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P32245 (MC4R_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 149. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Melanocortin receptor 4

Short name=MC4-R
Gene names
Name:MC4R
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length332 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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). Ref.15

Subunit structure

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. Ref.7 Ref.8 Ref.9

Subcellular location

Cell membrane; Multi-pass membrane protein.

Tissue specificity

Brain, placental, and gut tissues.

Involvement in 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17

Sequence similarities

Belongs to the G-protein coupled receptor 1 family.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
Obesity
   DomainTransmembrane
Transmembrane helix
   Molecular functionG-protein coupled receptor
Receptor
Transducer
   PTMDisulfide bond
Glycoprotein
Lipoprotein
Palmitate
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processadenylate cyclase-modulating G-protein coupled receptor signaling pathway

Traceable author statement PubMed 8794897. Source: ProtInc

diet induced thermogenesis

Inferred from electronic annotation. Source: Ensembl

energy reserve metabolic process

Inferred from electronic annotation. Source: Ensembl

feeding behavior

Traceable author statement PubMed 9771698. Source: ProtInc

insulin secretion

Inferred from electronic annotation. Source: Ensembl

negative regulation of feeding behavior

Inferred from electronic annotation. Source: Ensembl

positive regulation of bone resorption

Inferred from mutant phenotype PubMed 16614075. Source: HGNC

positive regulation of cAMP biosynthetic process

Inferred from direct assay Ref.7PubMed 19743876. Source: BHF-UCL

regulation of grooming behavior

Inferred from electronic annotation. Source: Ensembl

response to insulin

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentintegral component of membrane

Traceable author statement Ref.1. Source: ProtInc

nucleus

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionmelanocortin receptor activity

Traceable author statement PubMed 8794897. Source: ProtInc

melanocyte-stimulating hormone receptor activity

Inferred from physical interaction PubMed 19743876. Source: BHF-UCL

neuropeptide binding

Inferred from physical interaction PubMed 15927146. Source: UniProtKB

peptide hormone binding

Inferred from electronic annotation. Source: Ensembl

ubiquitin protein ligase binding

Inferred from physical interaction Ref.8. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 332332Melanocortin receptor 4
PRO_0000069722

Regions

Topological domain1 – 4343Extracellular Potential
Transmembrane44 – 6926Helical; Name=1; Potential
Topological domain70 – 8112Cytoplasmic Potential
Transmembrane82 – 10625Helical; Name=2; Potential
Topological domain107 – 12317Extracellular Potential
Transmembrane124 – 14522Helical; Name=3; Potential
Topological domain146 – 16520Cytoplasmic Potential
Transmembrane166 – 18621Helical; Name=4; Potential
Topological domain187 – 1915Extracellular Potential
Transmembrane192 – 21524Helical; Name=5; Potential
Topological domain216 – 24833Cytoplasmic Potential
Transmembrane249 – 27123Helical; Name=6; Potential
Topological domain272 – 2809Extracellular Potential
Transmembrane281 – 30424Helical; Name=7; Potential
Topological domain305 – 33228Cytoplasmic Potential

Amino acid modifications

Lipidation3181S-palmitoyl cysteine Potential
Glycosylation31N-linked (GlcNAc...) Potential
Glycosylation171N-linked (GlcNAc...) Potential
Glycosylation261N-linked (GlcNAc...) Potential
Disulfide bond84Interchain Ref.9

