MR1AA_DANRE
ID MR1AA_DANRE Reviewed; 350 AA.
AC P51046; Q567Z2; Q804J0;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Melatonin receptor type 1A-A;
DE Short=Mel-1A-R-A;
DE Short=Mel1a receptor A;
DE AltName: Full=Melatonin receptor Mel1a Z1.7-4;
DE AltName: Full=zMel1a1;
GN Name=mtnr1aa; Synonyms=mel1ar, mtnr1ar; ORFNames=zgc:110628;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-270.
RA Danilova N.P.;
RT "Zebrafish melatonin receptors.";
RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 130-282.
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).
RN [4]
RP INDUCTION.
RX PubMed=17622340; DOI=10.1371/journal.pone.0000587;
RA Shang E.H., Zhdanova I.V.;
RT "The circadian system is a target and modulator of prenatal cocaine
RT effects.";
RL PLoS ONE 2:E587-E587(2007).
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 -!- INDUCTION: By cocaine, which increases the levels of day-time
CC expression. {ECO:0000269|PubMed:17622340}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; BC092957; AAH92957.1; -; mRNA.
DR EMBL; AY166824; AAO23295.1; -; mRNA.
DR EMBL; U31822; AAA92494.1; -; mRNA.
DR RefSeq; NP_571468.1; NM_131393.1.
DR AlphaFoldDB; P51046; -.
DR SMR; P51046; -.
DR STRING; 7955.ENSDARP00000054673; -.
DR PaxDb; P51046; -.
DR GeneID; 30667; -.
DR KEGG; dre:30667; -.
DR CTD; 30667; -.
DR ZFIN; ZDB-GENE-990415-155; mtnr1aa.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; P51046; -.
DR OrthoDB; 907115at2759; -.
DR PhylomeDB; P51046; -.
DR Reactome; R-DRE-373076; Class A/1 (Rhodopsin-like receptors).
DR Reactome; R-DRE-418594; G alpha (i) signalling events.
DR PRO; PR:P51046; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0008502; F:melatonin receptor activity; IEA:InterPro.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
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; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 2: Evidence at transcript level;
KW Biological rhythms; Cell membrane; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..350
FT /note="Melatonin receptor type 1A-A"
FT /id="PRO_0000069743"
FT TOPO_DOM 1..29
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 30..50
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 51..63
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 64..84
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 85..101
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..122
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 123..144
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..165
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 166..187
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 188..208
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 209..240
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 241..261
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 262..267
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 268..288
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 289..350
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
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 100..177
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 59
FT /note="Q -> R (in Ref. 2; AAO23295)"
FT /evidence="ECO:0000305"
FT CONFLICT 103
FT /note="S -> G (in Ref. 2; AAO23295)"
FT /evidence="ECO:0000305"
FT CONFLICT 125
FT /note="C -> R (in Ref. 2; AAO23295)"
FT /evidence="ECO:0000305"
FT CONFLICT 223
FT /note="N -> P (in Ref. 1; AAH92957)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 350 AA; 39661 MW; D5E4C9678F7A777E CRC64;
MFMNGSSLNS SALDPSEQAL QRPPWVTTTL GCFLIFTIVV DILGNLLVIF SVYRNKKLQN
AGNIFVVSLA VADLVVAIYP YPLVLTSIFH RGWNLGYMHC QISGFLMGVS VIGSIFNITG
IAINCYCYIC HSLKYDKLYS DKNSVCYVLL IWALTVLAIV PNLFVGSLQY DPRVYSCTFE
QSASSAYTIA VVFFHFILPI MIVTYCYLRI WVLVIQVRRR VKNDNRPKIT PHDVRNFVTM
FVVFVLFAVC WAPLNFIGLA VAISPERVVP LIPEWLFVAS YFMAYFNSCL NAIVYGVLNQ
NFRREYKRIV VSVCTARIFF GESSNEAQER LKSKPSPLMT NNNQVKVDSV
