ID   ACTHR_SHEEP             Reviewed;         295 AA.
AC   Q9TU77;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Adrenocorticotropic hormone receptor;
DE            Short=ACTH receptor;
DE            Short=ACTH-R;
DE   AltName: Full=Adrenocorticotropin receptor;
DE   AltName: Full=Melanocortin receptor 2;
DE            Short=MC2-R;
GN   Name=MC2R;
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 [MRNA].
RC   STRAIN=Merino; TISSUE=Adrenal gland;
RA   Wang J., Rose J.C.;
RT   "Ovine adrenal ACTH receptor: cDNA cloning and developmental changes of
RT   mRNA levels.";
RL   Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Receptor for corticotropin (ACTH). This receptor is mediated
CC       by G proteins which activate adenylate cyclase (cAMP).
CC   -!- SUBUNIT: Interacts with MRAP; increasing ligand-sensitivity and
CC       generation of cAMP. Interacts with MRAP2; competing with MRAP for
CC       binding to MC2R and impairing the binding of corticotropin (ACTH) (By
CC       similarity). {ECO:0000250}.
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; AF116874; AAF04781.1; -; mRNA.
DR   RefSeq; NP_001009442.1; NM_001009442.1.
DR   AlphaFoldDB; Q9TU77; -.
DR   SMR; Q9TU77; -.
DR   STRING; 9940.ENSOARP00000004217; -.
DR   GeneID; 443482; -.
DR   KEGG; oas:443482; -.
DR   CTD; 4158; -.
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:0004978; F:corticotropin receptor activity; IEA:InterPro.
DR   InterPro; IPR001168; ACTH_rcpt.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   InterPro; IPR001671; Melcrt_ACTH_rcpt.
DR   PANTHER; PTHR22750:SF3; PTHR22750:SF3; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00520; ACTROPHINR.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00534; MCRFAMILY.
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..295
FT                   /note="Adrenocorticotropic hormone receptor"
FT                   /id="PRO_0000069059"
FT   TOPO_DOM        1..23
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        24..49
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        50..58
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        59..79
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        80..104
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        105..126
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        127..147
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        148..168
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        169..180
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        181..199
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        200..217
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        218..244
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        245..256
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        257..278
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        279..295
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   LIPID           293
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        12
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        17
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   295 AA;  33019 MW;  54C6F7FAA4A72C40 CRC64;
     MRHILNLYEN INSTARNNSD CPAVILPEEI FFTVSIVGVL ENLMVLLAVA KNKSLQSPMY
     FFICSLAISD MLGSLYKILE NVLIMFRNMG YLEPRGSFES TADDVVDSLF ILSLLGSICS
     LSVIAADRYI TIFHALQYHS IVTMHRALVV LTVLWAGCTG SGITIVTFSH HVPTVIAFTA
     LFPLMLAFIL CLYVHMFLLA RSHARRTSSL PKANMRGAIT LTVLLGVFIF CWAPFVLHVL
     LMTFCPADPY CACYMSLFQV NGVLIMCNAV IDPFIYAFRS PELRVAFKKM VICNW