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Melanocortin receptor 3 (MC3-R)

 MC3R_HUMAN              Reviewed;         323 AA.
P41968; Q4KN27; Q9H517;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
11-JUL-2012, sequence version 3.
05-DEC-2018, entry version 166.
RecName: Full=Melanocortin receptor 3;
Short=MC3-R;
Name=MC3R;
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-44.
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).
[2]
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.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[4]
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).
[5]
TRANSLATIONAL START SITE.
PubMed=22433616; DOI=10.1159/000336070;
Tarnow P., Rediger A., Schulz A., Gruters A., Biebermann H.;
"Identification of the translation start site of the human
melanocortin 3 receptor.";
Obes. Facts 5:45-51(2012).
[6]
VARIANT ASN-146, AND ASSOCIATION WITH SUSCEPTIBILITY TO OBESITY.
PubMed=11889220; DOI=10.1210/jcem.87.3.8461;
Lee Y.-S., Poh L.K.-S., Loke K.-Y.;
"A novel melanocortin 3 receptor gene (MC3R) mutation associated with
severe obesity.";
J. Clin. Endocrinol. Metab. 87:1423-1426(2002).
[7]
CHARACTERIZATION OF VARIANTS ILE-44 AND ASN-146.
PubMed=15292330; DOI=10.1210/jc.2004-0367;
Tao Y.-X., Segaloff D.L.;
"Functional characterization of melanocortin-3 receptor variants
identify a loss-of-function mutation involving an amino acid critical
for G protein-coupled receptor activation.";
J. Clin. Endocrinol. Metab. 89:3936-3942(2004).
[8]
VARIANT SER-298, CHARACTERIZATION OF VARIANT SER-298, AND ASSOCIATION
WITH SUSCEPTIBILITY TO OBESITY.
PubMed=18231126; DOI=10.1038/sj.ejhg.5202005;
Mencarelli M., Walker G.E., Maestrini S., Alberti L., Verti B.,
Brunani A., Petroni M.L., Tagliaferri M., Liuzzi A., Di Blasio A.M.;
"Sporadic mutations in melanocortin receptor 3 in morbid obese
individuals.";
Eur. J. Hum. Genet. 16:581-586(2008).
-!- FUNCTION: Receptor for MSH (alpha, beta and gamma) and ACTH. This
receptor is mediated by G proteins which activate adenylate
cyclase. Required for expression of anticipatory patterns of
activity and wakefulness during periods of limited nutrient
availability and for the normal regulation of circadian clock
activity in the brain. {ECO:0000250|UniProtKB:P33033}.
-!- INTERACTION:
Q8TCY5:MRAP; NbExp=2; IntAct=EBI-9538510, EBI-9538727;
-!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
-!- TISSUE SPECIFICITY: Brain, placental, and gut tissues.
-!- POLYMORPHISM: Genetic variations in MC3R define the body mass
index quantitative trait locus 9 (BMIQ9) [MIM:602025]. Variance in
body mass index is a susceptibility factor for obesity.
{ECO:0000269|PubMed:11889220, ECO:0000269|PubMed:18231126}.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
{ECO:0000255|PROSITE-ProRule:PRU00521}.
-!- SEQUENCE CAUTION:
Sequence=AAC13541.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=AAH69105.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=AAH69599.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=AAH96702.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=AAH96737.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=AAH98169.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=AAH98351.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=AAO72726.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; L06155; AAC13541.1; ALT_INIT; Genomic_DNA.
EMBL; AY227893; AAO72726.1; ALT_INIT; mRNA.
EMBL; AL139824; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC069105; AAH69105.1; ALT_INIT; mRNA.
EMBL; BC069599; AAH69599.1; ALT_INIT; mRNA.
EMBL; BC096702; AAH96702.1; ALT_INIT; mRNA.
EMBL; BC096737; AAH96737.1; ALT_INIT; mRNA.
EMBL; BC098169; AAH98169.1; ALT_INIT; mRNA.
EMBL; BC098351; AAH98351.1; ALT_INIT; mRNA.
CCDS; CCDS13449.2; -.
PIR; B46647; B46647.
RefSeq; NP_063941.3; NM_019888.3.
UniGene; Hs.248018; -.
ProteinModelPortal; P41968; -.
BioGrid; 110329; 1.
DIP; DIP-48790N; -.
IntAct; P41968; 2.
STRING; 9606.ENSP00000243911; -.
BindingDB; P41968; -.
ChEMBL; CHEMBL4644; -.
GuidetoPHARMACOLOGY; 284; -.
BioMuta; MC3R; -.
DMDM; 395398606; -.
PaxDb; P41968; -.
PRIDE; P41968; -.
ProteomicsDB; 55478; -.
DNASU; 4159; -.
Ensembl; ENST00000243911; ENSP00000243911; ENSG00000124089.
GeneID; 4159; -.
KEGG; hsa:4159; -.
UCSC; uc002xxb.2; human.
CTD; 4159; -.
DisGeNET; 4159; -.
EuPathDB; HostDB:ENSG00000124089.4; -.
GeneCards; MC3R; -.
H-InvDB; HIX0040556; -.
HGNC; HGNC:6931; MC3R.
MalaCards; MC3R; -.
MIM; 155540; gene.
MIM; 602025; phenotype.
neXtProt; NX_P41968; -.
OpenTargets; ENSG00000124089; -.
Orphanet; 217031; NON RARE IN EUROPE: Obesity due to MC3R deficiency.
