AY078982; AAL85489.3; -; mRNA.
DR   EMBL; AY255608; AAO85120.1; -; mRNA.
DR   CCDS; CCDS22841.1; -.
DR   AlphaFoldDB; Q8CIQ6; -.
DR   SMR; Q8CIQ6; -.
DR   STRING; 10090.ENSMUSP00000053086; -.
DR   GuidetoPHARMACOLOGY; 288; -.
DR   GlyGen; Q8CIQ6; 1 site.
DR   PaxDb; Q8CIQ6; -.
DR   PRIDE; Q8CIQ6; -.
DR   MGI; MGI:2181726; Mtnr1b.
DR   eggNOG; KOG3656; Eukaryota.
DR   InParanoid; Q8CIQ6; -.
DR   PhylomeDB; Q8CIQ6; -.
DR   Reactome; R-MMU-373076; Class A/1 (Rhodopsin-like receptors).
DR   Reactome; R-MMU-418594; G alpha (i) signalling events.
DR   ChiTaRS; Mtnr1b; mouse.
DR   PRO; PR:Q8CIQ6; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q8CIQ6; protein.
DR   GO; GO:0005887; C:integral component of plasma membrane; ISA:MGI.
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; ISA:MGI.
DR   GO; GO:0007623; P:circadian rhythm; TAS:MGI.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0042593; P:glucose homeostasis; ISO:MGI.
DR   GO; GO:0010754; P:negative regulation of cGMP-mediated signaling; ISO:MGI.
DR   GO; GO:0051481; P:negative regulation of cytosolic calcium ion concentration; ISO:MGI.
DR   GO; GO:1902260; P:negative regulation of delayed rectifier potassium channel activity; ISO:MGI.
DR   GO; GO:0046676; P:negative regulation of insulin secretion; ISO:MGI.
DR   GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:MGI.
DR   GO; GO:0051970; P:negative regulation of transmission of nerve impulse; ISO:MGI.
DR   GO; GO:0045906; P:negative regulation of vasoconstriction; ISO:MGI.
DR   GO; GO:0042753; P:positive regulation of circadian rhythm; ISO:MGI.
DR   GO; GO:0046010; P:positive regulation of circadian sleep/wake cycle, non-REM sleep; ISO:MGI.
DR   GO; GO:0051971; P:positive regulation of transmission of nerve impulse; ISO:MGI.
DR   GO; GO:0050796; P:regulation of insulin secretion; ISO:MGI.
DR   GO; GO:0098908; P:regulation of neuronal action potential; ISO:MGI.
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; Glycoprotein;
KW   Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..364
FT                   /note="Melatonin receptor type 1B"
FT                   /id="PRO_0000069871"
FT   TOPO_DOM        1..42
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        43..63
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        64..76
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        77..97
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        98..115
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        116..136
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        137..155
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        156..176
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        177..200
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        201..221
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        222..253
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        254..274
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        275..287
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        288..308
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        309..364
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          343..364
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        4
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        113..190
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   CONFLICT        237
FT                   /note="T -> E (in Ref. 2; AAL85489)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   364 AA;  40261 MW;  62DDA46BB59FEE7C CRC64;
     MPENSSIPNC CEASGLAARP SWSGSAGARP PVTARAPWVA PMLSTVVVVT TAVDFVGNLL
     VILSVLRNRK LRNAGNLFVV SLALADLVIA LYPYPLILVA IIRDGWVLGE AHCKASAFVM
     GLSVIGSVFN ITAIAINRYC CICHSTTYHR VCSHWYTPIY ISLVWLLTLV ALVPNFFVGS
     LEYDPRIYSC TFIQTASTQY TAAVVAIHFL LPMAVVSFCY LRIWVLVLQA RRKAKATRKL
     RLRPSDLRSF LTMFAVFVVF AICWAPLNCI GLAVAINPEA MALQVPEGLF VTSYFLAYFN
     SCLNAIVYGL LNQNFRREYK RILLAIWNTR RCIQHASKHC LTEERQGPTP PAARATVPVK
     EGAL
 
 
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