Natural variations

Natural variant111T → A in obesity; partial activity. Ref.15
VAR_038632
Natural variant301S → R in obesity. Ref.10
VAR_010704
Natural variant361S → 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. Ref.17
VAR_038633
Natural variant371D → V in obesity. Ref.10
Corresponds to variant rs13447325 [ dbSNP | Ensembl ].
VAR_010705
Natural variant501V → M in obesity. Ref.12
VAR_038634
Natural variant581S → C in obesity. Ref.12
VAR_038635
Natural variant621N → S in obesity; shows a partial cAMP response to alpha-MSH. Ref.13 Ref.15
VAR_038636
Natural variant781P → L in obesity. Ref.10
Corresponds to variant rs13447326 [ dbSNP | Ensembl ].
VAR_010706
Natural variant88 – 925Missing 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.
VAR_038637
Natural variant971N → D in obesity; completely unable to generate cAMP in response to ligand; shows evidence of impaired cell surface expression. Ref.13 Ref.15
VAR_038638
Natural variant1021I → 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. Ref.12
VAR_038639
Natural variant1021I → T in obesity. Ref.17
VAR_038640
Natural variant1031V → I. Ref.1 Ref.2 Ref.12 Ref.15 Ref.16 Ref.17
Corresponds to variant rs2229616 [ dbSNP | Ensembl ].
VAR_010707
Natural variant1061L → P in obesity; completely unable to generate cAMP in response to ligand; shows evidence of impaired cell surface expression. Ref.13
VAR_038641
Natural variant1121T → M Polymorphism with no effect on MC4R signaling. Ref.10 Ref.15 Ref.16 Ref.17
Corresponds to variant rs13447329 [ dbSNP | Ensembl ].
VAR_010708
Natural variant1251I → K in obesity; completely unable to generate cAMP in response to ligand; shows evidence of impaired cell surface expression. Ref.13 Ref.15
VAR_038642
Natural variant1271S → L in obesity; signaling properties in response to alpha-MSH, beta-MSH and gamma-1-MSH are impaired. Ref.16
Corresponds to variant rs13447331 [ dbSNP | Ensembl ].
VAR_038643
Natural variant1651R → Q in obesity; shows a partial cAMP response to alpha-MSH. Ref.13 Ref.15 Ref.17
Corresponds to variant rs13447332 [ dbSNP | Ensembl ].
VAR_038644
Natural variant1651R → W in obesity. Ref.10
Corresponds to variant rs13447332 [ dbSNP | Ensembl ].
VAR_010709
Natural variant1701I → V in obesity. Ref.12
Corresponds to variant rs121913560 [ dbSNP | Ensembl ].
VAR_038645
Natural variant1751A → T in obesity; shows a partial cAMP response to alpha-MSH. Ref.13 Ref.15 Ref.17
VAR_038646
Natural variant1811G → D in obesity; does not bind alpha-MSH. Ref.17
Corresponds to variant rs13447333 [ dbSNP | Ensembl ].
VAR_038647
Natural variant2191A → V in obesity; shows significantly impairment of cAMP-induced activity in response to melanotan II compared with the wild-type receptor. Ref.17
VAR_038648
Natural variant2261I → T. Ref.16
VAR_038649
Natural variant2511I → L. Ref.10 Ref.12 Ref.15 Ref.16 Ref.17
Corresponds to variant rs52820871 [ dbSNP | Ensembl ].
VAR_010710
Natural variant2521G → S in obesity. Ref.10
Corresponds to variant rs13447336 [ dbSNP | Ensembl ].
VAR_010711
Natural variant2531V → I in obesity; shows a partial cAMP response to alpha-MSH. Ref.13
Corresponds to variant rs187152753 [ dbSNP | Ensembl ].
VAR_038650
Natural variant2711C → R in obesity; completely unable to generate cAMP in response to ligand; shows impaired cell surface expression. Ref.15
VAR_038651
Natural variant2711C → Y in obesity; no activity. Ref.13 Ref.15
VAR_038652
Natural variant2741N → S in obesity. Ref.11
VAR_015357
Natural variant3161I → S in obesity; shows reduced cAMP response to alpha-MSH; retains normal affinity for the antagonist AGRP. Ref.13 Ref.15
VAR_038653
Natural variant3171I → T in obesity. Ref.10
Corresponds to variant rs13447337 [ dbSNP | Ensembl ].
VAR_010712
Natural variant3251L → F in obesity; does not bind alpha-MSH. Ref.17
VAR_038654

Experimental info

Sequence conflict1691I → S in AAB33341. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P32245 [UniParc].

Last modified October 25, 2004. Version 2.
Checksum: E80010BAADBED2B4

FASTA33236,943
        10         20         30         40         50         60 
MVNSTHRGMH TSLHLWNRSS YRLHSNASES LGKGYSDGGC YEQLFVSPEV FVTLGVISLL 

        70         80         90        100        110        120 
ENILVIVAIA KNKNLHSPMY FFICSLAVAD MLVSVSNGSE TIVITLLNST DTDAQSFTVN 

       130        140        150        160        170        180 
IDNVIDSVIC SSLLASICSL LSIAVDRYFT IFYALQYHNI MTVKRVGIII SCIWAACTVS 

       190        200        210        220        230        240 
GILFIIYSDS SAVIICLITM FFTMLALMAS LYVHMFLMAR LHIKRIAVLP GTGAIRQGAN 

