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Melanocortin receptor 4 (MC4-R)

 MC4R_HUMAN              Reviewed;         332 AA.
P32245; B2RAC3; Q16317; Q3MIJ6;
01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
25-OCT-2004, sequence version 2.
25-APR-2018, entry version 184.
RecName: Full=Melanocortin receptor 4;
Short=MC4-R;
Name=MC4R;
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], AND VARIANT ILE-103.
PubMed=8392067;
Gantz I., Miwa H., Konda Y., Shimoto Y., Tashiro T., Waston S.J.,
Delvalle J.;
"Molecular cloning, expression, and gene localization of a fourth
melanocortin receptor.";
J. Biol. Chem. 268:15174-15179(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ILE-103.
PubMed=7854347; DOI=10.1210/mend.8.10.7854347;
Mountjoy K.G., Mortrud M.T., Low M.J., Simerly R.B., Cone R.D.;
"Localization of the melanocortin-4 receptor (MC4-R) in neuroendocrine
and autonomic control circuits in the brain.";
Mol. Endocrinol. 8:1298-1308(1994).
[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=Subthalamic nucleus;
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.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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
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]
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).
[8]
INTERACTION WITH MGRN1.
PubMed=19737927; DOI=10.1074/jbc.M109.028100;
Perez-Oliva A.B., Olivares C., Jimenez-Cervantes C.,
Garcia-Borron J.C.;
"Mahogunin ring finger-1 (MGRN1) E3 ubiquitin ligase inhibits
signaling from melanocortin receptor by competition with Galphas.";
J. Biol. Chem. 284:31714-31725(2009).
[9]
INTERCHAIN DISULFIDE BOND, AND SUBUNIT.
PubMed=23088915; DOI=10.1016/j.bbamem.2012.10.011;
Chapman K.L., Findlay J.B.;
"The melanocortin 4 receptor: oligomer formation, interaction sites
and functional significance.";
Biochim. Biophys. Acta 1828:535-542(2013).
[10]
VARIANTS OBESITY PHE-30; VAL-37; LEU-78; TRP-165; SER-252 AND THR-317,
AND VARIANTS MET-112 AND LEU-251.
PubMed=10199800; DOI=10.1210/jcem.84.4.5728;
Hinney A., Schmidt A., Nottebom K., Heibult O., Becker I., Ziegler A.,
Gerber G., Sina M., Gorg T., Mayer H., Siegfried W., Fichter M.,
Remschmidt H., Hebebrand J.;
"Several mutations in the melanocortin-4 receptor gene including a
nonsense and a frameshift mutation associated with dominantly
inherited obesity in humans.";
J. Clin. Endocrinol. Metab. 84:1483-1486(1999).
[11]
VARIANT OBESITY SER-274.
PubMed=11443223; DOI=10.1210/jcem.86.7.7809;
Mergen M., Mergen H., Ozata M., Oner R., Oner C.;
"A novel melanocortin 4 receptor (MC4R) gene mutation associated with
morbid obesity.";
J. Clin. Endocrinol. Metab. 86:3448-3448(2001).
[12]
VARIANTS OBESITY MET-50; CYS-58; SER-102 AND VAL-170, AND VARIANTS
ILE-103 AND LEU-251.
PubMed=11487744; DOI=10.1067/mpd.2001.116284;
Dubern B., Clement K., Pelloux V., Froguel P., Girardet J.-P.,
Guy-Grand B., Tounian P.;
"Mutational analysis of melanocortin-4 receptor, agouti-related
protein, and alpha-melanocyte-stimulating hormone genes in severely
obese children.";
J. Pediatr. 139:204-209(2001).
[13]
VARIANTS OBESITY SER-62; ASP-97; PRO-106; LYS-125; GLN-165; THR-175;
ILE-253; TYR-271 AND SER-316, AND CHARACTERIZATION OF VARIANTS OBESITY
SER-62; ASP-97; PRO-106; LYS-125; GLN-165; THR-175; ILE-253; TYR-271
AND SER-316.
PubMed=12588803; DOI=10.1093/hmg/ddg057;
Yeo G.S.H., Lank E.J., Farooqi I.S., Keogh J., Challis B.G.,
O'Rahilly S.;
"Mutations in the human melanocortin-4 receptor gene associated with
severe familial obesity disrupts receptor function through multiple
molecular mechanisms.";
Hum. Mol. Genet. 12:561-574(2003).
