ACTHR_CAVPO
ID ACTHR_CAVPO Reviewed; 297 AA.
AC Q9Z1S9;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 115.
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 Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Hartley;
RA Fang V.S., Juan C.-C., Lin Y.-S., Liu S.-T., Ho L.-T.;
RT "Cloning of the guinea pig corticotropin (ACTH)-receptor gene.";
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
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; AF104058; AAD13614.1; -; mRNA.
DR RefSeq; NP_001166453.1; NM_001172982.1.
DR AlphaFoldDB; Q9Z1S9; -.
DR SMR; Q9Z1S9; -.
DR STRING; 10141.ENSCPOP00000017261; -.
DR Ensembl; ENSCPOT00000010788; ENSCPOP00000017261; ENSCPOG00000010691.
DR GeneID; 100135574; -.
DR KEGG; cpoc:100135574; -.
DR CTD; 4158; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01030000234510; -.
DR HOGENOM; CLU_009579_13_0_1; -.
DR InParanoid; Q9Z1S9; -.
DR OMA; AVIWTFC; -.
DR OrthoDB; 988552at2759; -.
DR TreeFam; TF332646; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000010691; Expressed in adrenal gland and 1 other tissue.
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 GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IEA:Ensembl.
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_0000069053"
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 296
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 297 AA; 33715 MW; 4FA0B6FCA2D3C1F6 CRC64;
MKHIIHASGN VNGTARNNSD CPHVALPEEI FFIISITGVL ENLIIILAVI KNKNLQFPMY
FFICSLAISD MLGSLYKILE SILIMFRNMG YFKPHGSFET TTDDIIDTMF ILSLLGSIFS
LLAIAVDRYI TIFHALQYHS IVTMHRTIAV LSIIWTFCIG SGITMVLFSH HVPTVLTFTS
LFPLMLVFIL CLYVHMFLMA RSHARNISTL PRGNMRGAIT LTILLGVFIF CWAPFILHIL
LVTFCPNNPY CTCYISLFHV NGMLIMCNAV IDPFIYAFRS PELRSAFRRM ISYSKCL
