P32244 (MC3R_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Melanocortin receptor 3
Short name=MC3-R

Gene names

Name:

Mc3r

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	323 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Receptor for MSH (alpha, beta and gamma) and ACTH.
Subcellular location	Cell membrane; Multi-pass membrane protein.
Tissue specificity	Brain.
Sequence similarities	Belongs to the G-protein coupled receptor 1 family.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Molecular function	G-protein coupled receptor Receptor Transducer
PTM	Glycoprotein Lipoprotein Palmitate
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	adenylate cyclase-modulating G-protein coupled receptor signaling pathway Inferred from direct assay Ref.2. Source: RGD homoiothermy Inferred from mutant phenotype PubMed 21091037. Source: RGD positive regulation of cAMP biosynthetic process Inferred from electronic annotation. Source: Compara regulation of blood pressure Inferred from mutant phenotype PubMed 21091037. Source: RGD regulation of heart rate Inferred from mutant phenotype PubMed 21091037. Source: RGD sodium ion homeostasis Inferred from expression pattern PubMed 19570553. Source: RGD
Cellular_component	integral to plasma membrane Traceable author statement PubMed 12045190. Source: RGD
Molecular_function	melanocortin receptor activity Inferred from direct assay PubMed 17023527. Source: RGD melanocyte-stimulating hormone receptor activity Inferred from electronic annotation. Source: Compara neuropeptide binding Inferred from electronic annotation. Source: Compara peptide hormone binding Inferred from direct assay PubMed 17023527. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 323	323	Melanocortin receptor 3		PRO_0000069720
Regions
	Topological domain	1 – 37	37	Extracellular Potential
	Transmembrane	38 – 63	26	Helical; Name=1; Potential
	Topological domain	64 – 75	12	Cytoplasmic Potential
	Transmembrane	76 – 100	25	Helical; Name=2; Potential
	Topological domain	101 – 118	18	Extracellular Potential
	Transmembrane	119 – 140	22	Helical; Name=3; Potential
	Topological domain	141 – 160	20	Cytoplasmic Potential
	Transmembrane	161 – 181	21	Helical; Name=4; Potential
	Topological domain	182 – 186	5	Extracellular Potential
	Transmembrane	187 – 210	24	Helical; Name=5; Potential
	Topological domain	211 – 245	35	Cytoplasmic Potential
	Transmembrane	246 – 268	23	Helical; Name=6; Potential
	Topological domain	269 – 277	9	Extracellular Potential
	Transmembrane	278 – 301	24	Helical; Name=7; Potential
	Topological domain	302 – 323	22	Cytoplasmic Potential
Amino acid modifications
	Lipidation	315	1	S-palmitoyl cysteine Potential
	Glycosylation	2	1	N-linked (GlcNAc...) Potential
	Glycosylation	16	1	N-linked (GlcNAc...) Potential
	Glycosylation	28	1	N-linked (GlcNAc...) Potential
Experimental info
	Sequence conflict	78	1	C → L in CAA50005. Ref.1
	Sequence conflict	81 – 82	2	AA → LQ in CAA50005. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P32244 [UniParc]. Last modified July 11, 2012. Version 2. Checksum: F4E57B88E7A0A736	FASTA	323	35,757
	10 20 30 40 50 60 MNSSCCPSSS YPTLPNLSQH PAAPSASNRS GSGFCEQVFI KPEVFLALGI VSLMENILVI 70 80 90 100 110 120 LAVVRNGNLH SPMYFFLCSL AAADMLVSLS NSLETIMIVV INSDSLTLED QFIQHMDNIF 130 140 150 160 170 180 DSMICISLVA SICNLLAIAV DRYVTIFYAL RYHSIMTVRK ALSLIVAIWV CCGICGVMFI 190 200 210 220 230 240 VYSESKMVIV CLITMFFAMV LLMGTLYIHM FLFARLHVQR IAALPPADGV APQQHSCMKG 250 260 270 280 290 300 AVTITILLGV FIFCWAPFFL HLVLIITCPT NPYCICYTAH FNTYLVLIMC NSVIDPLIYA 310 320 FRSLELRNTF KEILCGCNGM NVG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of a receptor for gamma melanotropin and other proopiomelanocortin peptides in the hypothalamus and limbic system." Roselli-Rehfuss L., Mountjoy K.G., Robbins L.S., Mortrud M.T., Low M.J., Simerly R.B., Cone R.D. Proc. Natl. Acad. Sci. U.S.A. 90:8856-8860(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Fischer. Tissue: Hypothalamus.
[2]	"Rattus norvegicus melanocortin 3 receptor: a corrected sequence." Daniels D., Suzuki A., Shapiro E., Luo L., Yee D.K., Fluharty S.J. Peptides 26:1835-1841(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Sprague-Dawley. Tissue: Brain.
[3]	"Genome sequence of the Brown Norway rat yields insights into mammalian evolution." Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M. , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S. Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Brown Norway.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X70667 mRNA. Translation: CAA50005.1. AY671938 mRNA. Translation: AAU87797.1. CH474062 Genomic DNA. Translation: EDL85154.1.
IPI	IPI00214326. IPI00851120.
PIR	S36636. A48254.
RefSeq	NP_001020441.3. NM_001025270.3.
UniGene	Rn.215838.
3D structure databases
ProteinModelPortal	P32244.
ModBase	Search...
Protein-protein interaction databases
STRING	10116.ENSRNOP00000005871.
Protein family/group databases
GPCRDB	Search...
Proteomic databases
PRIDE	P32244.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000005871; ENSRNOP00000005871; ENSRNOG00000004451.
GeneID	29310.
KEGG	rno:29310.
Organism-specific databases
CTD	4159.
RGD	3056. Mc3r.
Phylogenomic databases
eggNOG	NOG325361.
GeneTree	ENSGT00700000104085.
HOGENOM	HOG000246927.
HOVERGEN	HBG108148.
InParanoid	P32244.
KO	K04201.
OMA	VHMFLFA.
OrthoDB	EOG4640C7.
Gene expression databases
ArrayExpress	P32244.
Genevestigator	P32244.
GermOnline	ENSRNOG00000004451. Rattus norvegicus.
Family and domain databases
InterPro	IPR000276. GPCR_Rhodpsn. IPR017452. GPCR_Rhodpsn_7TM. IPR002122. Mcort_3_rcpt. IPR001908. Melancort_rcpt. IPR001671. Melcrt_ACTH_rcpt. [Graphical view]
PANTHER	PTHR22750:SF4. PTHR22750:SF4. 1 hit.
Pfam	PF00001. 7tm_1. 1 hit. [Graphical view]
PRINTS	PR00237. GPCRRHODOPSN. PR00534. MCRFAMILY. PR00535. MELNOCORTINR. PR01061. MELNOCORTN3R.
PROSITE	PS00237. G_PROTEIN_RECEP_F1_1. 1 hit. PS50262. G_PROTEIN_RECEP_F1_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P32244.
ChEMBL	CHEMBL4023.
NextBio	608746.

Entry information

Entry name

MC3R_RAT

Accession

Primary (citable) accession number: P32244
Secondary accession number(s): Q4KXA4

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	July 11, 2012
Last modified:	April 3, 2013
This is version 93 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program