MRAP_MOUSE
ID MRAP_MOUSE Reviewed; 127 AA.
AC Q9D159; Q3TZ49; Q8R439;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Melanocortin-2 receptor accessory protein;
DE AltName: Full=Fat cell-specific low molecular weight protein;
DE AltName: Full=Fat tissue-specific low MW protein;
GN Name=Mrap; Synonyms=Falp;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND PROTEIN SEQUENCE OF 1-12
RP AND 105-117.
RC TISSUE=Adipocyte;
RX PubMed=12054497; DOI=10.1016/s0006-291x(02)00354-6;
RA Xu A., Choi K.-L., Wang Y., Permana P.A., Xu L.Y., Bogardus C.,
RA Cooper G.J.S.;
RT "Identification of novel putative membrane proteins selectively expressed
RT during adipose conversion of 3T3-L1 cells.";
RL Biochem. Biophys. Res. Commun. 293:1161-1167(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Inner ear;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Modulator of melanocortin receptors (MC1R, MC2R, MC3R, MC4R
CC and MC5R). Acts by increasing ligand-sensitivity of melanocortin
CC receptors and enhancing generation of cAMP by the receptors. Required
CC both for MC2R trafficking to the cell surface of adrenal cells and for
CC signaling in response to corticotropin (ACTH). May be involved in the
CC intracellular trafficking pathways in adipocyte cells (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Homodimer and heterodimer. Forms antiparallel homodimers and
CC heterodimers with MRAP2. Interacts with MC1R, MC2R, MC3R, MC4R and MC5R
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane
CC protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250};
CC Single-pass membrane protein {ECO:0000250}. Note=The formation of
CC antiparallel homo- and heterodimers suggest that N- and C-terminus can
CC both localize in the cytoplasmic and extracellular parts, depending on
CC the context. Upon insulin stimulation, it is redistributed into spotty
CC structures throughout the cytoplasm (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Alpha;
CC IsoId=Q9D159-1; Sequence=Displayed;
CC Name=2; Synonyms=Beta;
CC IsoId=Q9D159-2; Sequence=VSP_003865, VSP_003866;
CC -!- TISSUE SPECIFICITY: Largely restricted to fat tissues. Predominantly
CC expressed in mouse epididymal (white adipose tissue) and interscapular
CC (brown adipose tissue) fat pads. Expression is weak or absent in lung,
CC spleen, intestine, kidney, heart and skeletal muscle.
CC -!- DEVELOPMENTAL STAGE: Expressed during adipocyte differentiation.
CC Expression appears 2 days following induction of adipose conversion,
CC reaching a peak after 6 days.
CC -!- SIMILARITY: Belongs to the MRAP family. {ECO:0000305}.
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DR EMBL; AY079153; AAL80043.1; -; mRNA.
DR EMBL; AY079154; AAL80044.1; -; mRNA.
DR EMBL; AK003912; BAB23071.1; -; mRNA.
DR EMBL; AK158113; BAE34361.1; -; mRNA.
DR EMBL; BC027543; AAH27543.1; -; mRNA.
DR CCDS; CCDS28317.1; -. [Q9D159-1]
DR PIR; JC7859; JC7859.
DR RefSeq; NP_084120.1; NM_029844.3. [Q9D159-1]
DR AlphaFoldDB; Q9D159; -.
DR SMR; Q9D159; -.
DR STRING; 10090.ENSMUSP00000043890; -.
DR iPTMnet; Q9D159; -.
DR PhosphoSitePlus; Q9D159; -.
DR jPOST; Q9D159; -.
DR MaxQB; Q9D159; -.
DR PaxDb; Q9D159; -.
DR PeptideAtlas; Q9D159; -.
DR PRIDE; Q9D159; -.
DR ProteomicsDB; 291439; -. [Q9D159-1]
DR Antibodypedia; 22543; 149 antibodies from 29 providers.
DR DNASU; 77037; -.
DR Ensembl; ENSMUST00000038197; ENSMUSP00000043890; ENSMUSG00000039956. [Q9D159-1]
DR GeneID; 77037; -.
DR KEGG; mmu:77037; -.
DR UCSC; uc007zwl.1; mouse. [Q9D159-1]
DR CTD; 56246; -.
DR MGI; MGI:1924287; Mrap.
DR VEuPathDB; HostDB:ENSMUSG00000039956; -.
DR eggNOG; ENOG502SB3E; Eukaryota.
DR GeneTree; ENSGT00650000093475; -.
DR HOGENOM; CLU_133578_0_0_1; -.
DR InParanoid; Q9D159; -.
DR OMA; HPTCPWS; -.
DR OrthoDB; 1583183at2759; -.
DR PhylomeDB; Q9D159; -.
DR TreeFam; TF338691; -.
DR BioGRID-ORCS; 77037; 3 hits in 71 CRISPR screens.
DR PRO; PR:Q9D159; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q9D159; protein.
DR Bgee; ENSMUSG00000039956; Expressed in adrenal gland and 131 other tissues.
DR ExpressionAtlas; Q9D159; baseline and differential.
DR Genevisible; Q9D159; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0031780; F:corticotropin hormone receptor binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0030545; F:signaling receptor regulator activity; IBA:GO_Central.
DR GO; GO:0070996; F:type 1 melanocortin receptor binding; ISO:MGI.
DR GO; GO:0031781; F:type 3 melanocortin receptor binding; ISO:MGI.
DR GO; GO:0031782; F:type 4 melanocortin receptor binding; ISO:MGI.
DR GO; GO:0031783; F:type 5 melanocortin receptor binding; ISO:MGI.
DR GO; GO:0050873; P:brown fat cell differentiation; IDA:MGI.
DR GO; GO:0106072; P:negative regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:1903077; P:negative regulation of protein localization to plasma membrane; ISO:MGI.
DR GO; GO:0106071; P:positive regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISO:MGI.
DR GO; GO:0106070; P:regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR InterPro; IPR028111; MRAP.
DR PANTHER; PTHR28675; PTHR28675; 1.
DR Pfam; PF15183; MRAP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Direct protein sequencing;
KW Endoplasmic reticulum; Membrane; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..127
FT /note="Melanocortin-2 receptor accessory protein"
FT /id="PRO_0000096571"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 97..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 94
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 36..55
FT /note="HSIVIALWLSLATFVVLLFL -> RKSEHRKVTRQRLGLGLSRG (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:12054497"
FT /id="VSP_003865"
FT VAR_SEQ 56..127
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12054497"
FT /id="VSP_003866"
SQ SEQUENCE 127 AA; 14170 MW; 87761AAAC35A8753 CRC64;
MANGTDASVP LTSYEYYLDY IDLIPVDEKK LKANKHSIVI ALWLSLATFV VLLFLILLYM
SWSGSPQMRH SPQPQPICSW THSFNLPLCL RRASLQTTEE PGRRAGTDQW LTQQSPSASA
PGPLALP
