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Melanocortin-2 receptor accessory protein (B27) (Fat cell-specific low molecular weight protein) (Fat tissue-specific low MW protein)

 MRAP_HUMAN              Reviewed;         172 AA.
Q8TCY5; Q5EBR3; Q8TDB7; Q8WXC1; Q8WXC2;
19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 2.
12-SEP-2018, entry version 133.
RecName: Full=Melanocortin-2 receptor accessory protein;
AltName: Full=B27;
AltName: Full=Fat cell-specific low molecular weight protein;
AltName: Full=Fat tissue-specific low MW protein;
Name=MRAP; Synonyms=C21orf61, FALP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
TISSUE=Adipocyte;
PubMed=12054497; DOI=10.1016/S0006-291X(02)00354-6;
Xu A., Choi K.-L., Wang Y., Permana P.A., Xu L.Y., Bogardus C.,
Cooper G.J.S.;
"Identification of novel putative membrane proteins selectively
expressed during adipose conversion of 3T3-L1 cells.";
Biochem. Biophys. Res. Commun. 293:1161-1167(2002).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4).
TISSUE=Brain;
PubMed=12036298; DOI=10.1006/geno.2002.6782;
Gardiner K., Slavov D., Bechtel L., Davisson M.;
"Annotation of human chromosome 21 for relevance to Down syndrome:
gene structure and expression analysis.";
Genomics 79:833-843(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
TISSUE=Thyroid;
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).
[4]
FUNCTION, SUBUNIT, AND INTERACTION WITH MC1R; MC2R; MC3R; MC4R; MC5R
AND MRAP2.
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).
[5]
FUNCTION, SUBUNIT, TOPOLOGY, AND INTERACTION WITH MC2R AND MRAP2.
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).
[6]
INVOLVEMENT IN GCCD2, FUNCTION, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, AND INTERACTION WITH MC2R.
PubMed=15654338; DOI=10.1038/ng1501;
Metherell L.A., Chapple J.P., Cooray S., David A., Becker C.,
Rueschendorf F., Naville D., Begeot M., Khoo B., Nuernberg P.,
Huebner A., Cheetham M.E., Clark A.J.L.;
"Mutations in MRAP, encoding a new interacting partner of the ACTH
receptor, cause familial glucocorticoid deficiency type 2.";
Nat. Genet. 37:166-170(2005).
-!- FUNCTION: Modulator of melanocortin receptors (MC1R, MC2R, MC3R,
MC4R and MC5R). Acts by increasing ligand-sensitivity of
melanocortin receptors and enhancing generation of cAMP by the
receptors. Required both for MC2R trafficking to the cell surface
of adrenal cells and for signaling in response to corticotropin
(ACTH). May be involved in the intracellular trafficking pathways
in adipocyte cells. {ECO:0000269|PubMed:15654338,
ECO:0000269|PubMed:19329486, ECO:0000269|PubMed:20371771}.
-!- SUBUNIT: Homodimer and heterodimer. Forms antiparallel homodimers
and heterodimers with MRAP2. Interacts with MC1R, MC2R, MC3R, MC4R
and MC5R. {ECO:0000269|PubMed:15654338,
ECO:0000269|PubMed:19329486, ECO:0000269|PubMed:20371771}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-9538727, EBI-9538727;
Q01726:MC1R; NbExp=2; IntAct=EBI-9538727, EBI-9538513;
Q01718:MC2R; NbExp=2; IntAct=EBI-9538727, EBI-9537171;
P41968:MC3R; NbExp=2; IntAct=EBI-9538727, EBI-9538510;
P32245:MC4R; NbExp=2; IntAct=EBI-9538727, EBI-3910694;
P33032:MC5R; NbExp=2; IntAct=EBI-9538727, EBI-9538507;
Q96G30:MRAP2; NbExp=3; IntAct=EBI-9538727, EBI-9537218;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15654338};
Single-pass membrane protein {ECO:0000269|PubMed:15654338}.
Endoplasmic reticulum membrane {ECO:0000269|PubMed:15654338};
Single-pass membrane protein {ECO:0000269|PubMed:15654338}.
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 (PubMed:20371771).
Upon insulin stimulation, it is redistributed into spotty
structures throughout the cytoplasm.
{ECO:0000269|PubMed:20371771}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=4;
IsoId=Q8TCY5-4; Sequence=Displayed;
Name=1; Synonyms=Alpha, MRAP-alpha;
IsoId=Q8TCY5-1; Sequence=VSP_021020;
Name=2; Synonyms=Beta, MRAP-beta;
IsoId=Q8TCY5-2; Sequence=VSP_003863, VSP_003864;
Name=3; Synonyms=Short;
IsoId=Q8TCY5-3; Sequence=VSP_003862;
-!- TISSUE SPECIFICITY: Expressed in adrenal cortex, testis, breast,
thyroid, lymph node, ovary and fat. Expressed in adipose tissues.
{ECO:0000269|PubMed:15654338}.
-!- DISEASE: Glucocorticoid deficiency 2 (GCCD2) [MIM:607398]: A form
of glucocorticoid deficiency, a rare autosomal recessive disorder
characterized by resistance to ACTH action on the adrenal cortex,
adrenal insufficiency and an inability of the adrenal cortex to
produce cortisol. It usually presents in the neonatal period or in
early childhood with episodes of hypoglycemia and other symptoms
related to cortisol deficiency, including failure to thrive,
recurrent illnesses or infections, convulsions, and shock. In a
small number of patients hypoglycemia can be sufficiently severe
and persistent that it leads to serious long-term neurological
damage or death. The diagnosis is readily confirmed with a low
plasma cortisol measurement in the presence of an elevated ACTH
level, and normal aldosterone and plasma renin measurements.