PharmGKB; PA30675; -.
eggNOG; KOG3656; Eukaryota.
eggNOG; ENOG410XRW9; LUCA.
GeneTree; ENSGT00940000153928; -.
HOGENOM; HOG000246927; -.
HOVERGEN; HBG108148; -.
InParanoid; P41968; -.
KO; K04201; -.
OMA; VHMFLFA; -.
OrthoDB; EOG091G0BVW; -.
PhylomeDB; P41968; -.
TreeFam; TF332646; -.
Reactome; R-HSA-375276; Peptide ligand-binding receptors.
Reactome; R-HSA-418555; G alpha (s) signalling events.
SIGNOR; P41968; -.
GeneWiki; Melanocortin_3_receptor; -.
GenomeRNAi; 4159; -.
PRO; PR:P41968; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000124089; Expressed in 4 organ(s), highest expression level in muscle tissue.
CleanEx; HS_MC3R; -.
Genevisible; P41968; HS.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
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; IPI:BHF-UCL.
GO; GO:0042923; F:neuropeptide binding; IMP:UniProtKB.
GO; GO:0017046; F:peptide hormone binding; IEA:Ensembl.
GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
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:0042309; P:homoiothermy; IEA:Ensembl.
GO; GO:0045475; P:locomotor rhythm; IEA:Ensembl.
GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; TAS:ProtInc.
GO; GO:0008217; P:regulation of blood pressure; IEA:Ensembl.
GO; GO:0060259; P:regulation of feeding behavior; IEA:Ensembl.
GO; GO:0002027; P:regulation of heart rate; IEA:Ensembl.
GO; GO:0055078; P:sodium ion homeostasis; IEA:Ensembl.
CDD; cd15352; 7tmA_MC3R; 1.
InterPro; IPR000276; GPCR_Rhodpsn.
InterPro; IPR017452; GPCR_Rhodpsn_7TM.
InterPro; IPR002122; Mcort_3_rcpt.
InterPro; IPR001908; Melancort_rcpt.
InterPro; IPR001671; Melcrt_ACTH_rcpt.
PANTHER; PTHR22750:SF4; PTHR22750:SF4; 1.
Pfam; PF00001; 7tm_1; 1.
PRINTS; PR00237; GPCRRHODOPSN.
PRINTS; PR00534; MCRFAMILY.
PRINTS; PR00535; MELNOCORTINR.
PRINTS; PR01061; MELNOCORTN3R.
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;
Biological rhythms; Cell membrane; Complete proteome;
G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane;
Palmitate; Polymorphism; Receptor; Reference proteome; Transducer;
Transmembrane; Transmembrane helix.
CHAIN 1 323 Melanocortin receptor 3.
/FTId=PRO_0000069718.
TOPO_DOM 1 37 Extracellular. {ECO:0000255}.
TRANSMEM 38 63 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 64 75 Cytoplasmic. {ECO:0000255}.
TRANSMEM 76 100 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 101 118 Extracellular. {ECO:0000255}.
TRANSMEM 119 140 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 141 160 Cytoplasmic. {ECO:0000255}.
TRANSMEM 161 181 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 182 186 Extracellular. {ECO:0000255}.
TRANSMEM 187 210 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 211 245 Cytoplasmic. {ECO:0000255}.
TRANSMEM 246 268 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 269 277 Extracellular. {ECO:0000255}.
TRANSMEM 278 301 Helical; Name=7. {ECO:0000255}.
TOPO_DOM 302 323 Cytoplasmic. {ECO:0000255}.
LIPID 315 315 S-palmitoyl cysteine. {ECO:0000255}.
CARBOHYD 2 2 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 16 16 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 28 28 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VARIANT 44 44 V -> I (have ligand binding and signaling
properties similar to wild-type;
dbSNP:rs3827103).
{ECO:0000269|PubMed:15292330,
ECO:0000269|PubMed:8463333}.
/FTId=VAR_020070.
VARIANT 146 146 I -> N (associated with susceptibility to
obesity; completely lacks signaling in
response to agonist stimulation;
coexpression of the wild-type and the
mutant receptor shows that it does not
exert dominant-negative activity on wild-
type; dbSNP:rs74315393).
{ECO:0000269|PubMed:11889220,
ECO:0000269|PubMed:15292330}.
/FTId=VAR_055000.
VARIANT 298 298 I -> S (associated with susceptibility to
obesity; in vitro expression studies
demonstrate that the mutation causes
complete loss of function; transfected
cells show diffuse cytoplasmic staining
indicating intracellular retention of the
receptor; dbSNP:rs121913556).
{ECO:0000269|PubMed:18231126}.
/FTId=VAR_055001.
SEQUENCE 323 AA; 36043 MW; 98B016FC80802A97 CRC64;
MNASCCLPSV QPTLPNGSEH LQAPFFSNQS SSAFCEQVFI KPEVFLSLGI VSLLENILVI
LAVVRNGNLH SPMYFFLCSL AVADMLVSVS NALETIMIAI VHSDYLTFED QFIQHMDNIF
DSMICISLVA SICNLLAIAV DRYVTIFYAL RYHSIMTVRK ALTLIVAIWV CCGVCGVVFI
VYSESKMVIV CLITMFFAMM LLMGTLYVHM FLFARLHVKR IAALPPADGV APQQHSCMKG
AVTITILLGV FIFCWAPFFL HLVLIITCPT NPYCICYTAH FNTYLVLIMC NSVIDPLIYA
FRSLELRNTF REILCGCNGM NLG


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