MC5R_MOUSE
ID MC5R_MOUSE Reviewed; 325 AA.
AC P41149;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Melanocortin receptor 5;
DE Short=MC5-R;
GN Name=Mc5r;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv;
RX PubMed=8161509; DOI=10.1021/bi00181a015;
RA Labbe O., Desarnaud F., Eggerickx D., Vassart G., Parmentier M.;
RT "Molecular cloning of a mouse melanocortin 5 receptor gene widely expressed
RT in peripheral tissues.";
RL Biochemistry 33:4543-4549(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8185570; DOI=10.1006/bbrc.1994.1580;
RA Gantz I., Shimoto Y., Konda Y., Miwa H., Dickinson C.J., Yamada T.;
RT "Molecular cloning, expression, and characterization of a fifth
RT melanocortin receptor.";
RL Biochem. Biophys. Res. Commun. 200:1214-1220(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=7739752; DOI=10.1007/bf00995160;
RA Fathi Z., Iben L.G., Parker E.M.;
RT "Cloning, expression, and tissue distribution of a fifth melanocortin
RT receptor subtype.";
RL Neurochem. Res. 20:107-113(1995).
CC -!- FUNCTION: Receptor for MSH (alpha, beta and gamma) and ACTH. The
CC activity of this receptor is mediated by G proteins which activate
CC adenylate cyclase. This receptor is a possible mediator of the
CC immunomodulation properties of melanocortins.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Skin, adrenal gland, skeletal muscle, bone marrow,
CC spleen, thymus, gonads, uterus and brain.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA76585.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X76295; CAA53943.1; -; Genomic_DNA.
DR EMBL; L22527; AAA21337.1; -; Genomic_DNA.
DR EMBL; U08354; AAA76585.1; ALT_INIT; mRNA.
DR PIR; I49008; I49008.
DR RefSeq; NP_038624.2; NM_013596.2.
DR AlphaFoldDB; P41149; -.
DR SMR; P41149; -.
DR STRING; 10090.ENSMUSP00000130497; -.
DR BindingDB; P41149; -.
DR ChEMBL; CHEMBL4489; -.
DR GuidetoPHARMACOLOGY; 286; -.
DR GlyGen; P41149; 4 sites.
DR iPTMnet; P41149; -.
DR PhosphoSitePlus; P41149; -.
DR PaxDb; P41149; -.
DR PRIDE; P41149; -.
DR Antibodypedia; 7155; 428 antibodies from 37 providers.
DR DNASU; 17203; -.
DR Ensembl; ENSMUST00000172148; ENSMUSP00000130497; ENSMUSG00000007480.
DR GeneID; 17203; -.
DR KEGG; mmu:17203; -.
DR CTD; 4161; -.
DR MGI; MGI:99420; Mc5r.
DR VEuPathDB; HostDB:ENSMUSG00000007480; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01030000234510; -.
DR InParanoid; P41149; -.
DR PhylomeDB; P41149; -.
DR Reactome; R-MMU-375276; Peptide ligand-binding receptors.
DR Reactome; R-MMU-418555; G alpha (s) signalling events.
DR PRO; PR:P41149; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; P41149; protein.
DR Bgee; ENSMUSG00000007480; Expressed in tail skin and 79 other tissues.
DR ExpressionAtlas; P41149; baseline and differential.
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; ISO:MGI.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0042562; F:hormone binding; ISO:MGI.
DR GO; GO:0004977; F:melanocortin receptor activity; ISO:MGI.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; ISO:MGI.
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; IPR000621; Melancort_rcpt_5.
DR InterPro; IPR001671; Melcrt_ACTH_rcpt.
DR PANTHER; PTHR22750:SF5; PTHR22750:SF5; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00534; MCRFAMILY.
DR PRINTS; PR00535; MELNOCORTINR.
DR PRINTS; PR01063; MELNOCORTN5R.
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; G-protein coupled receptor; Glycoprotein; Lipoprotein;
KW Membrane; Palmitate; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..325
FT /note="Melanocortin receptor 5"
FT /id="PRO_0000069729"
FT TOPO_DOM 1..37
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 38..61
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 62..73
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 74..97
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 98..114
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..138
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 139..155
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..179
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 180..186
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..211
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 212..239
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..265
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 266..273
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..297
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 298..325
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT LIPID 311
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT LIPID 312
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 11
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 15
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 74
FT /note="F -> Y (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 325 AA; 36953 MW; 5A014D1C1E0157EE CRC64;
MNSSSTLTVL NLTLNASEDG ILGSNVKNKS LACEEMGIAV EVFLTLGLVS LLENILVIGA
IVKNKNLHSP MYFFVGSLAV ADMLVSMSNA WETVTIYLLN NKHLVIADTF VRHIDNVFDS
MICISVVASM CSLLAIAVDR YITIFYALRY HHIMTARRSG VIIACIWTFC ISCGIVFIIY
YESKYVIICL ISMFFTMLFF MVSLYIHMFL LARNHVKRIA ASPRYNSVRQ RTSMKGAITL
TMLLGIFIVC WSPFFLHLIL MISCPQNVYC SCFMSYFNMY LILIMCNSVI DPLIYALRSQ
EMRRTFKEIV CCHGFRRPCR LLGGY
