MC5R_RAT
ID MC5R_RAT Reviewed; 325 AA.
AC P35345;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Melanocortin receptor 5;
DE Short=MC5-R;
GN Name=Mc5r;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Corpus striatum;
RX PubMed=8179577; DOI=10.1006/bbrc.1994.1550;
RA Griffon N., Mignon V., Facchinetti P., Diaz J., Schwartz J.-C.,
RA Sokoloff P.;
RT "Molecular cloning and characterization of the rat fifth melanocortin
RT receptor.";
RL Biochem. Biophys. Res. Commun. 200:1007-1014(1994).
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: Very low expression levels is detected in brain,
CC while high levels are found in adrenals, stomach, lung and spleen.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; L27081; AAA41577.1; -; mRNA.
DR PIR; JC2193; JC2193.
DR RefSeq; NP_037314.1; NM_013182.2.
DR RefSeq; XP_017456350.1; XM_017600861.1.
DR AlphaFoldDB; P35345; -.
DR SMR; P35345; -.
DR STRING; 10116.ENSRNOP00000022364; -.
DR BindingDB; P35345; -.
DR ChEMBL; CHEMBL2701; -.
DR GlyGen; P35345; 3 sites.
DR PhosphoSitePlus; P35345; -.
DR PaxDb; P35345; -.
DR Ensembl; ENSRNOT00000022364; ENSRNOP00000022364; ENSRNOG00000016685.
DR GeneID; 25726; -.
DR KEGG; rno:25726; -.
DR UCSC; RGD:3058; rat.
DR CTD; 4161; -.
DR RGD; 3058; Mc5r.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01030000234510; -.
DR HOGENOM; CLU_009579_13_0_1; -.
DR InParanoid; P35345; -.
DR OMA; LYCSCFM; -.
DR OrthoDB; 877700at2759; -.
DR PhylomeDB; P35345; -.
DR Reactome; R-RNO-375276; Peptide ligand-binding receptors.
DR PRO; PR:P35345; -.
DR Proteomes; UP000002494; Chromosome 18.
DR Bgee; ENSRNOG00000016685; Expressed in esophagus and 3 other tissues.
DR Genevisible; P35345; RN.
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:0042562; F:hormone binding; IDA:RGD.
DR GO; GO:0004977; F:melanocortin receptor activity; IDA:RGD.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; ISO:RGD.
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_0000069732"
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 15
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 325 AA; 37050 MW; 4E19FF1ABE8A6BDC CRC64;
MNSSSHLTLL DLTLNASEDN ILGQNVNNKS SACEDMGIAV EVFLTLGLVS LLENILVIGA
IVKNKNLHSP MYFFVGSLAV ADMLVSMSNA WETITIYLIN NKHVVIADTF VRHIDNVFDS
MICISVVASM CSLLAIAVDR YITIFYALRY HHIMTARRSG VIIACIWTFC ISCGIVFIIY
YESKYVIVCL ISMFFTMLFF MVSLYIHMFL LARNHVKRIA ASPRYNSVRQ RASMKGAITL
TMLLGIFIVC WSPFFLHLIL MISCPQNVYC ACFMSYFNMY LILIMCNSVI DPLIYALRSQ
EMRRTFKEII CCHGFRRTCT LLGRY
