MC4R_PIG
ID MC4R_PIG Reviewed; 332 AA.
AC O97504; Q2EF33; Q9N141; Q9N274;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Melanocortin receptor 4;
DE Short=MC4-R;
GN Name=MC4R;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Large white X Duroc; TISSUE=Kidney;
RA Ito Y., Minezawa M.;
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Yang X.Q., Yu H., Liu D.;
RT "The comparative analysis on MC4R gene of wild boar, domestic pig and their
RT crossbred.";
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 73-320, AND VARIANT ASN-298.
RX PubMed=10656927; DOI=10.1007/s003350010025;
RA Kim K.S., Larsen N., Short T., Plastow G., Rothschild M.F.;
RT "A missense variant of the porcine melanocortin-4 receptor (MC4R) gene is
RT associated with fatness, growth, and feed intake traits.";
RL Mamm. Genome 11:131-135(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 75-142.
RC TISSUE=Hypothalamus;
RA Matteri R.L., Dyer C.J.;
RL Submitted (JAN-2000) 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}.
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DR EMBL; AB021664; BAA36170.1; -; mRNA.
DR EMBL; DQ388767; ABD28176.1; -; mRNA.
DR EMBL; AF087937; AAF31753.1; -; Genomic_DNA.
DR EMBL; AF227727; AAF34778.1; -; mRNA.
DR RefSeq; NP_999338.1; NM_214173.1.
DR AlphaFoldDB; O97504; -.
DR SMR; O97504; -.
DR STRING; 9823.ENSSSCP00000005275; -.
DR PaxDb; O97504; -.
DR Ensembl; ENSSSCT00000091644; ENSSSCP00000074588; ENSSSCG00000051798.
DR GeneID; 397359; -.
DR KEGG; ssc:397359; -.
DR CTD; 4160; -.
DR VGNC; VGNC:103125; MC4R.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01030000234510; -.
DR InParanoid; O97504; -.
DR OMA; YCTCFMS; -.
DR OrthoDB; 869396at2759; -.
DR Proteomes; UP000008227; Chromosome 1.
DR Proteomes; UP000314985; Unplaced.
DR Bgee; ENSSSCG00000051798; Expressed in cerebellum and 9 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:0045780; P:positive regulation of bone resorption; IEA:Ensembl.
DR GO; GO:0019222; P:regulation of metabolic process; IBA:GO_Central.
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_0000069725"
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 298
FT /note="D -> N (associated with less backfat thickness,
FT slower growth rate and lower feed intake)"
FT /evidence="ECO:0000269|PubMed:10656927"
SQ SEQUENCE 332 AA; 36947 MW; 5CD1CD67008BFC81 CRC64;
MNSTHHHGMH TSLHFWNRST YGLHSNASEP LGKGYSEGGC YEQLFVSPEV FVTLGVISLL
ENILVIVAIA KNKNLHSPMY FFICSLAVAD MLVSVSNGSE TIVITLLNST DTDAQSFTVN
IDNVIDSVIC SSLLASICSL LSIAVDRYFT IFYALQYHNI MTVKRVGIII SCIWAVCTVS
GVLFIIYSDS SAVIICLITV FFTMLALMAS LYVHMFLMAR LHIKRIAVLP GTGTIRQGAN
MKGAITLTIL IGVFVVCWAP FFLHLIFYIS CPQNPYCVCF MSHFNLYLIL IMCNSIIDPL
IYALRSQELR KTFKEIICCY PLGGLCDLSS RY
