MCHR1_MACMU
ID MCHR1_MACMU Reviewed; 388 AA.
AC Q8MJ89;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 15-AUG-2003, sequence version 2.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=Melanin-concentrating hormone receptor 1;
DE Short=MCH receptor 1;
DE Short=MCH-R1;
DE Short=MCHR-1;
DE AltName: Full=G-protein coupled receptor 24;
DE AltName: Full=MCH-1R;
DE Short=MCH1R;
DE Short=MCHR;
DE Flags: Fragment;
GN Name=MCHR1; Synonyms=GPR24;
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12036292; DOI=10.1006/geno.2002.6771;
RA Tan C.P., Sano H., Iwaasa H., Pan J., Sailer A.W., Hreniuk D.L.,
RA Feighner S.D., Palyha O.C., Pong S.S., Figueroa D.J., Austin C.P.,
RA Jiang M.M., Yu H., Ito J., Ito M., Ito M., Guan X.M., MacNeil D.J.,
RA Kanatani A., Van der Ploeg L.H.T., Howard A.D.;
RT "Melanin-concentrating hormone receptor subtypes 1 and 2: species-specific
RT gene expression.";
RL Genomics 79:785-792(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 36-388.
RX PubMed=12182940; DOI=10.1016/s0196-9781(02)00077-3;
RA Fried S., O'Neill K., Hawes B.E.;
RT "Cloning and characterization of rhesus monkey MCH-R1 and MCH-R2.";
RL Peptides 23:1401-1408(2002).
CC -!- FUNCTION: Receptor for melanin-concentrating hormone, coupled to both G
CC proteins that inhibit adenylyl cyclase and G proteins that activate
CC phosphoinositide hydrolysis. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with NCDN. {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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM49793.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF513988; AAM49793.1; ALT_INIT; mRNA.
DR EMBL; AY078245; AAL80003.1; -; mRNA.
DR RefSeq; NP_001028057.1; NM_001032885.1.
DR AlphaFoldDB; Q8MJ89; -.
DR SMR; Q8MJ89; -.
DR STRING; 9544.ENSMMUP00000022864; -.
DR BindingDB; Q8MJ89; -.
DR ChEMBL; CHEMBL2029193; -.
DR GeneID; 574232; -.
DR KEGG; mcc:574232; -.
DR CTD; 2847; -.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; Q8MJ89; -.
DR OrthoDB; 1011272at2759; -.
DR Proteomes; UP000006718; Unplaced.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0030273; F:melanin-concentrating hormone receptor activity; IEA:InterPro.
DR GO; GO:0042923; F:neuropeptide binding; IBA:GO_Central.
DR GO; GO:0042277; F:peptide binding; IBA:GO_Central.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IBA:GO_Central.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR008361; MCH_rcpt.
DR InterPro; IPR004047; MCHR1.
DR PANTHER; PTHR24229:SF91; PTHR24229:SF91; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR01507; MCH1RECEPTOR.
DR PRINTS; PR01783; MCHRECEPTOR.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; G-protein coupled receptor; Glycoprotein; Membrane;
KW Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN <1..388
FT /note="Melanin-concentrating hormone receptor 1"
FT /id="PRO_0000069735"
FT TOPO_DOM <1..80
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 81..101
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 102..114
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 136..153
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 175..196
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 197..217
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 218..239
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..260
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 261..292
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 293..313
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 314..329
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 330..350
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 351..388
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 46..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 48
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 51
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT NON_TER 1
SQ SEQUENCE 388 AA; 42777 MW; 7F8528967DC431C1 CRC64;
ACAPGQGGRR WRLPQPAWVE GSSAWLWEPA TGTGWMDLEA SLLPTGPNTS NTSDGPDNLT
SAGSPPRSGS VSYINIIMPS VFGTICLLGI IGNSMVIFAV VKKSKLHWCN NVPDIFIINL
SVVDLLFLLG MPFMIHQLMG NGVWHFGETM CTLITAMDAN SQFTSTYILT AMAIDRYLAT
VHPISSTKFR KPSVATLVIC LLWALSFISI TPVWLYARLI PFPGGAVGCG IRLPNPDTDL
YWFTLYQFFL AFALPFVVIT AAYVRILQRM TSSVAPASQR SIRLRTKRVT RTAIAICLVF
FVCWAPYYVL QLTQLSISRP TLTFVYLYNA AISLGYANSC LNPFVYIVLC ETFRKRLVLS
VKPAAQGQLR AVSNAQTADE ERTESKGT