[14]
VARIANT OBESITY 88-VAL--LEU-92 DEL, AND CHARACTERIZATION OF VARIANT
OBESITY 88-VAL--LEU-92 DEL.
PubMed=14671178; DOI=10.1210/jc.2003-030903;
Donohoue P.A., Tao Y.-X., Collins M., Yeo G.S.H., O'Rahilly S.,
Segaloff D.L.;
"Deletion of codons 88-92 of the melanocortin-4 receptor gene: a novel
deleterious mutation in an obese female.";
J. Clin. Endocrinol. Metab. 88:5841-5845(2003).
[15]
VARIANTS OBESITY ALA-11; SER-62; ASP-97; LYS-125; GLN-165; THR-175;
TYR-271; ARG-271 AND SER-316, VARIANTS ILE-103; MET-112 AND LEU-251,
CHARACTERIZATION OF VARIANTS OBESITY ALA-11; SER-62; ASP-97; LYS-125;
GLN-165; THR-175; TYR-271 AND SER-316, CHARACTERIZATION OF VARIANTS
ILE-103; MET-112 AND LEU-251, AND FUNCTION.
PubMed=12646665; DOI=10.1056/NEJMoa022050;
Farooqi I.S., Keogh J.M., Yeo G.S.H., Lank E.J., Cheetham T.,
O'Rahilly S.;
"Clinical spectrum of obesity and mutations in the melanocortin 4
receptor gene.";
N. Engl. J. Med. 348:1085-1095(2003).
[16]
VARIANT OBESITY LEU-127, VARIANTS ILE-103; MET-112; THR-226 AND
LEU-251, CHARACTERIZATION OF VARIANT OBESITY LEU-127, AND
CHARACTERIZATION OF VARIANTS MET-112 AND THR-226.
PubMed=14764818; DOI=10.1210/jc.2003-031182;
Valli-Jaakola K., Lipsanen-Nyman M., Oksanen L., Hollenberg A.N.,
Kontula K., Bjoerbaek C., Schalin-Jaentti C.;
"Identification and characterization of melanocortin-4 receptor gene
mutations in morbidly obese Finnish children and adults.";
J. Clin. Endocrinol. Metab. 89:940-945(2004).
[17]
VARIANTS OBESITY TYR-36; THR-102; GLN-165; THR-175; ASP-181; VAL-219
AND PHE-325, VARIANTS ILE-103; MET-112 AND LEU-251, AND
CHARACTERIZATION OF VARIANTS OBESITY TYR-36; THR-102; GLN-165;
ASP-181; VAL-219 AND PHE-325.
PubMed=15486053; DOI=10.1210/jc.2004-0497;
Larsen L.H., Echwald S.M., Soerensen T.I.A., Andersen T., Wulff B.S.,
Pedersen O.;
"Prevalence of mutations and functional analyses of melanocortin 4
receptor variants identified among 750 men with juvenile-onset
obesity.";
J. Clin. Endocrinol. Metab. 90:219-224(2005).
[18]
VARIANT LYS-72, CHARACTERIZATION OF VARIANT LYS-72, INVOLVEMENT IN
EARLY ONSET OBESITY AND HYPERPHAGIA, FUNCTION, AND SUBCELLULAR
LOCATION.
PubMed=25163632; DOI=10.1007/s11033-014-3691-7;
Delhanty P.J., Bouw E., Huisman M., Vervenne R.M., Themmen A.P.,
van der Lely A.J., van den Akker E.L.;
"Functional characterization of a new human melanocortin-4 receptor
homozygous mutation (N72K) that is associated with early-onset
obesity.";
Mol. Biol. Rep. 41:7967-7972(2014).
-!- FUNCTION: Receptor specific to the heptapeptide core common to
adrenocorticotropic hormone and alpha-, beta-, and gamma-MSH.
Plays a central role in energy homeostasis and somatic growth.
This receptor is mediated by G proteins that stimulate adenylate
cyclase (cAMP). {ECO:0000269|PubMed:12646665,
ECO:0000269|PubMed:25163632}.
