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Melanocortin-2 receptor accessory protein 2 (MC2R accessory protein 2)

 MRAP2_HUMAN             Reviewed;         205 AA.
Q96G30; A8K9M1; Q8IXM9; Q8N2D1;
05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
01-MAR-2004, sequence version 2.
28-FEB-2018, entry version 118.
RecName: Full=Melanocortin-2 receptor accessory protein 2;
Short=MC2R accessory protein 2;
Name=MRAP2; Synonyms=C6orf117;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Amygdala, and Kidney;
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).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[3]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, and Colon;
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]
FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, GLYCOSYLATION AT ASN-9,
INTERACTION WITH MC1R; MC2R; MC3R; MC4R; MC5R AND MRAP, TISSUE
SPECIFICITY, AND MUTAGENESIS OF ASN-9.
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).
[6]
FUNCTION, SUBUNIT, TOPOLOGY, AND INTERACTION WITH MRAP.
PubMed=20371771; DOI=10.1126/scisignal.2000593;
Sebag J.A., Hinkle P.M.;
"Regulation of G protein-coupled receptor signaling: specific
dominant-negative effects of melanocortin 2 receptor accessory protein
2.";
Sci. Signal. 3:RA28-RA28(2010).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-89, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[8]
POLYMORPHISM, INVOLVEMENT IN OBESITY, AND VARIANTS TYR-88; VAL-115 AND
CYS-125.
PubMed=23869016; DOI=10.1126/science.1233000;
Asai M., Ramachandrappa S., Joachim M., Shen Y., Zhang R.,
Nuthalapati N., Ramanathan V., Strochlic D.E., Ferket P., Linhart K.,
Ho C., Novoselova T.V., Garg S., Ridderstrale M., Marcus C.,
Hirschhorn J.N., Keogh J.M., O'Rahilly S., Chan L.F., Clark A.J.,
Farooqi I.S., Majzoub J.A.;
"Loss of function of the melanocortin 2 receptor accessory protein 2
is associated with mammalian obesity.";
Science 341:275-278(2013).
-!- FUNCTION: Modulator of melanocortin receptor 4 (MC4R), a receptor
involved in energy homeostasis. Plays a central role in the
control of energy homeostasis and body weight regulation by
increasing ligand-sensitivity of MC4R and MC4R-mediated generation
of cAMP (By similarity). May also act as a negative regulator of
MC2R: competes with MRAP for binding to MC2R and impairs the
binding of corticotropin (ACTH) to MC2R. May also regulate
activity of other melanocortin receptors (MC1R, MC3R and MC5R);
however, additional evidences are required in vivo. {ECO:0000250,
ECO:0000269|PubMed:19329486, ECO:0000269|PubMed:20371771}.
-!- SUBUNIT: Homodimer and heterodimer. Forms antiparallel homodimers
and heterodimers with MRAP. Interacts with MC1R, MC2R, MC3R, MC4R
and MC5R. {ECO:0000269|PubMed:19329486,
ECO:0000269|PubMed:20371771}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-9537218, EBI-9537218;
Q8TCY5:MRAP; NbExp=3; IntAct=EBI-9537218, EBI-9538727;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19329486};
Single-pass membrane protein {ECO:0000269|PubMed:19329486}.
Endoplasmic reticulum membrane {ECO:0000269|PubMed:19329486};
Single-pass membrane protein {ECO:0000269|PubMed:19329486}.
Note=The formation of antiparallel homo- and heterodimers suggest
that N- and C-terminus can both localize in the cytoplasmic and
extracellular parts, depending on the context.
{ECO:0000269|PubMed:20371771}.
-!- TISSUE SPECIFICITY: Expressed in the adrenal gland and brain. Not
expressed in other tissues. {ECO:0000269|PubMed:19329486}.
-!- POLYMORPHISM: Genetic variations in MRAP2 define the body mass
index quantitative trait locus 18 (BMIQ18) [MIM:615457]. Variance
in body mass index is a susceptibility factor for obesity.
{ECO:0000269|PubMed:23869016}.
-!- 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:23869016}. Note=Disease
susceptibility may be associated with variations affecting the
gene represented in this entry.
-!- SIMILARITY: Belongs to the MRAP family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AK090775; BAC03517.1; -; mRNA.
EMBL; AK292736; BAF85425.1; -; mRNA.
EMBL; AL161621; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471051; EAW48646.1; -; Genomic_DNA.
EMBL; BC010003; AAH10003.2; -; mRNA.
EMBL; BC039855; AAH39855.1; -; mRNA.
CCDS; CCDS5001.1; -.
RefSeq; NP_001333470.1; NM_001346541.1.
RefSeq; NP_001333471.1; NM_001346542.1.
RefSeq; NP_001333473.1; NM_001346544.1.
RefSeq; NP_612418.2; NM_138409.3.
RefSeq; XP_016865709.1; XM_017010220.1.
UniGene; Hs.370055; -.
ProteinModelPortal; Q96G30; -.
BioGrid; 125195; 62.
DIP; DIP-48793N; -.
IntAct; Q96G30; 7.
