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MLX-interacting protein (Transcriptional activator MondoA)

 MLXIP_MOUSE             Reviewed;         917 AA.
Q2VPU4; Q6NXJ4; Q6P9J8; Q8C8C6; Q8VI53;
21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
10-JAN-2006, sequence version 1.
28-MAR-2018, entry version 97.
RecName: Full=MLX-interacting protein;
AltName: Full=Transcriptional activator MondoA;
Name=Mlxip {ECO:0000312|MGI:MGI:2141183};
Synonyms=Mir {ECO:0000312|EMBL:AAL55724.1};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1] {ECO:0000305, ECO:0000312|EMBL:AAY41069.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
STRAIN=C57BL/6J {ECO:0000312|EMBL:AAY41069.1};
TISSUE=Skeletal muscle {ECO:0000312|EMBL:AAY41069.1};
PubMed=16644671; DOI=10.2337/db05-0822;
Li M.V., Chang B., Imamura M., Poungvarin N., Chan L.;
"Glucose-dependent transcriptional regulation by an evolutionarily
conserved glucose-sensing module.";
Diabetes 55:1179-1189(2006).
[2] {ECO:0000305, ECO:0000312|EMBL:BAC33069.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC33069.1};
TISSUE=Cerebellum {ECO:0000312|EMBL:BAC33069.1};
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3] {ECO:0000305, ECO:0000312|EMBL:AAL55724.1}
PROTEIN SEQUENCE OF 215-220, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=OF1; TISSUE=Hippocampus;
Lubec G., Sunyer B., Chen W.-Q.;
Submitted (JAN-2009) to UniProtKB.
[4] {ECO:0000305, ECO:0000312|EMBL:AAH67045.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 473-917 (ISOFORM 1).
STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH67045.1};
TISSUE=Brain {ECO:0000312|EMBL:AAH67045.1};
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] {ECO:0000305, ECO:0000312|EMBL:AAL55724.1}
NUCLEOTIDE SEQUENCE [MRNA] OF 499-917 (ISOFORM 1).
STRAIN=Swiss Webster / NIH {ECO:0000312|EMBL:AAL55724.1};
Merla G., Cairo S., Reymond A.;
"Mir a new partner for the Max-like protein, Mlx.";
Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
[6] {ECO:0000305}
FUNCTION, SUBUNIT, INTERACTION WITH MLX, SUBCELLULAR LOCATION, AND
DEVELOPMENTAL STAGE.
PubMed=11073985; DOI=10.1128/MCB.20.23.8845-8854.2000;
Billin A.N., Eilers A.L., Coulter K.L., Logan J.S., Ayer D.E.;
"MondoA, a novel basic helix-loop-helix-leucine zipper transcriptional
activator that constitutes a positive branch of a max-like network.";
Mol. Cell. Biol. 20:8845-8854(2000).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Kidney, Pancreas, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Binds DNA as a heterodimer with MLX and activates
transcription. Binds to the canonical E box sequence 5'-CACGTG-3'.
Plays a role in transcriptional activation of glycolytic target
genes. Involved in glucose-responsive gene regulation.
{ECO:0000250|UniProtKB:Q9HAP2, ECO:0000269|PubMed:11073985,
ECO:0000269|PubMed:16644671}.
-!- SUBUNIT: Efficient DNA binding requires dimerization with another
bHLH protein. Binds DNA as a homodimer or a heterodimer with MLX.
{ECO:0000269|PubMed:11073985}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11073985}.
Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981,
ECO:0000269|PubMed:11073985}. Mitochondrion outer membrane
{ECO:0000269|PubMed:11073985}. Note=Predominantly cytoplasmic but
shuttles between cytoplasm and nucleus when associated with MLX.
Also associates with the outer mitochondrial membrane and may
shuttle between the outer mitochondrial membrane and the nucleus.
{ECO:0000250|UniProtKB:Q9HAP2, ECO:0000269|PubMed:11073985}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1 {ECO:0000269|PubMed:16644671};
IsoId=Q2VPU4-1; Sequence=Displayed;
Name=2 {ECO:0000269|PubMed:16141072};
IsoId=Q2VPU4-2; Sequence=VSP_052505, VSP_052506;
Note=No experimental confirmation available. {ECO:0000305};
-!- DEVELOPMENTAL STAGE: Broadly expressed from 9.5 dpc to at least 15
dpc, with slightly elevated levels in the developing nervous
system. {ECO:0000269|PubMed:11073985}.
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EMBL; AY968204; AAY41069.1; -; mRNA.
EMBL; AK047475; BAC33069.1; -; mRNA.
EMBL; BC060733; AAH60733.1; -; mRNA.
EMBL; BC067045; AAH67045.1; -; mRNA.
EMBL; AF265663; AAL55724.1; -; mRNA.
CCDS; CCDS19662.1; -. [Q2VPU4-1]
CCDS; CCDS39268.1; -. [Q2VPU4-2]
RefSeq; NP_598678.2; NM_133917.3.
RefSeq; NP_808250.1; NM_177582.3.
UniGene; Mm.83277; -.
ProteinModelPortal; Q2VPU4; -.
SMR; Q2VPU4; -.
BioGrid; 228948; 2.
STRING; 10090.ENSMUSP00000064943; -.
iPTMnet; Q2VPU4; -.
PhosphoSitePlus; Q2VPU4; -.
MaxQB; Q2VPU4; -.
PaxDb; Q2VPU4; -.
PRIDE; Q2VPU4; -.
GeneID; 208104; -.
KEGG; mmu:208104; -.
CTD; 22877; -.
