MTR1A_MOUSE
ID MTR1A_MOUSE Reviewed; 353 AA.
AC Q61184;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Melatonin receptor type 1A;
DE Short=Mel-1A-R;
DE Short=Mel1a receptor;
GN Name=Mtnr1a;
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=BALB/cJ;
RX PubMed=8754776; DOI=10.1210/endo.137.8.8754776;
RA Roca A.L., Godson C., Weaver D.R., Reppert S.M.;
RT "Structure, characterization, and expression of the gene encoding the mouse
RT Mel1a melatonin receptor.";
RL Endocrinology 137:3469-3477(1996).
CC -!- FUNCTION: High affinity receptor for melatonin. Likely to mediate the
CC reproductive and circadian actions of melatonin. The activity of this
CC receptor is mediated by pertussis toxin sensitive G proteins that
CC inhibit 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; U52222; AAB08755.1; -; mRNA.
DR CCDS; CCDS22273.1; -.
DR RefSeq; NP_032665.1; NM_008639.2.
DR AlphaFoldDB; Q61184; -.
DR SMR; Q61184; -.
DR STRING; 10090.ENSMUSP00000069872; -.
DR GlyGen; Q61184; 2 sites.
DR iPTMnet; Q61184; -.
DR PaxDb; Q61184; -.
DR PRIDE; Q61184; -.
DR Antibodypedia; 29126; 352 antibodies from 33 providers.
DR DNASU; 17773; -.
DR Ensembl; ENSMUST00000067984; ENSMUSP00000069872; ENSMUSG00000054764.
DR GeneID; 17773; -.
DR KEGG; mmu:17773; -.
DR UCSC; uc009loq.1; mouse.
DR CTD; 4543; -.
DR MGI; MGI:102967; Mtnr1a.
DR VEuPathDB; HostDB:ENSMUSG00000054764; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00940000160321; -.
DR HOGENOM; CLU_009579_3_3_1; -.
DR InParanoid; Q61184; -.
DR OMA; KPDNNPR; -.
DR OrthoDB; 907115at2759; -.
DR PhylomeDB; Q61184; -.
DR TreeFam; TF331693; -.
DR Reactome; R-MMU-373076; Class A/1 (Rhodopsin-like receptors).
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR BioGRID-ORCS; 17773; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Mtnr1a; mouse.
DR PRO; PR:Q61184; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q61184; protein.
DR Bgee; ENSMUSG00000054764; Expressed in lens of camera-type eye and 25 other tissues.
DR ExpressionAtlas; Q61184; baseline and differential.
DR Genevisible; Q61184; MM.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0043235; C:receptor complex; ISO:MGI.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0042562; F:hormone binding; ISO:MGI.
DR GO; GO:0008502; F:melatonin receptor activity; ISO:MGI.
DR GO; GO:0097159; F:organic cyclic compound binding; ISO:MGI.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0007623; P:circadian rhythm; IBA:GO_Central.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0046676; P:negative regulation of insulin secretion; ISO:MGI.
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 Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..353
FT /note="Melatonin receptor type 1A"
FT /id="PRO_0000069863"
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..66
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 67..87
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 88..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..145
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 167..190
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..211
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 212..243
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 244..264
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 265..277
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..298
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 299..353
FT /note="Cytoplasmic"
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 103..180
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 353 AA; 39837 MW; 0975C2FD41B54C74 CRC64;
MKGNVSELLN ATQQAPGGGE GGRPRPSWLA STLAFILIFT IVVDILGNLL VILSVYRNKK
LRNSGNIFVV SLAVADLVVA VYPYPLVLTS ILNNGWNLGY LHCQVSAFLM GLSVIGSIFN
ITGIAMNRYC YICHSLKYDK IYSNKNSLCY VFLIWMLTLI AIMPNLQTGT LQYDPRIYSC
TFTQSVSSAY TIAVVVFHFI VPMIIVIFCY LRIWVLVLQV RRRVKPDNKP KLKPQDFRNF
VTMFVVFVLF AICWAPLNLI GLIVASDPAT MVPRIPEWLF VASYYLAYFN SCLNAIIYGL
LNQNFRKEYK KIIVSLCTAK MFFVESSNEE ADKIKCKPSP LIPNNNLIKV DSV