       250        260        270        280        290        300 
MKGAITLTIL IGVFVVCWAP FFLHLIFYIS CPQNPYCVCF MSHFNLYLIL IMCNSIIDPL 

       310        320        330 
IYALRSQELR KTFKEIICCY PLGGLCDLSS RY 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning, expression, and gene localization of a fourth melanocortin receptor."
Gantz I., Miwa H., Konda Y., Shimoto Y., Tashiro T., Waston S.J., Delvalle J.
J. Biol. Chem. 268:15174-15179(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ILE-103.
[2]"Localization of the melanocortin-4 receptor (MC4-R) in neuroendocrine and autonomic control circuits in the brain."
Mountjoy K.G., Mortrud M.T., Low M.J., Simerly R.B., Cone R.D.
Mol. Endocrinol. 8:1298-1308(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ILE-103.
[3]"cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
Kopatz S.A., Aronstam R.S., Sharma S.V.
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Subthalamic nucleus.
[5]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[7]"MRAP and MRAP2 are bidirectional regulators of the melanocortin receptor family."
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.
Proc. Natl. Acad. Sci. U.S.A. 106:6146-6151(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MRAP AND MRAP2.
[8]"Mahogunin ring finger-1 (MGRN1) E3 ubiquitin ligase inhibits signaling from melanocortin receptor by competition with Galphas."
Perez-Oliva A.B., Olivares C., Jimenez-Cervantes C., Garcia-Borron J.C.
J. Biol. Chem. 284:31714-31725(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MGRN1.
[9]"The melanocortin 4 receptor: oligomer formation, interaction sites and functional significance."
Chapman K.L., Findlay J.B.
Biochim. Biophys. Acta 1828:535-542(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERCHAIN DISULFIDE BOND, SUBUNIT.
[10]"Several mutations in the melanocortin-4 receptor gene including a nonsense and a frameshift mutation associated with dominantly inherited obesity in humans."
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.
J. Clin. Endocrinol. Metab. 84:1483-1486(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS OBESITY ARG-30; VAL-37; LEU-78; TRP-165; SER-252 AND THR-317, VARIANTS MET-112 AND LEU-251.
[11]"A novel melanocortin 4 receptor (MC4R) gene mutation associated with morbid obesity."
Mergen M., Mergen H., Ozata M., Oner R., Oner C.
J. Clin. Endocrinol. Metab. 86:3448-3448(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OBESITY SER-274.
[12]"Mutational analysis of melanocortin-4 receptor, agouti-related protein, and alpha-melanocyte-stimulating hormone genes in severely obese children."
Dubern B., Clement K., Pelloux V., Froguel P., Girardet J.-P., Guy-Grand B., Tounian P.
J. Pediatr. 139:204-209(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS OBESITY MET-50; CYS-58; SER-102 AND VAL-170, VARIANTS ILE-103 AND LEU-251.
[13]"Mutations in the human melanocortin-4 receptor gene associated with severe familial obesity disrupts receptor function through multiple molecular mechanisms."
Yeo G.S.H., Lank E.J., Farooqi I.S., Keogh J., Challis B.G., O'Rahilly S.
Hum. Mol. Genet. 12:561-574(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS OBESITY SER-62; ASP-97; PRO-106; LYS-125; GLN-165; THR-175; ILE-253; TYR-271 AND SER-316, CHARACTERIZATION OF VARIANTS OBESITY SER-62; ASP-97; PRO-106; LYS-125; GLN-165; THR-175; ILE-253; TYR-271 AND SER-316.
[14]"Deletion of codons 88-92 of the melanocortin-4 receptor gene: a novel deleterious mutation in an obese female."
Donohoue P.A., Tao Y.-X., Collins M., Yeo G.S.H., O'Rahilly S., Segaloff D.L.
J. Clin. Endocrinol. Metab. 88:5841-5845(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OBESITY 88-VAL--LEU-92 DEL, CHARACTERIZATION OF VARIANT OBESITY 88-VAL--LEU-92 DEL.
[15]"Clinical spectrum of obesity and mutations in the melanocortin 4 receptor gene."
Farooqi I.S., Keogh J.M., Yeo G.S.H., Lank E.J., Cheetham T., O'Rahilly S.
N. Engl. J. Med. 348:1085-1095(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: 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, FUNCTION.
[16]"Identification and characterization of melanocortin-4 receptor gene mutations in morbidly obese Finnish children and adults."
Valli-Jaakola K., Lipsanen-Nyman M., Oksanen L., Hollenberg A.N., Kontula K., Bjoerbaek C., Schalin-Jaentti C.
J. Clin. Endocrinol. Metab. 89:940-945(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OBESITY LEU-127, VARIANTS ILE-103; MET-112; THR-226 AND LEU-251, CHARACTERIZATION OF VARIANT OBESITY LEU-127, CHARACTERIZATION OF VARIANTS MET-112 AND THR-226.
[17]"Prevalence of mutations and functional analyses of melanocortin 4 receptor variants identified among 750 men with juvenile-onset obesity."
Larsen L.H., Echwald S.M., Soerensen T.I.A., Andersen T., Wulff B.S., Pedersen O.
J. Clin. Endocrinol. Metab. 90:219-224(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: 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, CHARACTERIZATION OF VARIANTS OBESITY TYR-36; THR-102; GLN-165; ASP-181; VAL-219 AND PHE-325.
+Additional computationally mapped references.

