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Adrenocorticotropic hormone receptor (ACTH receptor) (ACTH-R) (Adrenocorticotropin receptor) (Melanocortin receptor 2) (MC2-R)

 ACTHR_HUMAN             Reviewed;         297 AA.
Q01718; A8K016; Q3MI45; Q504X6;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
01-JUL-1993, sequence version 1.
20-DEC-2017, entry version 166.
RecName: Full=Adrenocorticotropic hormone receptor;
Short=ACTH receptor;
Short=ACTH-R;
AltName: Full=Adrenocorticotropin receptor;
AltName: Full=Melanocortin receptor 2;
Short=MC2-R;
Name=MC2R; Synonyms=ACTHR;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Skin;
PubMed=1325670; DOI=10.1126/science.1325670;
Mountjoy K.G., Robbins L.S., Mortrud M., Cone R.D.;
"The cloning of a family of genes that encode the melanocortin
receptors.";
Science 257:1248-1251(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Suwa M., Sato T., Okouchi I., Arita M., Futami K., Matsumoto S.,
Tsutsumi S., Aburatani H., Asai K., Akiyama Y.;
"Genome-wide discovery and analysis of human seven transmembrane helix
receptor genes.";
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kopatz S.A., Aronstam R.S., Sharma S.V.;
"cDNA clones of human proteins involved in signal transduction
sequenced by the Guthrie cDNA resource center (www.cdna.org).";
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Adrenal gland;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-293.
PubMed=8463333;
Gantz I., Konda Y., Tashiro T., Shimoto Y., Miwa H., Munzert G.,
Watson S.J., Delvalle J., Yamada T.;
"Molecular cloning of a novel melanocortin receptor.";
J. Biol. Chem. 268:8246-8250(1993).
[8]
INTERACTION WITH MRAP.
PubMed=15654338; DOI=10.1038/ng1501;
Metherell L.A., Chapple J.P., Cooray S., David A., Becker C.,
Rueschendorf F., Naville D., Begeot M., Khoo B., Nuernberg P.,
Huebner A., Cheetham M.E., Clark A.J.L.;
"Mutations in MRAP, encoding a new interacting partner of the ACTH
receptor, cause familial glucocorticoid deficiency type 2.";
Nat. Genet. 37:166-170(2005).
[9]
FUNCTION, AND INTERACTION WITH MRAP AND MRAP2.
PubMed=19329486; DOI=10.1073/pnas.0809918106;
Chan L.F., Webb T.R., Chung T.T., Meimaridou E., Cooray S.N.,
Guasti L., Chapple J.P., Egertova M., Elphick M.R., Cheetham M.E.,
Metherell L.A., Clark A.J.;
"MRAP and MRAP2 are bidirectional regulators of the melanocortin
receptor family.";
Proc. Natl. Acad. Sci. U.S.A. 106:6146-6151(2009).
[10]
FUNCTION, AND INTERACTION WITH MRAP AND MRAP2.
PubMed=20371771; DOI=10.1126/scisignal.2000593;
Sebag J.A., Hinkle P.M.;
"Regulation of G protein-coupled receptor signaling: specific
dominant-negative effects of melanocortin 2 receptor accessory protein
2.";
Sci. Signal. 3:RA28-RA28(2010).
[11]
REVIEW ON GCCD1 VARIANTS.
Clark A.J.L., Weber A.;
"Molecular insights into inherited ACTH resistance syndromes.";
Trends Endocrinol. Metab. 5:209-214(1994).
[12]
VARIANT GCCD1 ILE-74.
PubMed=8094489; DOI=10.1016/0140-6736(93)90208-X;
Clark A.J.L., McLoughlin L., Grossman A.;
"Familial glucocorticoid deficiency associated with point mutation in
the adrenocorticotropin receptor.";
Lancet 341:461-462(1993).
[13]
VARIANT GCCD1 ARG-120.
PubMed=8227361; DOI=10.1172/JCI116853;
Tsigos C., Arai K., Hung W., Chrousos G.P.;
"Hereditary isolated glucocorticoid deficiency is associated with
abnormalities of the adrenocorticotropin receptor gene.";
J. Clin. Invest. 92:2458-2461(1993).
[14]
VARIANTS GCCD1 ASN-107 AND PHE-251.
