MTR1A_CHICK
ID MTR1A_CHICK Reviewed; 353 AA.
AC P49285;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Melatonin receptor type 1A;
DE Short=Mel-1A-R;
DE Short=Mel1a receptor;
DE AltName: Full=CKA;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7576645; DOI=10.1016/0896-6273(95)90090-x;
RA Reppert S.M., Weaver D.R., Cassone V.M., Godson C., Kolakowski L.F. Jr.;
RT "Melatonin receptors are for the birds: molecular analysis of two receptor
RT subtypes differentially expressed in chick brain.";
RL Neuron 15:1003-1015(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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed in optic tectum and retina, less in
CC neostriatum, hypothalamus and thalamus.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; U31820; AAA92498.1; -; mRNA.
DR RefSeq; NP_990693.1; NM_205362.1.
DR AlphaFoldDB; P49285; -.
DR SMR; P49285; -.
DR STRING; 9031.ENSGALP00000022058; -.
DR BindingDB; P49285; -.
DR ChEMBL; CHEMBL2095154; -.
DR DrugCentral; P49285; -.
DR PaxDb; P49285; -.
DR Ensembl; ENSGALT00000022097; ENSGALP00000022058; ENSGALG00000013576.
DR GeneID; 396319; -.
DR KEGG; gga:396319; -.
DR CTD; 4543; -.
DR VEuPathDB; HostDB:geneid_396319; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00940000160321; -.
DR HOGENOM; CLU_009579_3_3_1; -.
DR InParanoid; P49285; -.
DR OMA; KPDNNPR; -.
DR OrthoDB; 907115at2759; -.
DR PhylomeDB; P49285; -.
DR TreeFam; TF331693; -.
DR Reactome; R-GGA-373076; Class A/1 (Rhodopsin-like receptors).
DR Reactome; R-GGA-418594; G alpha (i) signalling events.
DR PRO; PR:P49285; -.
DR Proteomes; UP000000539; Chromosome 4.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0043235; C:receptor complex; IEA:Ensembl.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0042562; F:hormone binding; IEA:Ensembl.
DR GO; GO:1904408; F:melatonin binding; IDA:AgBase.
DR GO; GO:0008502; F:melatonin receptor activity; IEA:Ensembl.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IEA:Ensembl.
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:0046325; P:negative regulation of glucose import; IDA:AgBase.
DR GO; GO:0045820; P:negative regulation of glycolytic process; IDA:AgBase.
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_0000069868"
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 REGION 1..26
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 9
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; 39896 MW; DBF078C7F2AF291D CRC64;
MRANGSELNG TVLPRDPPAE GSPRRPPWVT STLATILIFT IVVDLLGNLL VILSVYRNKK
LRNAGNIFVV SLAIADLVVA IYPYPLVLTS VFHNGWNLGY LHCQISGFLM GLSVIGSIFN
ITGIAINRYC YICHSLKYDK LYSDKNSLCY VGLIWVLTVV AIVPNLFVGS LQYDPRIYSC
TFAQSVSSAY TIAVVFFHFI LPIAIVTYCY LRIWILVIQV RRRVKPDNNP RLKPHDFRNF
VTMFVVFVLF AVCWAPLNFI GLAVAVDPET IIPRIPEWLF VSSYYMAYFN SCLNAIIYGL
LNQNFRREYK KIVVSFCTAK AFFQDSSNDA ADRIRSKPSP LITNNNQVKV DSV
