P32245 (MC4R_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Melanocortin receptor 4
Short name=MC4-R

Gene names

Name:

MC4R

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	332 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Receptor specific to the heptapeptide core common to adrenocorticotropic hormone and alpha-, beta-, and gamma-MSH. This receptor is mediated by G proteins that stimulate adenylate cyclase.
Subunit structure	Interacts with ATRNL1 By similarity. Interacts with MGRN1, but does not undergo MGRN1-mediated ubiquitination; this interaction competes with GNAS-binding and thus inhibits agonist-induced cAMP production. Ref.7
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.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15
Sequence similarities	Belongs to the G-protein coupled receptor 1 family.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Coding sequence diversity	Polymorphism
Disease	Disease mutation Obesity
Domain	Transmembrane Transmembrane helix
Molecular function	G-protein coupled receptor Receptor Transducer
PTM	Glycoprotein Lipoprotein Palmitate
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	adenylate cyclase-modulating G-protein coupled receptor signaling pathway Traceable author statement PubMed 8794897. Source: ProtInc diet induced thermogenesis Inferred from electronic annotation. Source: Compara energy reserve metabolic process Inferred from electronic annotation. Source: Compara feeding behavior Traceable author statement PubMed 9771698. Source: ProtInc insulin secretion Inferred from electronic annotation. Source: Compara negative regulation of feeding behavior Inferred from electronic annotation. Source: Compara positive regulation of bone resorption Inferred from mutant phenotype PubMed 16614075. Source: HGNC positive regulation of cAMP biosynthetic process Inferred from direct assay PubMed 19329486PubMed 19743876. Source: BHF-UCL response to insulin stimulus Inferred from electronic annotation. Source: Compara
Cellular_component	integral to membrane Traceable author statement Ref.1. Source: ProtInc nucleus Inferred from electronic annotation. Source: Compara plasma membrane Traceable author statement. Source: Reactome
Molecular_function	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: Compara
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 332

332

Melanocortin receptor 4

PRO_0000069722

Regions

Topological domain

1 – 43

43

Extracellular Potential

Transmembrane

44 – 69

26

Helical; Name=1; Potential

Topological domain

70 – 81

12

Cytoplasmic Potential

Transmembrane

82 – 106

25

Helical; Name=2; Potential

Topological domain

107 – 123

17

Extracellular Potential

Transmembrane

124 – 145

22

Helical; Name=3; Potential

Topological domain

146 – 165

20

Cytoplasmic Potential

Transmembrane

166 – 186

21

Helical; Name=4; Potential

Topological domain

187 – 191

5

Extracellular Potential

Transmembrane

192 – 215

24

Helical; Name=5; Potential

Topological domain

216 – 248

33

Cytoplasmic Potential

Transmembrane

249 – 271

23

Helical; Name=6; Potential

Topological domain

272 – 280

9

Extracellular Potential

Transmembrane

281 – 304

24

Helical; Name=7; Potential

Topological domain

305 – 332

28

Cytoplasmic Potential

Amino acid modifications

Lipidation

318

1

S-palmitoyl cysteine Potential

Glycosylation

3

1

N-linked (GlcNAc...) Potential

Glycosylation

17

1

N-linked (GlcNAc...) Potential

Glycosylation

26

1

N-linked (GlcNAc...) Potential

Natural variations

Natural variant

11

1

T → A in obesity; partial activity. Ref.13

VAR_038632

Natural variant

30

1

S → R in obesity. Ref.8

VAR_010704

Natural variant

36

1

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. Ref.15

VAR_038633

Natural variant

37

1

D → V in obesity. Ref.8
Corresponds to variant rs13447325 [ dbSNP | Ensembl ].

VAR_010705

Natural variant

50

1

V → M in obesity. Ref.10

VAR_038634

Natural variant

58

1

S → C in obesity. Ref.10

VAR_038635

Natural variant

62

1

N → S in obesity; shows a partial cAMP response to alpha-MSH. Ref.11 Ref.13

VAR_038636

Natural variant

78

1

P → L in obesity. Ref.8
Corresponds to variant rs13447326 [ dbSNP | Ensembl ].

VAR_010706

Natural variant

88 – 92

5

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.

VAR_038637

Natural variant

97

1

N → D in obesity; completely unable to generate cAMP in response to ligand; shows evidence of impaired cell surface expression. Ref.11 Ref.13

VAR_038638

Natural variant

102

1

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. Ref.10

VAR_038639

Natural variant

102

1

I → T in obesity. Ref.15

VAR_038640

Natural variant

103

1

V → I. Ref.1 Ref.2 Ref.10 Ref.13 Ref.14 Ref.15
Corresponds to variant rs2229616 [ dbSNP | Ensembl ].

VAR_010707

Natural variant

106

1

L → P in obesity; completely unable to generate cAMP in response to ligand; shows evidence of impaired cell surface expression. Ref.11

VAR_038641

Natural variant

112

1

T → M Polymorphism with no effect on MC4R signaling. Ref.8 Ref.13 Ref.14 Ref.15
Corresponds to variant rs13447329 [ dbSNP | Ensembl ].

VAR_010708

Natural variant

125

1

I → K in obesity; completely unable to generate cAMP in response to ligand; shows evidence of impaired cell surface expression. Ref.11 Ref.13

VAR_038642

Natural variant

127

1

S → L in obesity; signaling properties in response to alpha-MSH, beta-MSH and gamma-1-MSH are impaired. Ref.14
Corresponds to variant rs13447331 [ dbSNP | Ensembl ].

VAR_038643

Natural variant

165

1

R → Q in obesity; shows a partial cAMP response to alpha-MSH. Ref.11 Ref.13 Ref.15
Corresponds to variant rs13447332 [ dbSNP | Ensembl ].