-!- SUBUNIT: Interacts with ATRNL1 (By similarity). Homodimer;
disulfide-linked, also forms higher order oligomers. Interacts
with MGRN1, but does not undergo MGRN1-mediated ubiquitination;
this interaction competes with GNAS-binding and thus inhibits
agonist-induced cAMP production. Interacts with MRAP and MRAP2;
these associated factors increase ligand-sensitivity and
generation of cAMP. {ECO:0000250, ECO:0000269|PubMed:19329486,
ECO:0000269|PubMed:19737927, ECO:0000269|PubMed:23088915}.
-!- INTERACTION:
Q8TCY5:MRAP; NbExp=2; IntAct=EBI-3910694, EBI-9538727;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25163632};
Multi-pass membrane protein {ECO:0000255}.
-!- TISSUE SPECIFICITY: Brain, placental, and gut tissues.
-!- DISEASE: Obesity (OBESITY) [MIM:601665]: A condition characterized
by an increase of body weight beyond the limitation of skeletal
and physical requirements, as the result of excessive accumulation
of body fat. {ECO:0000269|PubMed:10199800,
ECO:0000269|PubMed:11443223, ECO:0000269|PubMed:11487744,
ECO:0000269|PubMed:12588803, ECO:0000269|PubMed:12646665,
ECO:0000269|PubMed:14671178, ECO:0000269|PubMed:14764818,
ECO:0000269|PubMed:15486053}. 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}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Melanocortin receptor entry;
URL="https://en.wikipedia.org/wiki/Melanocortin_receptor";
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EMBL; L08603; AAA35791.1; -; Genomic_DNA.
EMBL; S77415; AAB33341.1; -; Genomic_DNA.
EMBL; AY236539; AAO92061.1; -; Genomic_DNA.
EMBL; AK314130; BAG36820.1; -; mRNA.
EMBL; CH471096; EAW63105.1; -; Genomic_DNA.
EMBL; BC069172; AAH69172.1; -; mRNA.
EMBL; BC101802; AAI01803.1; -; mRNA.
EMBL; BC111992; AAI11993.1; -; mRNA.
CCDS; CCDS11976.1; -.
PIR; A57055; A57055.
RefSeq; NP_005903.2; NM_005912.2.
UniGene; Hs.532833; -.
PDB; 2IQP; Model; -; A=29-321.
PDB; 2IQR; Model; -; A=28-321.
PDB; 2IQS; Model; -; A=28-321.
PDB; 2IQU; Model; -; A=28-321.
PDB; 2IQV; Model; -; A=40-321.
PDB; 2IQW; Model; -; A=40-321.
PDBsum; 2IQP; -.
PDBsum; 2IQR; -.
PDBsum; 2IQS; -.
PDBsum; 2IQU; -.
PDBsum; 2IQV; -.
PDBsum; 2IQW; -.
ProteinModelPortal; P32245; -.
BioGrid; 110330; 6.
DIP; DIP-48791N; -.
IntAct; P32245; 3.
STRING; 9606.ENSP00000299766; -.
BindingDB; P32245; -.
ChEMBL; CHEMBL259; -.
GuidetoPHARMACOLOGY; 285; -.
TCDB; 9.A.14.2.3; the g-protein-coupled receptor (gpcr) family.
iPTMnet; P32245; -.
PhosphoSitePlus; P32245; -.
BioMuta; MC4R; -.
DMDM; 60392672; -.
PaxDb; P32245; -.
PRIDE; P32245; -.
Ensembl; ENST00000299766; ENSP00000299766; ENSG00000166603.
GeneID; 4160; -.
KEGG; hsa:4160; -.
UCSC; uc002lie.2; human.
CTD; 4160; -.
DisGeNET; 4160; -.
EuPathDB; HostDB:ENSG00000166603.4; -.
GeneCards; MC4R; -.
HGNC; HGNC:6932; MC4R.
HPA; HPA016719; -.
MalaCards; MC4R; -.
MIM; 155541; gene.
MIM; 601665; phenotype.
neXtProt; NX_P32245; -.
OpenTargets; ENSG00000166603; -.
Orphanet; 71529; Obesity due to melanocortin 4 receptor deficiency.
PharmGKB; PA30676; -.
eggNOG; KOG3656; Eukaryota.
eggNOG; ENOG410XRW9; LUCA.
GeneTree; ENSGT00770000120529; -.
HOGENOM; HOG000246927; -.
HOVERGEN; HBG108148; -.
InParanoid; P32245; -.
KO; K04202; -.
