MC5R_PANTR
ID MC5R_PANTR Reviewed; 325 AA.
AC Q9TT23;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=Melanocortin receptor 5;
DE Short=MC5-R;
GN Name=MC5R;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11286624; DOI=10.1046/j.0022-202x.2001.01286.x;
RA Hatta N., Dixon C., Ray A.J., Phillips S.R., Cunliffe W.J., Dale M.,
RA Todd C., Meggit S., Birch-MacHin M.A., Rees J.L.;
RT "Expression, candidate gene, and population studies of the melanocortin 5
RT receptor.";
RL J. Invest. Dermatol. 116:564-570(2001).
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 -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AF208691; AAF19441.1; -; Genomic_DNA.
DR RefSeq; NP_001009119.1; NM_001009119.1.
DR AlphaFoldDB; Q9TT23; -.
DR SMR; Q9TT23; -.
DR GeneID; 468599; -.
DR KEGG; ptr:468599; -.
DR CTD; 4161; -.
DR InParanoid; Q9TT23; -.
DR OrthoDB; 877700at2759; -.
DR Proteomes; UP000002277; Unplaced.
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:0004977; F:melanocortin receptor activity; IBA:GO_Central.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
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 3: Inferred from homology;
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_0000069730"
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 20
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; 36647 MW; 9AFD17F0ACA059BB CRC64;
MNSSFHLHFL DLNLNATEGN LSGPNVKNKS SPCEDMGIAV EVFLTLGVIS LLENILVIGA
IVKNKNLHSP MYFFVCSLAV ADMLVSMSSA WETITIYLLN NKHLVIADAF VRHIDNVFDS
MICISVVASM CSLLAIAVDR YVTIFYALRY HHIMTARRSG AIIAGIWAFC TGCGIVFILY
SESTYVILCL ISMFFAMLFL LVSLYIHMFL LARTHVKRIA ALPRASSARQ RTSMQGAVTV
TMLLGVFTVC WAPFFLHLTL MLSCPQNLYC SCFMSHFNMY LILIMCNSVM DPLIYAFRSQ
EMRKTFKEII CCRGFRIACS FPRRD
