MTR1A_SHEEP
ID MTR1A_SHEEP Reviewed; 366 AA.
AC P48040; O46608;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=Melatonin receptor type 1A;
DE Short=Mel-1A-R;
DE Short=Mel1a receptor;
GN Name=MTNR1A;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=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).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9194573; DOI=10.1016/s0167-4889(96)00179-6;
RA Barrett P., Conway S., Jockers R., Strosberg A.D., Guardiola-Lemaitre B.,
RA Delagrange P., Morgan P.J.;
RT "Cloning and functional analysis of a polymorphic variant of the ovine Mel
RT 1a melatonin receptor.";
RL Biochim. Biophys. Acta 1356:299-307(1997).
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 -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; U14109; AAB17721.1; -; mRNA.
DR EMBL; AF045219; AAC02699.1; -; mRNA.
DR PIR; I46469; I46469.
DR RefSeq; NP_001009725.1; NM_001009725.1.
DR AlphaFoldDB; P48040; -.
DR SMR; P48040; -.
DR STRING; 9940.ENSOARP00000008886; -.
DR BindingDB; P48040; -.
DR GeneID; 443022; -.
DR KEGG; oas:443022; -.
DR CTD; 4543; -.
DR eggNOG; KOG3656; Eukaryota.
DR OrthoDB; 907115at2759; -.
DR Proteomes; UP000002356; Unplaced.
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; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..366
FT /note="Melatonin receptor type 1A"
FT /id="PRO_0000069867"
FT TOPO_DOM 1..45
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 46..66
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 67..79
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..100
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 101..118
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..139
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 140..158
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..179
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 180..203
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..224
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 225..256
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 257..277
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 278..290
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 291..311
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 312..366
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 16
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 23
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 116..193
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT VARIANT 282
FT /note="A -> D (in Mel 1a(beta))"
FT VARIANT 358
FT /note="H -> R (in Mel 1a(beta))"
FT VARIANT 361
FT /note="I -> V (in Mel 1a(beta))"
SQ SEQUENCE 366 AA; 40401 MW; 5386E0DFF9710E4A CRC64;
MAGRLWGSPG GTPKGNGSSA LLNVSQAAPG AGDGVRPRPS WLAATLASIL IFTIVVDIVG
NLLVVLSVYR NKKLRNAGNV FVVSLAVADL LVAVYPYPLA LASIVNNGWS LSSLHCQLSG
FLMGLSVIGS VFSITGIAIN RYCCICHSLR YGKLYSGTNS LCYVFLIWTL TLVAIVPNLC
VGTLQYDPRI YSCTFTQSVS SAYTIAVVVF HFIVPMLVVV FCYLRIWALV LQVRWKVKPD
NKPKLKPQDF RNFVTMFVVF VLFAICWAPL NFIGLVVASD PASMAPRIPE WLFVASYYMA
YFNSCLNAII YGLLNQNFRQ EYRKIIVSLC TTKMFFVDSS NHVADRIKRK PSPLIANHNL
IKVDSV
