ACTHR_PIG
ID ACTHR_PIG Reviewed; 297 AA.
AC Q8HYN8;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 107.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX PubMed=12464015; DOI=10.1046/j.1365-2052.2002.00899.x;
RA Jacobs K., Van Poucke M., Mattheeuws M., Chardon P., Yerle M., Rohrer G.,
RA Van Zeveren A., Peelman L.J.;
RT "Characterization of the porcine melanocortin 2 receptor gene (MC2R).";
RL Anim. Genet. 33:415-421(2002).
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: Expressed in skin and adrenal gland tissues.
CC {ECO:0000269|PubMed:12464015}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AF450083; AAO13968.1; -; Genomic_DNA.
DR RefSeq; XP_003482080.1; XM_003482032.3.
DR RefSeq; XP_013854659.1; XM_013999205.1.
DR AlphaFoldDB; Q8HYN8; -.
DR SMR; Q8HYN8; -.
DR STRING; 9823.ENSSSCP00000020075; -.
DR PaxDb; Q8HYN8; -.
DR Ensembl; ENSSSCT00000045304; ENSSSCP00000074587; ENSSSCG00000039227.
DR Ensembl; ENSSSCT00005003833; ENSSSCP00005002246; ENSSSCG00005002526.
DR Ensembl; ENSSSCT00045051914; ENSSSCP00045036132; ENSSSCG00045030454.
DR Ensembl; ENSSSCT00070053548; ENSSSCP00070045393; ENSSSCG00070026700.
DR GeneID; 100739231; -.
DR KEGG; ssc:100739231; -.
DR CTD; 4158; -.
DR VGNC; VGNC:99701; MC2R.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01030000234510; -.
DR HOGENOM; CLU_009579_13_0_1; -.
DR InParanoid; Q8HYN8; -.
DR OMA; AVIWTFC; -.
DR OrthoDB; 988552at2759; -.
DR TreeFam; TF332646; -.
DR Proteomes; UP000008227; Chromosome 6.
DR Proteomes; UP000314985; Chromosome 6.
DR Bgee; ENSSSCG00000039227; Expressed in oocyte and 4 other tissues.
DR Genevisible; Q8HYN8; SS.
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_0000069058"
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"
SQ SEQUENCE 297 AA; 33283 MW; 494F17C9CF224954 CRC64;
MKHITDLYES VNSTMSNKSD CPPVVLPEEV FFTISVIGVL ENLIVLLAVI KNKNLQSPMY
FFICSLAISD MLGSLYKILE NILIIFRNMG YLEPRGGFES TADDVVDSLF ILSLLGSICS
LSAIAADRYI TIFHALQYQR LVTPRRAAVV LLIIWACCIG SGITIVTFSH HVPAVIAFTA
LFPLMLVFIL CLYGHMFLLA RSHARRVSTL PRANMKGAIT LTVLLGVFIF CWAPFVLHIL
LMTFCPADPY CACYLALFQV NAVLIMCNAI IDPFIYAFRS PELRDAFKKM IICKRYP
