MTR1L_SHEEP
ID MTR1L_SHEEP Reviewed; 575 AA.
AC Q28558; O46624;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Melatonin-related receptor;
DE AltName: Full=G protein-coupled receptor 50;
DE AltName: Full=H9;
GN Name=GPR50;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9744482; DOI=10.1046/j.1365-2826.1998.00229.x;
RA Drew J.E., Barrett P., Williams L.M., Conway S., Morgan P.J.;
RT "The ovine melatonin-related receptor: cloning and preliminary distribution
RT and binding studies.";
RL J. Neuroendocrinol. 10:651-661(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 128-245.
RX PubMed=8647286; DOI=10.1016/0014-5793(96)00437-1;
RA Reppert S.M., Weaver D.R., Ebisawa T., Mahle C.D., Kolakowski L.F. Jr.;
RT "Cloning of a melatonin-related receptor from human pituitary.";
RL FEBS Lett. 386:219-224(1996).
CC -!- FUNCTION: Does not bind melatonin. {ECO:0000250}.
CC -!- SUBUNIT: Homodimer, and heterodimer with MTNR1A and MTNR1B.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AF047829; AAC04275.1; -; mRNA.
DR EMBL; U52221; AAC48609.1; -; mRNA.
DR RefSeq; NP_001009726.1; NM_001009726.1.
DR AlphaFoldDB; Q28558; -.
DR SMR; Q28558; -.
DR STRING; 9940.ENSOARP00000009392; -.
DR GeneID; 443023; -.
DR KEGG; oas:443023; -.
DR CTD; 9248; -.
DR eggNOG; KOG3656; Eukaryota.
DR OrthoDB; 907115at2759; -.
DR Proteomes; UP000002356; Unplaced.
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; 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; PR01151; MELATONIN1XR.
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; Membrane;
KW Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..575
FT /note="Melatonin-related receptor"
FT /id="PRO_0000069881"
FT TOPO_DOM 1..30
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 31..51
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 52..64
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 65..85
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 86..103
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 104..124
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 125..143
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 144..164
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 165..188
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..209
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 210..239
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..260
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 261..273
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..294
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 295..575
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 368..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..421
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..474
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 101..178
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 138
FT /note="R -> L (in Ref. 2; AAC48609)"
FT /evidence="ECO:0000305"
FT CONFLICT 158
FT /note="L -> M (in Ref. 2; AAC48609)"
FT /evidence="ECO:0000305"
FT CONFLICT 218..219
FT /note="Missing (in Ref. 2; AAC48609)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 575 AA; 62810 MW; E2CA1C11FFE7DEF8 CRC64;
MGRTLAVPTP YGCIGCKLPQ PDYPPALIVF MFCAMVITIV VDLIGNSMVI LAVSKNKKLR
NSGNVFVVSL SVADMLVAIY PYPLMLHAMA IGGWDLSKLQ CQMVGFITGL SVVGSIFNIM
AIAINRYCYI CHSLQYERIF SVRNTCIYLA VTWIMTVLAV LPNMYIGTIE YDPRTYTCIF
NYVNNPAFAV TIVCIHFVLP LLIVGFCYVK IWTKVLAARD PAGQNPDNQL AEVRNFLTMF
VIFLLFAVCW CPINALTVLV AVNPKEMAGK IPNWVYLAAY FIAYFNSCLN AVIYGVLNEN
FRREYWTIFH AMRHPVLFLS GLLTDVREMQ EAQAHTHARA RARTQAHEQD HAHACPAVEE
IPMSVRNVPL PGHGAAGQPE CVSGHPKPAS GHSRSVSARR KSASAHPKSA SGQSKSATVY
PKPTSVHFKP SSVYFKADSV YFKPSSSHPK PITGPSKTAI SPATSFPKPT TGYTQHATIH
SEPTTLDYLE PITTSHSKPV IASHSELAAS CHLECNIFDL SDPTSSPASD SSNSAASLLD
PTAAAAATVN PTVVTTDYHE IVLIDVDADS DEMAV