Web resources

GeneReviews
Wikipedia

Melanocortin receptor entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L08603 Genomic DNA. Translation: AAA35791.1.
S77415 Genomic DNA. Translation: AAB33341.1.
AY236539 Genomic DNA. Translation: AAO92061.1.
AK314130 mRNA. Translation: BAG36820.1.
CH471096 Genomic DNA. Translation: EAW63105.1.
BC069172 mRNA. Translation: AAH69172.1.
BC101802 mRNA. Translation: AAI01803.1.
BC111992 mRNA. Translation: AAI11993.1.
PIRA57055.
RefSeqNP_005903.2. NM_005912.2.
UniGeneHs.532833.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2IQPmodel-A29-321[»]
2IQRmodel-A28-321[»]
2IQSmodel-A28-321[»]
2IQUmodel-A28-321[»]
2IQVmodel-A40-321[»]
2IQWmodel-A40-321[»]
ProteinModelPortalP32245.
SMRP32245. Positions 50-320.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110330. 6 interactions.
DIPDIP-48791N.
IntActP32245. 1 interaction.
STRING9606.ENSP00000299766.

Chemistry

BindingDBP32245.
ChEMBLCHEMBL2111323.
GuidetoPHARMACOLOGY285.

Protein family/group databases

TCDB9.A.14.2.3. the g-protein-coupled receptor (gpcr) family.
GPCRDBSearch...

PTM databases

PhosphoSiteP32245.

Polymorphism databases

DMDM60392672.

Proteomic databases

PaxDbP32245.
PRIDEP32245.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000299766; ENSP00000299766; ENSG00000166603.
GeneID4160.
KEGGhsa:4160.
UCSCuc002lie.1. human.

Organism-specific databases

CTD4160.
GeneCardsGC18M058011.
HGNCHGNC:6932. MC4R.
HPAHPA016719.
MIM155541. gene.
601665. phenotype.
neXtProtNX_P32245.
Orphanet71529. Obesity due to melanocortin 4 receptor deficiency.
PharmGKBPA30676.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG269550.
HOGENOMHOG000246927.
HOVERGENHBG108148.
InParanoidP32245.
KOK04202.
OMATSLHFWN.
OrthoDBEOG7QK0CF.
PhylomeDBP32245.
TreeFamTF332646.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.

Gene expression databases

ArrayExpressP32245.
BgeeP32245.
CleanExHS_MC4R.
GenevestigatorP32245.

Family and domain databases

Gene3D1.20.1070.10. 1 hit.
InterProIPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR000155. Mcort_rcpt_4.
IPR001908. Melancort_rcpt.
IPR001671. Melcrt_ACTH_rcpt.
[Graphical view]
PfamPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSPR00237. GPCRRHODOPSN.
PR00534. MCRFAMILY.
PR00535. MELNOCORTINR.
PR01062. MELNOCORTN4R.
PROSITEPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiMelanocortin_4_receptor.
GenomeRNAi4160.
NextBio16390.
PROP32245.
SOURCESearch...

Entry information

Entry nameMC4R_HUMAN
AccessionPrimary (citable) accession number: P32245
Secondary accession number(s): B2RAC3, Q16317, Q3MIJ6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 25, 2004
Last modified: April 16, 2014
This is version 149 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 18

Human chromosome 18: entries, gene names and cross-references to MIM

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries