MLXIP_MOUSE
ID MLXIP_MOUSE Reviewed; 917 AA.
AC Q2VPU4; Q6NXJ4; Q6P9J8; Q8C8C6; Q8VI53;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=MLX-interacting protein;
DE AltName: Full=Transcriptional activator MondoA;
GN Name=Mlxip {ECO:0000312|MGI:MGI:2141183};
GN Synonyms=Mir {ECO:0000312|EMBL:AAL55724.1};
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] {ECO:0000305, ECO:0000312|EMBL:AAY41069.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAY41069.1};
RC TISSUE=Skeletal muscle {ECO:0000312|EMBL:AAY41069.1};
RX PubMed=16644671; DOI=10.2337/db05-0822;
RA Li M.V., Chang B., Imamura M., Poungvarin N., Chan L.;
RT "Glucose-dependent transcriptional regulation by an evolutionarily
RT conserved glucose-sensing module.";
RL Diabetes 55:1179-1189(2006).
RN [2] {ECO:0000305, ECO:0000312|EMBL:BAC33069.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC33069.1};
RC TISSUE=Cerebellum {ECO:0000312|EMBL:BAC33069.1};
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] {ECO:0000305, ECO:0000312|EMBL:AAL55724.1}
RP PROTEIN SEQUENCE OF 215-220, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [4] {ECO:0000305, ECO:0000312|EMBL:AAH67045.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 473-917 (ISOFORM 1).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH67045.1};
RC TISSUE=Brain {ECO:0000312|EMBL:AAH67045.1};
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 [5] {ECO:0000305, ECO:0000312|EMBL:AAL55724.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 499-917 (ISOFORM 1).
RC STRAIN=Swiss Webster / NIH {ECO:0000312|EMBL:AAL55724.1};
RA Merla G., Cairo S., Reymond A.;
RT "Mir a new partner for the Max-like protein, Mlx.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000305}
RP FUNCTION, SUBUNIT, INTERACTION WITH MLX, SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=11073985; DOI=10.1128/mcb.20.23.8845-8854.2000;
RA Billin A.N., Eilers A.L., Coulter K.L., Logan J.S., Ayer D.E.;
RT "MondoA, a novel basic helix-loop-helix-leucine zipper transcriptional
RT activator that constitutes a positive branch of a max-like network.";
RL Mol. Cell. Biol. 20:8845-8854(2000).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Pancreas, and Spleen;
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: Binds DNA as a heterodimer with MLX and activates
CC transcription. Binds to the canonical E box sequence 5'-CACGTG-3'.
CC Plays a role in transcriptional activation of glycolytic target genes.
CC Involved in glucose-responsive gene regulation.
CC {ECO:0000250|UniProtKB:Q9HAP2, ECO:0000269|PubMed:11073985,
CC ECO:0000269|PubMed:16644671}.
CC -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC protein. Binds DNA as a homodimer or a heterodimer with MLX.
CC {ECO:0000269|PubMed:11073985}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11073985}. Nucleus
CC {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:11073985}.
CC Mitochondrion outer membrane {ECO:0000269|PubMed:11073985}.
CC Note=Predominantly cytoplasmic but shuttles between cytoplasm and
CC nucleus when associated with MLX. Also associates with the outer
CC mitochondrial membrane and may shuttle between the outer mitochondrial
CC membrane and the nucleus. {ECO:0000250|UniProtKB:Q9HAP2,
CC ECO:0000269|PubMed:11073985}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:16644671};
CC IsoId=Q2VPU4-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:16141072};
CC IsoId=Q2VPU4-2; Sequence=VSP_052505, VSP_052506;
CC -!- DEVELOPMENTAL STAGE: Broadly expressed from 9.5 dpc to at least 15 dpc,
CC with slightly elevated levels in the developing nervous system.
CC {ECO:0000269|PubMed:11073985}.
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DR EMBL; AY968204; AAY41069.1; -; mRNA.
DR EMBL; AK047475; BAC33069.1; -; mRNA.
DR EMBL; BC060733; AAH60733.1; -; mRNA.
DR EMBL; BC067045; AAH67045.1; -; mRNA.
DR EMBL; AF265663; AAL55724.1; -; mRNA.
DR CCDS; CCDS19662.1; -. [Q2VPU4-1]
DR CCDS; CCDS39268.1; -. [Q2VPU4-2]
DR RefSeq; NP_598678.2; NM_133917.3.
DR RefSeq; NP_808250.1; NM_177582.3.
DR AlphaFoldDB; Q2VPU4; -.
DR SMR; Q2VPU4; -.
DR BioGRID; 228948; 3.
DR STRING; 10090.ENSMUSP00000064943; -.
DR iPTMnet; Q2VPU4; -.
DR PhosphoSitePlus; Q2VPU4; -.
DR MaxQB; Q2VPU4; -.
DR PaxDb; Q2VPU4; -.
DR PRIDE; Q2VPU4; -.
DR ProteomicsDB; 295682; -. [Q2VPU4-1]
DR ProteomicsDB; 295683; -. [Q2VPU4-2]
DR DNASU; 208104; -.
DR GeneID; 208104; -.
DR KEGG; mmu:208104; -.
DR CTD; 22877; -.
DR MGI; MGI:2141183; Mlxip.
DR eggNOG; KOG3582; Eukaryota.
DR InParanoid; Q2VPU4; -.
DR OrthoDB; 388166at2759; -.
DR PhylomeDB; Q2VPU4; -.
DR BioGRID-ORCS; 208104; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Mlxip; mouse.
DR PRO; PR:Q2VPU4; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q2VPU4; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IDA:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR InterPro; IPR032648; MLXIP.
DR PANTHER; PTHR15741:SF23; PTHR15741:SF23; 1.
DR Pfam; PF00010; HLH; 1.
DR SMART; SM00353; HLH; 1.
DR SUPFAM; SSF47459; SSF47459; 1.
DR PROSITE; PS50888; BHLH; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Alternative splicing; Cytoplasm;
KW Direct protein sequencing; DNA-binding; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9HAP2"
FT CHAIN 2..917
FT /note="MLX-interacting protein"
FT /id="PRO_0000298764"
FT DOMAIN 717..767
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 1..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 73..327
FT /note="Required for cytoplasmic localization"
FT /evidence="ECO:0000250|UniProtKB:Q9HAP2"
FT REGION 322..445
FT /note="Transactivation domain"
FT /evidence="ECO:0000269|PubMed:11073985"
FT REGION 347..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 632..711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 767..788
FT /note="Leucine-zipper"
FT REGION 830..879
FT /note="Mediates heterotypic interactions between MLXIP and
FT MLX and is required for cytoplasmic localization"
FT /evidence="ECO:0000250|UniProtKB:Q9HAP2"
FT REGION 897..917
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..402
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 632..657
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..711
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9HAP2"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HAP2"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HAP2"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 667
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HAP2"
FT VAR_SEQ 583..614
FT /note="AAFSGQPQKVIMTSAPLKREGILASTVSPSNV -> GELVGGVVSQNCLGSN
FT VSLSLRLYIGKNSLPT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_052505"
FT VAR_SEQ 615..917
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_052506"
FT CONFLICT 179
FT /note="R -> K (in Ref. 2; BAC33069)"
FT /evidence="ECO:0000305"
SQ 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