OMA; MHTSLHF; -.
OrthoDB; EOG091G0BVW; -.
PhylomeDB; P32245; -.
TreeFam; TF332646; -.
Reactome; R-HSA-375276; Peptide ligand-binding receptors.
Reactome; R-HSA-418555; G alpha (s) signalling events.
SIGNOR; P32245; -.
GeneWiki; Melanocortin_4_receptor; -.
GenomeRNAi; 4160; -.
PRO; PR:P32245; -.
Proteomes; UP000005640; Chromosome 18.
Bgee; ENSG00000166603; -.
CleanEx; HS_MC4R; -.
Genevisible; P32245; HS.
GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
GO; GO:0005634; C:nucleus; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0004977; F:melanocortin receptor activity; TAS:ProtInc.
GO; GO:0004980; F:melanocyte-stimulating hormone receptor activity; IDA:UniProtKB.
GO; GO:0042923; F:neuropeptide binding; IMP:UniProtKB.
GO; GO:0017046; F:peptide hormone binding; IEA:Ensembl.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
GO; GO:0007189; P:adenylate cyclase-activating G-protein coupled receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0007188; P:adenylate cyclase-modulating G-protein coupled receptor signaling pathway; TAS:ProtInc.
GO; GO:0002024; P:diet induced thermogenesis; IEA:Ensembl.
GO; GO:0006112; P:energy reserve metabolic process; IEA:Ensembl.
GO; GO:0007631; P:feeding behavior; TAS:ProtInc.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; TAS:Reactome.
GO; GO:0030073; P:insulin secretion; IEA:Ensembl.
GO; GO:2000252; P:negative regulation of feeding behavior; IEA:Ensembl.
GO; GO:0045780; P:positive regulation of bone resorption; IMP:HGNC.
GO; GO:2000821; P:regulation of grooming behavior; IEA:Ensembl.
GO; GO:0019222; P:regulation of metabolic process; IEA:Ensembl.
GO; GO:0032868; P:response to insulin; IEA:Ensembl.
CDD; cd15353; 7tmA_MC4R; 1.
InterPro; IPR000276; GPCR_Rhodpsn.
InterPro; IPR017452; GPCR_Rhodpsn_7TM.
InterPro; IPR000155; Mcort_rcpt_4.
InterPro; IPR001908; Melancort_rcpt.
InterPro; IPR001671; Melcrt_ACTH_rcpt.
Pfam; PF00001; 7tm_1; 1.
PRINTS; PR00237; GPCRRHODOPSN.
PRINTS; PR00534; MCRFAMILY.
PRINTS; PR00535; MELNOCORTINR.
PRINTS; PR01062; MELNOCORTN4R.
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;
3D-structure; Cell membrane; Complete proteome; Disease mutation;
Disulfide bond; G-protein coupled receptor; Glycoprotein; Lipoprotein;
Membrane; Obesity; Palmitate; Polymorphism; Receptor;
Reference proteome; Transducer; Transmembrane; Transmembrane helix.
CHAIN 1 332 Melanocortin receptor 4.
/FTId=PRO_0000069722.
TOPO_DOM 1 43 Extracellular. {ECO:0000255}.
TRANSMEM 44 69 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 70 81 Cytoplasmic. {ECO:0000255}.
TRANSMEM 82 106 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 107 123 Extracellular. {ECO:0000255}.
TRANSMEM 124 145 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 146 165 Cytoplasmic. {ECO:0000255}.
TRANSMEM 166 186 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 187 191 Extracellular. {ECO:0000255}.
TRANSMEM 192 215 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 216 248 Cytoplasmic. {ECO:0000255}.
TRANSMEM 249 271 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 272 280 Extracellular. {ECO:0000255}.
TRANSMEM 281 304 Helical; Name=7. {ECO:0000255}.
TOPO_DOM 305 332 Cytoplasmic. {ECO:0000255}.
LIPID 318 318 S-palmitoyl cysteine. {ECO:0000255}.
CARBOHYD 3 3 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 17 17 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 26 26 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 84 84 Interchain.
VARIANT 11 11 T -> A (in obesity; partial activity;
dbSNP:rs372794914).
{ECO:0000269|PubMed:12646665}.
/FTId=VAR_038632.
VARIANT 30 30 S -> F (in obesity; dbSNP:rs13447323).
