MTR1A_PHOSU
ID MTR1A_PHOSU Reviewed; 353 AA.
AC P49217;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Melatonin receptor type 1A;
DE Short=Mel-1A-R;
DE Short=Mel1a receptor;
GN Name=MTNR1A;
OS Phodopus sungorus (Striped hairy-footed hamster) (Djungarian hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Phodopus.
OX NCBI_TaxID=10044;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Weaver D.R., Liu C., Reppert S.M.;
RL Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 130-285.
RC TISSUE=Hypothalamus, and Pituitary pars tuberalis;
RX PubMed=7946354; DOI=10.1016/0896-6273(94)90055-8;
RA Reppert S.M., Weaver D.R., Ebisawa T.;
RT "Cloning and characterization of a mammalian melatonin receptor that
RT mediates reproductive and circadian responses.";
RL Neuron 13:1177-1185(1994).
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.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: At least in the brain, more precisely in the pars
CC tuberalis and the suprachiasmatic nucleus.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; U14110; AAB17722.1; -; mRNA.
DR PIR; I84498; I84498.
DR AlphaFoldDB; P49217; -.
DR SMR; P49217; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008502; F:melatonin receptor activity; IEA:InterPro.
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; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..353
FT /note="Melatonin receptor type 1A"
FT /id="PRO_0000069864"
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..147
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..168
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 169..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 REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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; 39685 MW; 224ABB160393BAC0 CRC64;
MKGNGSTLLN ASQQAPGVGE GGGPRPSWLA STLAFILIFT IVVDILGNLL VILSVYRNKK
LRNAGNIFVV SLAIADLVVA IYPYPLVLTS IFNNGWNLGY LHCQISAFLM GLSVIGSIFN
ITGIAINRYC YICHSLKYDR LYSNKNSLCY VFLIWVLTLV AIMPNLQTGT LQYDPRIYSC
TFTQSVSSAY TIAVVVFHFI VPMIIVIFCY LRIWILVLQV RRRVKPDSKP RLKPQDFRNF
VTMFVVFVLF AICWAPLNFI GLIVASDPAT MAPRIPEWLF VASYYMAYFN SCLNAIIYGL
LNQNFRQEYK RILVSLFTAK MCFVDSSNDP ADKIKCKPAP LIANNNLIKV DSV
