MTR1C_XENLA
ID MTR1C_XENLA Reviewed; 420 AA.
AC P49219; P87499;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Melatonin receptor type 1C;
DE Short=Mel-1C-R;
DE Short=Mel1c (alpha) receptor;
DE Short=Mel1c receptor;
GN Name=mtnr1c;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Dermal melanophore;
RX PubMed=7517042; DOI=10.1073/pnas.91.13.6133;
RA Ebisawa T., Karne S., Lerner M.R., Reppert S.M.;
RT "Expression cloning of a high-affinity melatonin receptor from Xenopus
RT dermal melanophores.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:6133-6137(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND FUNCTION.
RC TISSUE=Dermal melanophore;
RX PubMed=9212055; DOI=10.1210/mend.11.8.9964;
RA Jockers R., Petit L., Lacroix I., de Coppet P., Barrett P., Morgan P.J.,
RA Guardiola B., Delagrange P., Marullo S., Strosberg A.D.;
RT "Novel isoforms of Mel1c melatonin receptors modulating intracellular
RT cyclic guanosine 3',5'-monophosphate levels.";
RL Mol. Endocrinol. 11:1070-1081(1997).
CC -!- FUNCTION: High affinity receptor for melatonin. Likely to mediate the
CC potent effects of melatonin on pigment aggregation in melanophores. The
CC activity of this receptor is mediated by pertussis toxin sensitive G
CC proteins that inhibit adenylate cyclase activity.
CC {ECO:0000269|PubMed:7517042, ECO:0000269|PubMed:9212055}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P49219-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P49219-2; Sequence=VSP_040031, VSP_040032;
CC -!- TISSUE SPECIFICITY: Moderately expressed in dermal melanophores.
CC {ECO:0000269|PubMed:7517042}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; U09561; AAA70166.1; -; mRNA.
DR EMBL; U67879; AAB48389.1; -; mRNA.
DR EMBL; U67880; AAB48390.1; -; mRNA.
DR PIR; I51666; I51666.
DR RefSeq; NP_001081388.1; NM_001087919.1. [P49219-1]
DR AlphaFoldDB; P49219; -.
DR SMR; P49219; -.
DR BindingDB; P49219; -.
DR ChEMBL; CHEMBL5495; -.
DR PRIDE; P49219; -.
DR GeneID; 397808; -.
DR KEGG; xla:397808; -.
DR CTD; 397808; -.
DR Xenbase; XB-GENE-6466037; mtnr1c.S.
DR OrthoDB; 732872at2759; -.
DR Proteomes; UP000186698; Chromosome 8S.
DR Bgee; 397808; Expressed in oocyte and 12 other tissues.
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; 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 Alternative splicing; Cell membrane; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..420
FT /note="Melatonin receptor type 1C"
FT /id="PRO_0000069877"
FT TOPO_DOM 1..34
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 35..55
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 56..73
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 74..94
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 95..106
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 107..127
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 128..152
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 153..173
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 174..192
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..213
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 214..245
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 246..266
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 267..279
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 280..303
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 304..420
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 5
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 105..182
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT VAR_SEQ 353..354
FT /note="LG -> YV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9212055"
FT /id="VSP_040031"
FT VAR_SEQ 355..420
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9212055"
FT /id="VSP_040032"
SQ SEQUENCE 420 AA; 47425 MW; 81F8698D70CC0733 CRC64;
MMEVNSTCLD CRTPGTIRTE QDAQDSASQG LTSALAVVLI FTIVVDVLGN ILVILSVLRN
KKLQNAGNLF VVSLSIADLV VAVYPYPVIL IAIFQNGWTL GNIHCQISGF LMGLSVIGSV
FNITAIAINR YCYICHSLRY DKLYNQRSTW CYLGLTWILT IIAIVPNFFV GSLQYDPRIF
SCTFAQTVSS SYTITVVVVH FIVPLSVVTF CYLRIWVLVI QVKHRVRQDF KQKLTQTDLR
NFLTMFVVFV LFAVCWAPLN FIGLAVAINP FHVAPKIPEW LFVLSYFMAY FNSCLNAVIY
GVLNQNFRKE YKRILMSLLT PRLLFLDTSR GGTEGLKSKP SPAVTNNNQA DMLGEARSLW
LSRRNGAKMV IIIRPRKAQI AIIHQIFWPQ SSWATCRQDT KITGEEDGCR ELCKDGISQR
