MC4R_BOVIN
ID MC4R_BOVIN Reviewed; 332 AA.
AC Q9GLJ8; A6QNL9;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Melanocortin receptor 4;
DE Short=MC4-R;
GN Name=MC4R;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS ALA-145 AND THR-172.
RC STRAIN=Holstein;
RX PubMed=11531696; DOI=10.1046/j.1365-2052.2001.00750.x;
RA Haegeman A., Coopman F., Jacobs K., Mattheeuws M., Van Zeveren A.,
RA Peelman L.J.;
RT "Bovine melanocortin receptor 4: cDNA sequence, polymorphisms and
RT mapping.";
RL Anim. Genet. 32:189-192(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Receptor specific to the heptapeptide core common to
CC adrenocorticotropic hormone and alpha-, beta-, and gamma-MSH. Plays a
CC central role in energy homeostasis and somatic growth. This receptor is
CC mediated by G proteins that stimulate adenylate cyclase (cAMP).
CC {ECO:0000250|UniProtKB:P32245}.
CC -!- SUBUNIT: Interacts with ATRNL1 (By similarity). Homodimer; disulfide-
CC linked, also forms higher order oligomers. Interacts with MGRN1, but
CC does not undergo MGRN1-mediated ubiquitination; this interaction
CC competes with GNAS-binding and thus inhibits agonist-induced cAMP
CC production. Interacts with MRAP and MRAP2; these associated factors
CC increase ligand-sensitivity and generation of cAMP (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P32245};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF265221; AAG17639.1; -; mRNA.
DR EMBL; BC148892; AAI48893.1; -; mRNA.
DR RefSeq; NP_776535.1; NM_174110.1.
DR AlphaFoldDB; Q9GLJ8; -.
DR SMR; Q9GLJ8; -.
DR STRING; 9913.ENSBTAP00000026223; -.
DR PaxDb; Q9GLJ8; -.
DR Ensembl; ENSBTAT00000026223; ENSBTAP00000026223; ENSBTAG00000019676.
DR GeneID; 281300; -.
DR KEGG; bta:281300; -.
DR CTD; 4160; -.
DR VEuPathDB; HostDB:ENSBTAG00000019676; -.
DR VGNC; VGNC:31295; MC4R.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01030000234510; -.
DR HOGENOM; CLU_009579_13_0_1; -.
DR InParanoid; Q9GLJ8; -.
DR OMA; YCTCFMS; -.
DR OrthoDB; 869396at2759; -.
DR TreeFam; TF332646; -.
DR Reactome; R-BTA-375276; Peptide ligand-binding receptors.
DR Proteomes; UP000009136; Chromosome 24.
DR Bgee; ENSBTAG00000019676; Expressed in occipital lobe and 17 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0004980; F:melanocyte-stimulating hormone receptor activity; IBA:GO_Central.
DR GO; GO:0042923; F:neuropeptide binding; IEA:Ensembl.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007631; P:feeding behavior; IEA:Ensembl.
DR GO; GO:0030073; P:insulin secretion; IEA:Ensembl.
DR GO; GO:0045780; P:positive regulation of bone resorption; IEA:Ensembl.
DR GO; GO:1903998; P:regulation of eating behavior; IEA:Ensembl.
DR GO; GO:0019222; P:regulation of metabolic process; IBA:GO_Central.
DR GO; GO:0032868; P:response to insulin; IEA:Ensembl.
DR GO; GO:1990680; P:response to melanocyte-stimulating hormone; IEA:Ensembl.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR001908; MC3-5R.
DR InterPro; IPR000155; Mcort_rcpt_4.
DR InterPro; IPR001671; Melcrt_ACTH_rcpt.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00534; MCRFAMILY.
DR PRINTS; PR00535; MELNOCORTINR.
DR PRINTS; PR01062; MELNOCORTN4R.
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; Glycoprotein;
KW Lipoprotein; Membrane; Palmitate; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..332
FT /note="Melanocortin receptor 4"
FT /id="PRO_0000069721"
FT TOPO_DOM 1..43
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 44..69
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 70..81
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..106
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 107..123
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 124..145
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 146..165
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 166..186
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 187..191
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 192..215
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 216..248
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 249..271
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 272..280
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 281..304
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 305..332
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT LIPID 318
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 17
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 26
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 84
FT /note="Interchain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT VARIANT 145
FT /note="V -> A"
FT /evidence="ECO:0000269|PubMed:11531696"
FT VARIANT 172
FT /note="A -> T"
FT /evidence="ECO:0000269|PubMed:11531696"
SQ SEQUENCE 332 AA; 36620 MW; C28356955F9D8FBD CRC64;
MNSTQPLGMH TSLHSWNRSA HGMPTNVSES LAKGYSDGGC YEQLFVSPEV FVTLGVISLL
ENILVIVAIA KNKNLHSPMY FFICSLAVAD MLVSVSNGSE TIVITLLNST DTDAQSFTVD
IDNVIDSVIC SSLLASICSL LSIAVDRYFT IFYALQYHNI MTVKRVAITI SAIWAACTVS
GVLFIIYSDS SAVIICLITV FFTMLALMAS LYVHMFLMAR LHIKRIAVLP GSGTIRQGAN
MKGAITLTIL IGVFVVCWAP FFLHLIFYIS CPQNPYCVCF MSHFNLYLIL IMCNSIIDPL
IYALRSQELR KTFKEIICCS PLGGLCDLSS RY