VAR_038644

Natural variant

165

1

R → W in obesity. Ref.8
Corresponds to variant rs13447332 [ dbSNP | Ensembl ].

VAR_010709

Natural variant

170

1

I → V in obesity. Ref.10

VAR_038645

Natural variant

175

1

A → T in obesity; shows a partial cAMP response to alpha-MSH. Ref.11 Ref.13 Ref.15

VAR_038646

Natural variant

181

1

G → D in obesity; does not bind alpha-MSH. Ref.15
Corresponds to variant rs13447333 [ dbSNP | Ensembl ].

VAR_038647

Natural variant

219

1

A → V in obesity; shows significantly impairment of cAMP-induced activity in response to melanotan II compared with the wild-type receptor. Ref.15

VAR_038648

Natural variant

226

1

I → T. Ref.14

VAR_038649

Natural variant

251

1

I → L. Ref.8 Ref.10 Ref.13 Ref.14 Ref.15
Corresponds to variant rs52820871 [ dbSNP | Ensembl ].

VAR_010710

Natural variant

252

1

G → S in obesity. Ref.8
Corresponds to variant rs13447336 [ dbSNP | Ensembl ].

VAR_010711

Natural variant

253

1

V → I in obesity; shows a partial cAMP response to alpha-MSH. Ref.11

VAR_038650

Natural variant

271

1

C → R in obesity; completely unable to generate cAMP in response to ligand; shows impaired cell surface expression. Ref.13

VAR_038651

Natural variant

271

1

C → Y in obesity; no activity. Ref.11 Ref.13

VAR_038652

Natural variant

274

1

N → S in obesity. Ref.9

VAR_015357

Natural variant

316

1

I → S in obesity; shows reduced cAMP response to alpha-MSH; retains normal affinity for the antagonist AGRP. Ref.11 Ref.13

VAR_038653

Natural variant

317

1

I → T in obesity. Ref.8
Corresponds to variant rs13447337 [ dbSNP | Ensembl ].

VAR_010712

Natural variant

325

1

L → F in obesity; does not bind alpha-MSH. Ref.15

VAR_038654

Experimental info

Sequence conflict

169

1

I → S in AAB33341. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

332

Helix Strand Turn

Details...

Helix

48 – 71

24

Helix

78 – 104

27

Beta strand

107 – 112

6

Turn

113 – 115

3

Beta strand

116 – 119

4

Helix

122 – 151

30

Helix

163 – 185

23

Helix

191 – 198

8

Turn

199 – 201

3

Helix

202 – 226

25

Helix

233 – 257

25

Helix

259 – 270

12

Beta strand

271 – 275

5

Helix

283 – 291

9

Helix

294 – 305

12

Helix

307 – 317

11

Sequences

	Sequence		Length	Mass (Da)
	P32245 [UniParc]. Last modified October 25, 2004. Version 2. Checksum: E80010BAADBED2B4	FASTA	332	36,943
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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]	"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.
[8]	"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.
[9]	"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.
[10]	"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.
[11]	"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.
[12]	"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.
[13]	"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.
[14]	"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.
[15]	"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.

IPI

IPI00027684.

PIR

A57055.

RefSeq

NP_005903.2. NM_005912.2.

UniGene

Hs.532833.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2IQP	model	-	A	29-321	[»]
2IQR	model	-	A	28-321	[»]
2IQS	model	-	A	28-321	[»]
2IQU	model	-	A	28-321	[»]
2IQV	model	-	A	40-321	[»]
2IQW	model	-	A	40-321	[»]

ProteinModelPortal

P32245.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-48791N.

IntAct

P32245. 1 interaction.

STRING

9606.ENSP00000299766.

Protein family/group databases

GPCRDB

Search...

PTM databases

PhosphoSite

P32245.

Polymorphism databases

DMDM

60392672.

Proteomic databases

PaxDb

P32245.

PRIDE

P32245.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000299766; ENSP00000299766; ENSG00000166603.

GeneID

4160.

KEGG

hsa:4160.

UCSC

uc002lie.1. human.

Organism-specific databases

CTD

4160.

GeneCards

GC18M058011.

HGNC

HGNC:6932. MC4R.

HPA

HPA016719.

MIM

155541. gene.
601665. phenotype.

neXtProt

NX_P32245.

Orphanet

71529. Obesity due to melanocortin-4 receptor deficiency.

PharmGKB

PA30676.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG269550.

HOGENOM

HOG000246927.

HOVERGEN

HBG108148.

InParanoid

P32245.

KO

K04202.

OMA

TSLHFWN.

OrthoDB

EOG45DWPS.

PhylomeDB

P32245.

Enzyme and pathway databases

Pathway_Interaction_DB

syndecan_3_pathway. Syndecan-3-mediated signaling events.

Reactome

REACT_111102. Signal Transduction.

Gene expression databases

ArrayExpress

P32245.

Bgee

P32245.

CleanEx

HS_MC4R.

Genevestigator

P32245.

GermOnline

ENSG00000166603. Homo sapiens.

Family and domain databases

InterPro

IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR000155. Mcort_rcpt_4.
IPR001908. Melancort_rcpt.
IPR001671. Melcrt_ACTH_rcpt.
[Graphical view]

Pfam

PF00001. 7tm_1. 1 hit.
[Graphical view]

PRINTS

PR00237. GPCRRHODOPSN.
PR00534. MCRFAMILY.
PR00535. MELNOCORTINR.
PR01062. MELNOCORTN4R.

PROSITE

PS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P32245.

ChEMBL

CHEMBL259.

GenomeRNAi

4160.

NextBio

16390.

SOURCE

Search...

Entry information

Entry name

MC4R_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 139 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.