ACTHR_BOVIN
ID ACTHR_BOVIN Reviewed; 297 AA.
AC P34974;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 148.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Cone R.D., Mountjoy K.G.;
RT "Molecular genetics of the ACTH and melanocyte-stimulating hormone
RT receptors.";
RL Trends Endocrinol. Metab. 4:26-31(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Adrenal cortex;
RX PubMed=8305507; DOI=10.1016/0167-4889(94)90157-0;
RA Raikhinstein M., Zohar M., Hanukoglu I.;
RT "cDNA cloning and sequence analysis of the bovine adrenocorticotropic
RT hormone (ACTH) receptor.";
RL Biochim. Biophys. Acta 1220:329-332(1994).
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 -!- TISSUE SPECIFICITY: Melanocytes and corticoadrenal tissue.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; L23149; AAA30355.1; -; mRNA.
DR EMBL; X74501; CAA52610.1; -; mRNA.
DR PIR; I45849; I45849.
DR PIR; S42767; S42767.
DR RefSeq; NP_776534.1; NM_174109.2.
DR AlphaFoldDB; P34974; -.
DR SMR; P34974; -.
DR STRING; 9913.ENSBTAP00000014661; -.
DR PaxDb; P34974; -.
DR Ensembl; ENSBTAT00000014661; ENSBTAP00000014661; ENSBTAG00000011038.
DR GeneID; 281299; -.
DR KEGG; bta:281299; -.
DR CTD; 4158; -.
DR VEuPathDB; HostDB:ENSBTAG00000011038; -.
DR VGNC; VGNC:31293; MC2R.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01030000234510; -.
DR HOGENOM; CLU_009579_13_0_1; -.
DR InParanoid; P34974; -.
DR OMA; AVIWTFC; -.
DR OrthoDB; 988552at2759; -.
DR TreeFam; TF332646; -.
DR Reactome; R-BTA-375276; Peptide ligand-binding receptors.
DR Proteomes; UP000009136; Chromosome 24.
DR Bgee; ENSBTAG00000011038; Expressed in adrenal gland and 3 other tissues.
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:0004978; F:corticotropin receptor activity; IEA:InterPro.
DR GO; GO:0004930; F:G protein-coupled 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; 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..297
FT /note="Adrenocorticotropic hormone receptor"
FT /id="PRO_0000069052"
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..297
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"
FT CONFLICT 145..150
FT /note="HRALVI -> APCPRH (in Ref. 1; AAA30355)"
FT /evidence="ECO:0000305"
FT CONFLICT 278
FT /note="F -> L (in Ref. 2; CAA52610)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 297 AA; 33293 MW; 8B77A8C2E268BB1E CRC64;
MKHILNLYEN INSTARNNSD CPAVILPEEI FFTVSIVGVL ENLMVLLAVA KNKSLQSPMY
FFICSLAISD MLGSLYKILE NVLIMFKNMG YLEPRGSFES TADDVVDSLF ILSLLGSICS
LSVIAADRYI TIFHALQYHR IMTPHRALVI LTVLWAGCTG SGITIVTFSH HVPTVIAFTA
LFPLMLAFIL CLYVHMFLLA RSHTRRTPSL PKANMRGAVT LTVLLGVFIF CWAPFVLHVL
LMTFCPADPY CACYMSLFQV NGVLIMCNAI IDPFIYAFRS PELRVAFKKM VICNCYQ