PubMed=8636348; DOI=10.1210/jcem.81.4.8636348;
Naville D., Barjhoux L., Jaillard C., Faury D., Despert F., Esteva B.,
Durand P., Saez J.M., Begeot M.;
"Demonstration by transfection studies that mutations in the
adrenocorticotropin receptor gene are one cause of the hereditary
syndrome of glucocorticoid deficiency.";
J. Clin. Endocrinol. Metab. 81:1442-1448(1996).
[15]
VARIANTS GCCD1 ASN-103 AND TRP-137.
PubMed=10971458; DOI=10.1046/j.1365-2265.2000.01040.x;
Ishii T., Ogata T., Sasaki G., Sato S., Kinoshita E.I., Matsuo N.;
"Novel mutations of the ACTH receptor gene in a female adult patient
with adrenal unresponsiveness to ACTH.";
Clin. Endocrinol. (Oxf.) 53:389-392(2000).
[16]
VARIANTS GCCD1 ILE-74; TRP-137 AND CYS-254.
PubMed=12213892; DOI=10.1210/jc.2002-020501;
Fluck C.E., Martens J.W.M., Conte F.A., Miller W.L.;
"Clinical, genetic, and functional characterization of
adrenocorticotropin receptor mutations using a novel receptor assay.";
J. Clin. Endocrinol. Metab. 87:4318-4323(2002).
[17]
VARIANT PRO-137.
PubMed=20108423;
Mueller O.T., Coovadia A.;
"Novel human pathological mutations. Gene symbol: MC2R. Disease:
Glucocorticoid deficiency.";
Hum. Genet. 127:112-112(2010).
-!- FUNCTION: Receptor for corticotropin (ACTH). This receptor is
mediated by G proteins (G(s)) which activate adenylate cyclase
(cAMP). {ECO:0000269|PubMed:19329486,
ECO:0000269|PubMed:20371771}.
-!- SUBUNIT: Interacts with MRAP; increasing ligand-sensitivity and
generation of cAMP. Interacts with MRAP2; competing with MRAP for
binding to MC2R and impairing the binding of corticotropin (ACTH).
{ECO:0000269|PubMed:15654338, ECO:0000269|PubMed:19329486,
ECO:0000269|PubMed:20371771}.
-!- INTERACTION:
Q8TCY5:MRAP; NbExp=2; IntAct=EBI-9537171, EBI-9538727;
-!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
-!- TISSUE SPECIFICITY: Melanocytes and corticoadrenal tissue.
-!- DISEASE: Glucocorticoid deficiency 1 (GCCD1) [MIM:202200]: A rare,
potentially lethal, autosomal recessive disorder characterized by
resistance to ACTH action on the adrenal cortex, adrenal
insufficiency and an inability of the adrenal cortex to produce
cortisol. It usually presents in the neonatal period or in early
childhood with episodes of hypoglycemia and other symptoms related
to cortisol deficiency, including failure to thrive, recurrent
illnesses or infections, convulsions, and shock. In a small number
of patients hypoglycemia can be sufficiently severe and persistent
that it leads to serious long-term neurological damage or death.
The diagnosis is readily confirmed with a low plasma cortisol
measurement in the presence of an elevated ACTH level, and normal
aldosterone and plasma renin measurements.
{ECO:0000269|PubMed:10971458, ECO:0000269|PubMed:12213892,
ECO:0000269|PubMed:8094489, ECO:0000269|PubMed:8227361,
ECO:0000269|PubMed:8636348}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
{ECO:0000255|PROSITE-ProRule:PRU00521}.
-----------------------------------------------------------------------
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EMBL; X65633; CAA46587.1; -; Genomic_DNA.
EMBL; AB065915; BAC06130.1; -; Genomic_DNA.
EMBL; AK289381; BAF82070.1; -; mRNA.
EMBL; AK315319; BAG37722.1; -; mRNA.
EMBL; CH471113; EAX01503.1; -; Genomic_DNA.
EMBL; BC069074; AAH69074.1; -; mRNA.
EMBL; BC094710; AAH94710.1; -; mRNA.
EMBL; BC104169; AAI04170.1; -; mRNA.
EMBL; BC104170; AAI04171.1; -; mRNA.
