MTR1C_CHICK
ID MTR1C_CHICK Reviewed; 346 AA.
AC P49288;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Melatonin receptor type 1C;
DE Short=Mel-1C-R;
DE Short=Mel1c receptor;
DE AltName: Full=CKB;
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, neostriatum,
CC hypothalamus, thalamus and pineal gland, less in cerebellum and retina.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; U31821; AAA92499.1; -; mRNA.
DR RefSeq; NP_990692.1; NM_205361.1.
DR AlphaFoldDB; P49288; -.
DR SMR; P49288; -.
DR STRING; 9031.ENSGALP00000014739; -.
DR BindingDB; P49288; -.
DR ChEMBL; CHEMBL3196; -.
DR DrugCentral; P49288; -.
DR Ensembl; ENSGALT00000014755; ENSGALP00000014739; ENSGALG00000009067.
DR GeneID; 396318; -.
DR KEGG; gga:396318; -.
DR CTD; 9248; -.
DR VEuPathDB; HostDB:geneid_396318; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00940000160515; -.
DR HOGENOM; CLU_009579_3_3_1; -.
DR OMA; RIWTLVI; -.
DR OrthoDB; 732872at2759; -.
DR PhylomeDB; P49288; -.
DR PRO; PR:P49288; -.
DR Proteomes; UP000000539; Chromosome 4.
DR Bgee; ENSGALG00000009067; Expressed in lung and 7 other tissues.
DR ExpressionAtlas; P49288; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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:1904408; F:melatonin binding; IDA:AgBase.
DR GO; GO:0008502; F:melatonin receptor activity; IEA:InterPro.
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; IPR002279; Mel_rcpt_1C.
DR InterPro; IPR002280; Mel_rcpt_1X.
DR InterPro; IPR000025; Melatonin_rcpt.
DR PANTHER; PTHR24228:SF56; PTHR24228:SF56; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR01150; MELATONIN1CR.
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..346
FT /note="Melatonin receptor type 1C"
FT /id="PRO_0000069876"
FT TOPO_DOM 1..26
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 27..47
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 48..60
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 61..81
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 82..99
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 100..120
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 121..139
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..160
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 161..184
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 206..237
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..258
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 259..271
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 272..292
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 293..346
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 326..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 7
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 97..174
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 346 AA; 38576 MW; 2431C474C25A8E23 CRC64;
MERPGSNGSC SGCRLEGGPA ARAASGLAAV LIVTIVVDVL GNALVILSVL RNKKLRNAGN
IFVVSLSVAD LVVAVYPYPL ILSAIFHNGW TMGNIHCQIS GFLMGLSVIG SIFNITAIAI
NRYCYICHSL RYDKLFNLKN TCCYICLTWT LTVVAIVPNF FVGSLQYDPR IYSCTFAQTV
STSYTITVVV VHFIVPLSIV TFCYLRIWIL VIQVKHRVRQ DCKQKIRAAD IRNFLTMFVV
FVLFAVCWGP LNFIGLAVSI NPSKVQPHIP EWLFVLSYFM AYFNSCLNAV IYGLLNQNFR
KEYKRILLML RTPRLLFIDV SKGGTEGLKS KPSPAVTNNN QAEIHL