{ECO:0000269|PubMed:15654338}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the MRAP family. {ECO:0000305}.
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EMBL; AF483549; AAL86908.1; -; mRNA.
EMBL; AY079152; AAL80042.1; -; mRNA.
EMBL; AF454915; AAL51048.1; -; mRNA.
EMBL; AF454916; AAL51049.1; -; mRNA.
EMBL; BC062721; AAH62721.1; -; mRNA.
CCDS; CCDS13612.1; -. [Q8TCY5-2]
CCDS; CCDS13613.1; -. [Q8TCY5-4]
RefSeq; NP_001272323.1; NM_001285394.1. [Q8TCY5-3]
RefSeq; NP_848932.1; NM_178817.3. [Q8TCY5-4]
RefSeq; NP_996781.1; NM_206898.1. [Q8TCY5-2]
RefSeq; XP_006724091.1; XM_006724028.3. [Q8TCY5-4]
RefSeq; XP_016883896.1; XM_017028407.1. [Q8TCY5-2]
UniGene; Hs.584940; -.
ProteinModelPortal; Q8TCY5; -.
BioGrid; 121114; 2.
DIP; DIP-29948N; -.
IntAct; Q8TCY5; 6.
STRING; 9606.ENSP00000306697; -.
iPTMnet; Q8TCY5; -.
PhosphoSitePlus; Q8TCY5; -.
BioMuta; MRAP; -.
DMDM; 116242634; -.
PaxDb; Q8TCY5; -.
PRIDE; Q8TCY5; -.
ProteomicsDB; 74191; -.
ProteomicsDB; 74192; -. [Q8TCY5-1]
ProteomicsDB; 74193; -. [Q8TCY5-2]
ProteomicsDB; 74194; -. [Q8TCY5-3]
DNASU; 56246; -.
Ensembl; ENST00000303645; ENSP00000306697; ENSG00000170262. [Q8TCY5-4]
Ensembl; ENST00000339944; ENSP00000343661; ENSG00000170262. [Q8TCY5-2]
Ensembl; ENST00000399784; ENSP00000382684; ENSG00000170262. [Q8TCY5-4]
GeneID; 56246; -.
KEGG; hsa:56246; -.
UCSC; uc002ypj.4; human. [Q8TCY5-4]
CTD; 56246; -.
DisGeNET; 56246; -.
EuPathDB; HostDB:ENSG00000170262.12; -.
GeneCards; MRAP; -.
HGNC; HGNC:1304; MRAP.
HPA; HPA011024; -.
MalaCards; MRAP; -.
MIM; 607398; phenotype.
MIM; 609196; gene.
neXtProt; NX_Q8TCY5; -.
OpenTargets; ENSG00000170262; -.
Orphanet; 361; Familial glucocorticoid deficiency.
PharmGKB; PA25856; -.
eggNOG; ENOG410J5NI; Eukaryota.
eggNOG; ENOG410ZAA2; LUCA.
GeneTree; ENSGT00650000093475; -.
HOGENOM; HOG000113646; -.
HOVERGEN; HBG052507; -.
InParanoid; Q8TCY5; -.
KO; K22398; -.
OMA; CPWSHSL; -.
OrthoDB; EOG091G0YHB; -.
PhylomeDB; Q8TCY5; -.
TreeFam; TF338691; -.
SIGNOR; Q8TCY5; -.
ChiTaRS; MRAP; human.
GenomeRNAi; 56246; -.
PRO; PR:Q8TCY5; -.
Proteomes; UP000005640; Chromosome 21.
Bgee; ENSG00000170262; Expressed in 102 organ(s), highest expression level in right adrenal gland.
CleanEx; HS_MRAP; -.
Genevisible; Q8TCY5; 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: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:0072659; P:protein localization to plasma membrane; IDA:BHF-UCL.
InterPro; IPR028111; MRAP.
PANTHER; PTHR28675; PTHR28675; 1.
Pfam; PF15183; MRAP; 1.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Complete proteome;
Endoplasmic reticulum; Membrane; Reference proteome; Transmembrane;
Transmembrane helix.
CHAIN 1 172 Melanocortin-2 receptor accessory
protein.
/FTId=PRO_0000096570.
TRANSMEM 38 58 Helical. {ECO:0000255}.
VAR_SEQ 1 59 Missing (in isoform 3).
{ECO:0000303|PubMed:12036298}.
/FTId=VSP_003862.
VAR_SEQ 68 68 M -> MR (in isoform 1).
{ECO:0000303|PubMed:12054497}.
/FTId=VSP_021020.
VAR_SEQ 69 101 RNSPKHHQTCPWSHGLNLHLCIQKCLPCHREPL -> SFNT
DESLLHSEVLPQTRAISCDELQAPREEGAA (in
isoform 2).
{ECO:0000303|PubMed:12054497}.
/FTId=VSP_003863.
VAR_SEQ 102 172 Missing (in isoform 2).
{ECO:0000303|PubMed:12054497}.
/FTId=VSP_003864.
SEQUENCE 172 AA; 19136 MW; 9F93F39B40FAAFEA CRC64;
MANGTNASAP YYSYEYYLDY LDLIPVDEKK LKAHKHSIVI AFWVSLAAFV VLLFLILLYM
SWSASPQMRN SPKHHQTCPW SHGLNLHLCI QKCLPCHREP LATSQAQASS VEPGSRTGPD
QPLRQESSST LPLGGFQTHP TLLWELTLNG GPLVRSKPSE PPPGDRTSQL QS


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