EMBL; AY225229; AAO67714.1; -; Genomic_DNA.
CCDS; CCDS11869.1; -.
PIR; C43265; C43265.
RefSeq; NP_000520.1; NM_000529.2.
RefSeq; NP_001278840.1; NM_001291911.1.
RefSeq; XP_016881270.1; XM_017025781.1.
UniGene; Hs.248144; -.
ProteinModelPortal; Q01718; -.
BioGrid; 110328; 2.
DIP; DIP-29949N; -.
IntAct; Q01718; 2.
STRING; 9606.ENSP00000333821; -.
BindingDB; Q01718; -.
ChEMBL; CHEMBL1965; -.
DrugBank; DB01285; Corticotropin.
DrugBank; DB01284; Tetracosactide.
GuidetoPHARMACOLOGY; 283; -.
TCDB; 9.A.14.2.4; the g-protein-coupled receptor (gpcr) family.
iPTMnet; Q01718; -.
PhosphoSitePlus; Q01718; -.
BioMuta; MC2R; -.
DMDM; 399002; -.
PaxDb; Q01718; -.
PeptideAtlas; Q01718; -.
PRIDE; Q01718; -.
Ensembl; ENST00000327606; ENSP00000333821; ENSG00000185231.
GeneID; 4158; -.
KEGG; hsa:4158; -.
UCSC; uc002ksp.2; human.
CTD; 4158; -.
DisGeNET; 4158; -.
EuPathDB; HostDB:ENSG00000185231.4; -.
GeneCards; MC2R; -.
HGNC; HGNC:6930; MC2R.
MalaCards; MC2R; -.
MIM; 202200; phenotype.
MIM; 607397; gene.
neXtProt; NX_Q01718; -.
OpenTargets; ENSG00000185231; -.
Orphanet; 361; Familial glucocorticoid deficiency.
PharmGKB; PA30674; -.
eggNOG; KOG3656; Eukaryota.
eggNOG; ENOG410XRW9; LUCA.
GeneTree; ENSGT00770000120529; -.
HOGENOM; HOG000246927; -.
HOVERGEN; HBG108148; -.
InParanoid; Q01718; -.
KO; K04200; -.
OMA; PAIYAFR; -.
OrthoDB; EOG091G0BVW; -.
PhylomeDB; Q01718; -.
TreeFam; TF332646; -.
Reactome; R-HSA-375276; Peptide ligand-binding receptors.
Reactome; R-HSA-418555; G alpha (s) signalling events.
Reactome; R-HSA-5579031; Defective ACTH causes Obesity and Pro-opiomelanocortinin deficiency (POMCD).
SIGNOR; Q01718; -.
GeneWiki; ACTH_receptor; -.
GenomeRNAi; 4158; -.
PRO; PR:Q01718; -.
Proteomes; UP000005640; Chromosome 18.
Bgee; ENSG00000185231; -.
CleanEx; HS_MC2R; -.
ExpressionAtlas; Q01718; baseline and differential.
Genevisible; Q01718; HS.
GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0004978; F:corticotropin receptor activity; TAS:ProtInc.
GO; GO:0004977; F:melanocortin receptor activity; TAS:ProtInc.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; TAS:Reactome.
GO; GO:0007187; P:G-protein coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; TAS:ProtInc.
GO; GO:0001890; P:placenta development; IEA:Ensembl.
GO; GO:0030819; P:positive regulation of cAMP biosynthetic process; IDA:BHF-UCL.
InterPro; IPR001168; ACTH_rcpt.
InterPro; IPR000276; GPCR_Rhodpsn.
InterPro; IPR017452; GPCR_Rhodpsn_7TM.
InterPro; IPR001671; Melcrt_ACTH_rcpt.
PANTHER; PTHR22750:SF3; PTHR22750:SF3; 1.
Pfam; PF00001; 7tm_1; 1.
PRINTS; PR00520; ACTROPHINR.
PRINTS; PR00237; GPCRRHODOPSN.
PRINTS; PR00534; MCRFAMILY.
SMART; SM01381; 7TM_GPCR_Srsx; 1.
PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Disease mutation;
G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane;
Palmitate; Polymorphism; Receptor; Reference proteome; Transducer;
Transmembrane; Transmembrane helix.