STRING; 9606.ENSP00000257776; -.
iPTMnet; Q96G30; -.
PhosphoSitePlus; Q96G30; -.
BioMuta; MRAP2; -.
DMDM; 68565259; -.
PaxDb; Q96G30; -.
PeptideAtlas; Q96G30; -.
PRIDE; Q96G30; -.
DNASU; 112609; -.
Ensembl; ENST00000257776; ENSP00000257776; ENSG00000135324.
GeneID; 112609; -.
KEGG; hsa:112609; -.
UCSC; uc003pkg.5; human.
CTD; 112609; -.
DisGeNET; 112609; -.
EuPathDB; HostDB:ENSG00000135324.5; -.
GeneCards; MRAP2; -.
HGNC; HGNC:21232; MRAP2.
MalaCards; MRAP2; -.
MIM; 601665; phenotype.
MIM; 615410; gene.
MIM; 615457; phenotype.
neXtProt; NX_Q96G30; -.
OpenTargets; ENSG00000135324; -.
PharmGKB; PA162396161; -.
eggNOG; ENOG410IHNK; Eukaryota.
eggNOG; ENOG4111S4H; LUCA.
GeneTree; ENSGT00650000093438; -.
HOGENOM; HOG000290703; -.
HOVERGEN; HBG095178; -.
InParanoid; Q96G30; -.
OMA; TGAPHQE; -.
OrthoDB; EOG091G0J7D; -.
PhylomeDB; Q96G30; -.
TreeFam; TF338691; -.
SIGNOR; Q96G30; -.
GenomeRNAi; 112609; -.
PRO; PR:Q96G30; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000135324; -.
CleanEx; HS_MRAP2; -.
Genevisible; Q96G30; HS.
GO; GO:0005783; C:endoplasmic reticulum; IDA:BHF-UCL.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
GO; GO:0031780; F:corticotropin hormone receptor binding; IPI:BHF-UCL.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0070996; F:type 1 melanocortin receptor binding; IPI:BHF-UCL.
GO; GO:0031781; F:type 3 melanocortin receptor binding; IPI:BHF-UCL.
GO; GO:0031782; F:type 4 melanocortin receptor binding; IPI:BHF-UCL.
GO; GO:0031783; F:type 5 melanocortin receptor binding; IPI:BHF-UCL.
GO; GO:0097009; P:energy homeostasis; ISS:UniProtKB.
GO; GO:0006112; P:energy reserve metabolic process; ISS:UniProtKB.
GO; GO:0007631; P:feeding behavior; ISS:UniProtKB.
GO; GO:0106072; P:negative regulation of adenylate cyclase-activating G-protein coupled receptor signaling pathway; IDA:BHF-UCL.
GO; GO:1903077; P:negative regulation of protein localization to plasma membrane; IDA:BHF-UCL.
GO; GO:0106071; P:positive regulation of adenylate cyclase-activating G-protein coupled receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0030819; P:positive regulation of cAMP biosynthetic process; IEA:Ensembl.
GO; GO:0072659; P:protein localization to plasma membrane; IDA:BHF-UCL.
InterPro; IPR028111; MRAP.
Pfam; PF15183; MRAP; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Endoplasmic reticulum; Glycoprotein;
Membrane; Obesity; Phosphoprotein; Polymorphism; Reference proteome;
Transmembrane; Transmembrane helix.
CHAIN 1 205 Melanocortin-2 receptor accessory protein
2.
/FTId=PRO_0000089522.
TRANSMEM 45 65 Helical. {ECO:0000255}.
MOD_RES 89 89 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CARBOHYD 9 9 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19329486}.
VARIANT 88 88 N -> Y (found in a patient with obesity;
unknown pathological significance;
dbSNP:rs761868293).
{ECO:0000269|PubMed:23869016}.
/FTId=VAR_069986.
VARIANT 115 115 L -> V (found in a patient with obesity;
unknown pathological significance;
dbSNP:rs368589399).
{ECO:0000269|PubMed:23869016}.
/FTId=VAR_069987.
VARIANT 125 125 R -> C (found in a patient with obesity;
unknown pathological significance;
dbSNP:rs148904867).
{ECO:0000269|PubMed:23869016}.
/FTId=VAR_069988.
MUTAGEN 9 9 N->Q: Abolishes N-glycosylation.
{ECO:0000269|PubMed:19329486}.
CONFLICT 62 62 F -> I (in Ref. 1; BAC03517).
{ECO:0000305}.
SEQUENCE 205 AA; 23548 MW; 3B18B493AE75260B CRC64;
MSAQRLISNR TSQQSASNSD YTWEYEYYEI GPVSFEGLKA HKYSIVIGFW VGLAVFVIFM
FFVLTLLTKT GAPHQDNAES SEKRFRMNSF VSDFGRPLEP DKVFSRQGNE ESRSLFHCYI
NEVERLDRAK ACHQTTALDS DVQLQEAIRS SGQPEEELNR LMKFDIPNFV NTDQNYFGED
DLLISEPPIV LETKPLSQTS HKDLD


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