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   27-MAR-2024, entry version 104.
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   GlyCosmos; P49219; 1 site, No reported glycans.
DR   GeneID; 397808; -.
DR   KEGG; xla:397808; -.
DR   AGR; Xenbase:XB-GENE-6466037; -.
DR   CTD; 397808; -.
DR   Xenbase; XB-GENE-6466037; mtnr1c.S.
DR   OrthoDB; 5397093at2759; -.
DR   Proteomes; UP000186698; Chromosome 8S.
DR   Bgee; 397808; Expressed in oocyte and 12 other cell types or tissues.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008502; F:melatonin receptor activity; IEA:InterPro.
DR   CDD; cd15401; 7tmA_Mel1C; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   InterPro; IPR002279; Mel_rcpt_1C.
DR   InterPro; IPR000025; Melatonin_rcpt.
DR   PANTHER; PTHR24228; B2 BRADYKININ RECEPTOR/ANGIOTENSIN II RECEPTOR; 1.
DR   PANTHER; PTHR24228:SF56; MELATONIN-RELATED RECEPTOR; 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   SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 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
//