CHAIN 1 297 Adrenocorticotropic hormone receptor.
/FTId=PRO_0000069054.
TOPO_DOM 1 23 Extracellular. {ECO:0000250}.
TRANSMEM 24 49 Helical; Name=1. {ECO:0000250}.
TOPO_DOM 50 58 Cytoplasmic. {ECO:0000250}.
TRANSMEM 59 79 Helical; Name=2. {ECO:0000250}.
TOPO_DOM 80 104 Extracellular. {ECO:0000250}.
TRANSMEM 105 126 Helical; Name=3. {ECO:0000250}.
TOPO_DOM 127 147 Cytoplasmic. {ECO:0000250}.
TRANSMEM 148 168 Helical; Name=4. {ECO:0000250}.
TOPO_DOM 169 180 Extracellular. {ECO:0000250}.
TRANSMEM 181 199 Helical; Name=5. {ECO:0000250}.
TOPO_DOM 200 217 Cytoplasmic. {ECO:0000250}.
TRANSMEM 218 244 Helical; Name=6. {ECO:0000250}.
TOPO_DOM 245 256 Extracellular. {ECO:0000250}.
TRANSMEM 257 278 Helical; Name=7. {ECO:0000250}.
TOPO_DOM 279 297 Cytoplasmic. {ECO:0000250}.
LIPID 293 293 S-palmitoyl cysteine. {ECO:0000255}.
CARBOHYD 12 12 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 17 17 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VARIANT 27 27 P -> R (in dbSNP:rs28926178).
/FTId=VAR_003509.
VARIANT 74 74 S -> I (in GCCD1; complete loss of
activity; dbSNP:rs104894658).
{ECO:0000269|PubMed:12213892,
ECO:0000269|PubMed:8094489}.
/FTId=VAR_003510.
VARIANT 103 103 D -> N (in GCCD1; dbSNP:rs768093045).
{ECO:0000269|PubMed:10971458}.
/FTId=VAR_010702.
VARIANT 107 107 D -> N (in GCCD1; dbSNP:rs104894661).
{ECO:0000269|PubMed:8636348}.
/FTId=VAR_015095.
VARIANT 120 120 S -> R (in GCCD1; dbSNP:rs104894656).
{ECO:0000269|PubMed:8227361}.
/FTId=VAR_003511.
VARIANT 128 128 R -> C (in GCCD1; dbSNP:rs104894657).
/FTId=VAR_003512.
VARIANT 137 137 R -> P (found in a glucocorticoid
deficiency patient carrying also mutation
I-74). {ECO:0000269|PubMed:20108423}.
/FTId=VAR_064986.
VARIANT 137 137 R -> W (in GCCD1; partial loss of
ACTIVITY; dbSNP:rs104894660).
{ECO:0000269|PubMed:10971458,
ECO:0000269|PubMed:12213892}.
/FTId=VAR_010703.
VARIANT 146 146 R -> H (in GCCD1; dbSNP:rs758709668).
/FTId=VAR_003513.
VARIANT 251 251 C -> F (in GCCD1; dbSNP:rs104894662).
{ECO:0000269|PubMed:8636348}.
/FTId=VAR_015096.
VARIANT 254 254 Y -> C (in GCCD1; complete loss of
activity; dbSNP:rs28940892).
{ECO:0000269|PubMed:12213892}.
/FTId=VAR_015295.
VARIANT 278 278 F -> C (in dbSNP:rs28926182).
/FTId=VAR_049369.
SEQUENCE 297 AA; 33927 MW; 66EE31961ABB8773 CRC64;
MKHIINSYEN INNTARNNSD CPRVVLPEEI FFTISIVGVL ENLIVLLAVF KNKNLQAPMY
FFICSLAISD MLGSLYKILE NILIILRNMG YLKPRGSFET TADDIIDSLF VLSLLGSIFS
LSVIAADRYI TIFHALRYHS IVTMRRTVVV LTVIWTFCTG TGITMVIFSH HVPTVITFTS
LFPLMLVFIL CLYVHMFLLA RSHTRKISTL PRANMKGAIT LTILLGVFIF CWAPFVLHVL
LMTFCPSNPY CACYMSLFQV NGMLIMCNAV IDPFIYAFRS PELRDAFKKM IFCSRYW


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