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 24-JAN-2024, entry version 89.
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 GlyCosmos; Q9TU77; 2 sites, No reported glycans.
DR PaxDb; 9940-ENSOARP00000004217; -.
DR GeneID; 443482; -.
DR KEGG; oas:443482; -.
DR CTD; 4158; -.
DR eggNOG; KOG3656; Eukaryota.
DR OrthoDB; 4160596at2759; -.
DR Proteomes; UP000002356; Unplaced.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004978; F:corticotropin receptor activity; IEA:InterPro.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
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; ADRENOCORTICOTROPIC HORMONE RECEPTOR; 1.
DR PANTHER; PTHR22750; G-PROTEIN COUPLED RECEPTOR; 1.
DR Pfam; PF00001; 7tm_1; 2.
DR PRINTS; PR00520; ACTROPHINR.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00534; MCRFAMILY.
DR SMART; SM01381; 7TM_GPCR_Srsx; 1.
DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 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
//
