ACTHR_MOUSE
ID ACTHR_MOUSE Reviewed; 296 AA.
AC Q64326;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 165.
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; Synonyms=Acthr;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7875603; DOI=10.1016/0378-1119(94)00768-n;
RA Kubo M., Ishizuka T., Kijima H., Kakinuma M., Koike T.;
RT "Cloning of a mouse adrenocorticotropin receptor-encoding gene.";
RL Gene 153:279-280(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7626130; DOI=10.1006/bbrc.1995.2056;
RA Cammas F.M., Kapas S., Barker S., Clark A.J.;
RT "Cloning, characterization and expression of a functional mouse ACTH
RT receptor.";
RL Biochem. Biophys. Res. Commun. 212:912-918(1995).
CC -!- FUNCTION: Receptor for corticotropin (ACTH). This receptor is mediated
CC by G proteins (G(s)) 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; D31952; BAA06722.1; -; Genomic_DNA.
DR EMBL; S78985; AAB34919.1; -; Genomic_DNA.
DR CCDS; CCDS29328.1; -.
DR PIR; JC4046; JC4046.
DR RefSeq; NP_001258645.1; NM_001271716.1.
DR RefSeq; NP_001258646.1; NM_001271717.1.
DR RefSeq; NP_001288301.1; NM_001301372.1.
DR RefSeq; NP_032586.1; NM_008560.3.
DR AlphaFoldDB; Q64326; -.
DR SMR; Q64326; -.
DR STRING; 10090.ENSMUSP00000058691; -.
DR BindingDB; Q64326; -.
DR ChEMBL; CHEMBL2279; -.
DR GuidetoPHARMACOLOGY; 283; -.
DR GlyGen; Q64326; 2 sites.
DR iPTMnet; Q64326; -.
DR PhosphoSitePlus; Q64326; -.
DR PaxDb; Q64326; -.
DR PRIDE; Q64326; -.
DR Antibodypedia; 21964; 286 antibodies from 32 providers.
DR DNASU; 17200; -.
DR Ensembl; ENSMUST00000052347; ENSMUSP00000058691; ENSMUSG00000045569.
DR GeneID; 17200; -.
DR KEGG; mmu:17200; -.
DR UCSC; uc008fnm.2; mouse.
DR CTD; 4158; -.
DR MGI; MGI:96928; Mc2r.
DR VEuPathDB; HostDB:ENSMUSG00000045569; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01030000234510; -.
DR HOGENOM; CLU_009579_13_0_1; -.
DR InParanoid; Q64326; -.
DR OMA; AVIWTFC; -.
DR OrthoDB; 988552at2759; -.
DR PhylomeDB; Q64326; -.
DR TreeFam; TF332646; -.
DR Reactome; R-MMU-375276; Peptide ligand-binding receptors.
DR Reactome; R-MMU-418555; G alpha (s) signalling events.
DR BioGRID-ORCS; 17200; 1 hit in 70 CRISPR screens.
DR PRO; PR:Q64326; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q64326; protein.
DR Bgee; ENSMUSG00000045569; Expressed in adrenal gland and 31 other tissues.
DR ExpressionAtlas; Q64326; baseline and differential.
DR Genevisible; Q64326; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0001890; P:placenta development; IEA:Ensembl.
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 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..296
FT /note="Adrenocorticotropic hormone receptor"
FT /id="PRO_0000069056"
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..296
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 296 AA; 33982 MW; 8ECB3D9A028CB9B8 CRC64;
MKHIINSYEH TNDTARNNSD CPDVVLPEEI FFTISVIGIL ENLIVLLAVI KNKNLQSPMY
FFICSLAISD MLGSLYKILE NILIMFRNMG YLKPRGSFES TADDIIDCMF ILSLLGSIFS
LSVIAADRYI TIFHALQYHS IVTMRRTIIT LTIIWMFCTG SGITMVIFSH HIPTVLTFTS
LFPLMLVFIL CLYIHMFLLA RSHARKISTL PRTNMKGAMT LTILLGVFIF CWAPFVLHVL
LMTFCPNNPY CVCYMSLFQV NGMLIMCNAV IDPFIYAFRS PELRDAFKRM LFCNRY