{ECO:0000269|PubMed:10199800}.
/FTId=VAR_010704.
VARIANT 36 36 S -> Y (in obesity; shows the same
affinity as the wild-type but significant
impairment of cAMP-induced activity in
response to melanotan II compared with
the wild-type receptor).
{ECO:0000269|PubMed:15486053}.
/FTId=VAR_038633.
VARIANT 37 37 D -> V (in obesity; dbSNP:rs13447325).
{ECO:0000269|PubMed:10199800}.
/FTId=VAR_010705.
VARIANT 50 50 V -> M (in obesity; dbSNP:rs121913557).
{ECO:0000269|PubMed:11487744}.
/FTId=VAR_038634.
VARIANT 58 58 S -> C (in obesity; dbSNP:rs121913558).
{ECO:0000269|PubMed:11487744}.
/FTId=VAR_038635.
VARIANT 62 62 N -> S (in obesity; shows a partial cAMP
response to alpha-MSH;
dbSNP:rs121913566).
{ECO:0000269|PubMed:12588803,
ECO:0000269|PubMed:12646665}.
/FTId=VAR_038636.
VARIANT 72 72 N -> K (probable disease-associated
mutation found in a patient with early
onset obesity and hyperphagia; loss of
plasma membrane localization; loss of
receptor function).
{ECO:0000269|PubMed:25163632}.
/FTId=VAR_077570.
VARIANT 78 78 P -> L (in obesity; dbSNP:rs13447326).
{ECO:0000269|PubMed:10199800}.
/FTId=VAR_010706.
VARIANT 88 92 Missing (in obesity; the mutant receptor
is expressed well on the cell surface but
is completely devoid of ligand binding
and cAMP generation in response to
agonist stimulation).
{ECO:0000269|PubMed:14671178}.
/FTId=VAR_038637.
VARIANT 97 97 N -> D (in obesity; completely unable to
generate cAMP in response to ligand;
shows evidence of impaired cell surface
expression; dbSNP:rs121913565).
{ECO:0000269|PubMed:12588803,
ECO:0000269|PubMed:12646665}.
/FTId=VAR_038638.
VARIANT 102 102 I -> S (in obesity; shows the same
affinity as the wild-type but significant
impairment of cAMP-induced activity in
response to melanotan II compared with
the wild-type receptor;
dbSNP:rs121913559).
{ECO:0000269|PubMed:11487744}.
/FTId=VAR_038639.
VARIANT 102 102 I -> T (in obesity; dbSNP:rs121913559).
{ECO:0000269|PubMed:15486053}.
/FTId=VAR_038640.
VARIANT 103 103 V -> I (in dbSNP:rs2229616).
{ECO:0000269|PubMed:11487744,
ECO:0000269|PubMed:12646665,
ECO:0000269|PubMed:14764818,
ECO:0000269|PubMed:15486053,
ECO:0000269|PubMed:7854347,
ECO:0000269|PubMed:8392067}.
/FTId=VAR_010707.
VARIANT 106 106 L -> P (in obesity; completely unable to
generate cAMP in response to ligand;
shows evidence of impaired cell surface
expression).
{ECO:0000269|PubMed:12588803}.
/FTId=VAR_038641.
VARIANT 112 112 T -> M (polymorphism; no effect on MC4R
signaling; dbSNP:rs13447329).
{ECO:0000269|PubMed:10199800,
ECO:0000269|PubMed:12646665,
ECO:0000269|PubMed:14764818,
ECO:0000269|PubMed:15486053}.
/FTId=VAR_010708.
VARIANT 125 125 I -> K (in obesity; completely unable to
generate cAMP in response to ligand;
shows evidence of impaired cell surface
expression).
{ECO:0000269|PubMed:12588803,
ECO:0000269|PubMed:12646665}.
/FTId=VAR_038642.
VARIANT 127 127 S -> L (in obesity; signaling properties
in response to alpha-MSH, beta-MSH and
gamma-1-MSH are impaired;
dbSNP:rs13447331).
{ECO:0000269|PubMed:14764818}.
/FTId=VAR_038643.
VARIANT 165 165 R -> Q (in obesity; shows a partial cAMP
response to alpha-MSH; dbSNP:rs13447332).
{ECO:0000269|PubMed:12588803,
ECO:0000269|PubMed:12646665,
ECO:0000269|PubMed:15486053}.