MGI; MGI:2141183; Mlxip.
eggNOG; KOG3582; Eukaryota.
eggNOG; ENOG410XTA5; LUCA.
HOGENOM; HOG000113606; -.
HOVERGEN; HBG062003; -.
InParanoid; Q2VPU4; -.
KO; K09113; -.
PhylomeDB; Q2VPU4; -.
PRO; PR:Q2VPU4; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_MLXIP; -.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0003700; F:DNA binding transcription factor activity; IBA:GO_Central.
GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; ISO:MGI.
GO; GO:0000989; F:transcription factor activity, transcription factor binding; IEA:InterPro.
GO; GO:0001228; F:transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:MGI.
GO; GO:0006913; P:nucleocytoplasmic transport; IDA:MGI.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
GO; GO:1900402; P:regulation of carbohydrate metabolic process by regulation of transcription from RNA polymerase II promoter; ISO:MGI.
GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
CDD; cd00083; HLH; 1.
Gene3D; 4.10.280.10; -; 1.
InterPro; IPR011598; bHLH_dom.
InterPro; IPR036638; HLH_DNA-bd_sf.
InterPro; IPR032648; MLXIP.
PANTHER; PTHR15741:SF23; PTHR15741:SF23; 1.
Pfam; PF00010; HLH; 1.
SMART; SM00353; HLH; 1.
SUPFAM; SSF47459; SSF47459; 1.
PROSITE; PS50888; BHLH; 1.
1: Evidence at protein level;
Acetylation; Activator; Alternative splicing; Complete proteome;
Cytoplasm; Direct protein sequencing; DNA-binding; Membrane;
Mitochondrion; Mitochondrion outer membrane; Nucleus; Phosphoprotein;
Reference proteome; Transcription; Transcription regulation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q9HAP2}.
CHAIN 2 917 MLX-interacting protein.
/FTId=PRO_0000298764.
DOMAIN 717 767 bHLH. {ECO:0000255|PROSITE-
ProRule:PRU00981}.
REGION 73 327 Required for cytoplasmic localization.
{ECO:0000250|UniProtKB:Q9HAP2}.
REGION 322 445 Transactivation domain.
{ECO:0000269|PubMed:11073985}.
REGION 767 788 Leucine-zipper.
REGION 830 879 Mediates heterotypic interactions between
MLXIP and MLX and is required for
cytoplasmic localization.
{ECO:0000250|UniProtKB:Q9HAP2}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:Q9HAP2}.
MOD_RES 9 9 Phosphoserine.
{ECO:0000250|UniProtKB:Q9HAP2}.
MOD_RES 33 33 Phosphoserine.
{ECO:0000250|UniProtKB:Q9HAP2}.
MOD_RES 39 39 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 667 667 Phosphoserine.
{ECO:0000250|UniProtKB:Q9HAP2}.
VAR_SEQ 583 614 AAFSGQPQKVIMTSAPLKREGILASTVSPSNV -> GELVG
GVVSQNCLGSNVSLSLRLYIGKNSLPT (in isoform
2). {ECO:0000303|PubMed:16141072}.
/FTId=VSP_052505.
VAR_SEQ 615 917 Missing (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_052506.
CONFLICT 179 179 R -> K (in Ref. 2; BAC33069).
{ECO:0000305}.
SEQUENCE 917 AA; 100804 MW; 2944C041E78F89FC CRC64;
MAADVFMCSP RRPRSRGRSV LLKPQVPEDD DDSDTDEPSP PPPSGVATSA RAHASAAPLP
PRAGPGREEP PRRQQIIHSG HFMVSSPHRE HPPKKGYDFD TVNKQTCQTY SFGKTSSCHL
SIDASLTKLF ECMTLAYSGK LVSPKWKNFK GLKLQWRDKI RLNNAIWRAW YMQYLEKRRN
PVCHFVTPLD GSVDVDEHRR PEAITTEGKY WKSRIEIVIR EYHKWRTYFK KRLQQHKDED
LSSLAQDDDM LYWHKHGDGW KTPVPMEEDS LLDTDMLMSE FSDTLFSTLS SHQPVAWPNP
REIAHLGNAD MIQPGLIPLQ PNLDFMDTFE PFQDLFSSSR SIFGSMLPPP SSLPAADPSS
PPSQGNILPN TALPPASLPN SLITSSAAPS LDPTEGQGCE RTSQTVDPFI QPADFGPSEP
PLSVPQPFLP VFTMTLLSPG PAPAPVPTAL PLVPSPAPTL NPPTPPAFLQ PQKFAGVSKS
TPVITHTASA TLTHDASATT FSQNQGLVIT AHHPTPSSSP CALALSPVPQ PPAVGPPQPH
LTFIHPKPVS LTGVRHKQPP KIVPAPKPEP VSLVLKNACI APAAFSGQPQ KVIMTSAPLK
REGILASTVS PSNVVIASAA ITRASGVTEF LSHSTSSQPS PVSRLFSPST VQDSLVKGEQ
VSLHGGSPQV PATGSSRDCP NSGQASPCPS EQSPSPQSPQ NNCSGKSTDP KNVAALKNRQ
KHISAEQKRR FNIRMGFNTL NSLISNNSKQ TSHAITLQKT MEYITKLQQE RMQMQEEARR
LREEIEELNT TIISCQQLLP ATGVPVNCRQ LDHMRDMFDE YVKSRTLQNW KFWIFSMIIK
PLFESFKGMV STSSLEEFHR TALSWLDQHC SLPVLRPMVL STLRQLSTTT SILTDPSQLP
EQASEAVTRM GKRSGES


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