ID   MC5R_SHEEP              Reviewed;         325 AA.
AC   P41983;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Melanocortin receptor 5;
DE            Short=MC5-R;
GN   Name=MC5R;
OS   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Ovis.
OX   NCBI_TaxID=9940;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Pituitary anterior lobe;
RX   PubMed=8060485; DOI=10.1677/jme.0.0120203;
RA   Barrett P., Macdonald A., Helliwell R., Davidson G., Morgan P.J.;
RT   "Cloning and expression of a new member of the melanocyte-stimulating
RT   hormone receptor family.";
RL   J. Mol. Endocrinol. 12:203-213(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   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; Z31369; CAA83239.1; -; Genomic_DNA.
DR   PIR; I46416; I46416.
DR   AlphaFoldDB; P41983; -.
DR   SMR; P41983; -.
DR   STRING; 9940.ENSOARP00000002365; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   Proteomes; UP000002356; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004977; F:melanocortin receptor activity; IEA:InterPro.
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_0000069733"
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   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;  36585 MW;  DEA75992BCC4F934 CRC64;
     MNSSFHLHFL DLGLNATEGN LSGLSVRNAS SPCEDMGIAV EVFLALGLIS LLENILVIGA
     IVRNRNLHIP MYFFVGSLAV ADMLVSLSNF WETITIYLLT NKHLVMADAS VRHLDNVFDS
     MICISVVASM CSLLAIAVDR YVTIFCRLRY QRIMTGRRSG AIIAGIWAFC TSCGTVFIVY
     YESTYVVVCL IAMFLTMLLL MASLYTHMFL LARTHVRRIA ALPGHSSVRQ RTGVKGAITL
     AMLLGVFIIC WAPFFLHLIL MISCPQNLYC SCFMSHFNMY LILIMCNSVI DPLIYAFRSQ
     EMRKTFKEIV CFQGFRTPCR FPSTY