/FTId=VAR_038644.
VARIANT 165 165 R -> W (in obesity; dbSNP:rs13447332).
{ECO:0000269|PubMed:10199800}.
/FTId=VAR_010709.
VARIANT 170 170 I -> V (in obesity; dbSNP:rs121913560).
{ECO:0000269|PubMed:11487744}.
/FTId=VAR_038645.
VARIANT 175 175 A -> T (in obesity; shows a partial cAMP
response to alpha-MSH;
dbSNP:rs121913563).
{ECO:0000269|PubMed:12588803,
ECO:0000269|PubMed:12646665,
ECO:0000269|PubMed:15486053}.
/FTId=VAR_038646.
VARIANT 181 181 G -> D (in obesity; does not bind alpha-
MSH; dbSNP:rs13447333).
{ECO:0000269|PubMed:15486053}.
/FTId=VAR_038647.
VARIANT 219 219 A -> V (in obesity; shows significantly
impairment of cAMP-induced activity in
response to melanotan II compared with
the wild-type receptor;
dbSNP:rs121913567).
{ECO:0000269|PubMed:15486053}.
/FTId=VAR_038648.
VARIANT 226 226 I -> T (in dbSNP:rs193922686).
{ECO:0000269|PubMed:14764818}.
/FTId=VAR_038649.
VARIANT 251 251 I -> L (in dbSNP:rs52820871).
{ECO:0000269|PubMed:10199800,
ECO:0000269|PubMed:11487744,
ECO:0000269|PubMed:12646665,
ECO:0000269|PubMed:14764818,
ECO:0000269|PubMed:15486053}.
/FTId=VAR_010710.
VARIANT 252 252 G -> S (in obesity; dbSNP:rs13447336).
{ECO:0000269|PubMed:10199800}.
/FTId=VAR_010711.
VARIANT 253 253 V -> I (in obesity; shows a partial cAMP
response to alpha-MSH;
dbSNP:rs187152753).
{ECO:0000269|PubMed:12588803}.
/FTId=VAR_038650.
VARIANT 271 271 C -> R (in obesity; completely unable to
generate cAMP in response to ligand;
shows impaired cell surface expression;
dbSNP:rs1057517991).
{ECO:0000269|PubMed:12646665}.
/FTId=VAR_038651.
VARIANT 271 271 C -> Y (in obesity; no activity;
dbSNP:rs121913562).
{ECO:0000269|PubMed:12588803,
ECO:0000269|PubMed:12646665}.
/FTId=VAR_038652.
VARIANT 274 274 N -> S (in obesity; dbSNP:rs121913561).
{ECO:0000269|PubMed:11443223}.
/FTId=VAR_015357.
VARIANT 316 316 I -> S (in obesity; shows reduced cAMP
response to alpha-MSH; retains normal
affinity for the antagonist AGRP;
dbSNP:rs121913564).
{ECO:0000269|PubMed:12588803,
ECO:0000269|PubMed:12646665}.
/FTId=VAR_038653.
VARIANT 317 317 I -> T (in obesity; dbSNP:rs13447337).
{ECO:0000269|PubMed:10199800}.
/FTId=VAR_010712.
VARIANT 325 325 L -> F (in obesity; does not bind alpha-
MSH). {ECO:0000269|PubMed:15486053}.
/FTId=VAR_038654.
CONFLICT 169 169 I -> S (in Ref. 2; AAB33341).
{ECO:0000305}.
SEQUENCE 332 AA; 36943 MW; E80010BAADBED2B4 CRC64;
MVNSTHRGMH TSLHLWNRSS YRLHSNASES LGKGYSDGGC YEQLFVSPEV FVTLGVISLL
ENILVIVAIA KNKNLHSPMY FFICSLAVAD MLVSVSNGSE TIVITLLNST DTDAQSFTVN
IDNVIDSVIC SSLLASICSL LSIAVDRYFT IFYALQYHNI MTVKRVGIII SCIWAACTVS
GILFIIYSDS SAVIICLITM FFTMLALMAS LYVHMFLMAR LHIKRIAVLP GTGAIRQGAN
MKGAITLTIL IGVFVVCWAP FFLHLIFYIS CPQNPYCVCF MSHFNLYLIL IMCNSIIDPL
IYALRSQELR KTFKEIICCY PLGGLCDLSS RY


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