MLXPL_RAT
ID MLXPL_RAT Reviewed; 865 AA.
AC Q8VIP2;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Carbohydrate-responsive element-binding protein;
DE Short=ChREBP;
DE AltName: Full=Class D basic helix-loop-helix protein 14;
DE Short=bHLHd14;
DE AltName: Full=MLX interactor;
DE AltName: Full=MLX-interacting protein-like;
DE AltName: Full=WS basic-helix-loop-helix leucine zipper protein;
DE Short=WS-bHLH;
DE AltName: Full=Williams-Beuren syndrome chromosomal region 14 protein;
GN Name=Mlxipl; Synonyms=Wbscr14;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION AT SER-568, AND MUTAGENESIS OF
RP SER-568.
RX PubMed=11724780; DOI=10.1074/jbc.m107895200;
RA Kawaguchi T., Osatomi K., Yamashita H., Kabashima T., Uyeda K.;
RT "Mechanism for fatty acid 'sparing' effect on glucose-induced
RT transcription: regulation of carbohydrate-responsive element-binding
RT protein by AMP-activated protein kinase.";
RL J. Biol. Chem. 277:3829-3835(2002).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-25; THR-27 AND
RP SER-615, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Transcriptional repressor. Binds to the canonical and non-
CC canonical E box sequences 5'-CACGTG-3' (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Binds DNA as a heterodimer with TCFL4/MLX. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
CC -!- PTM: Phosphorylation at Ser-568 by AMPK inactivates the DNA-binding
CC activity. {ECO:0000269|PubMed:11724780}.
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DR EMBL; AB074517; BAB77523.1; -; mRNA.
DR RefSeq; NP_598236.1; NM_133552.1.
DR PDB; 5F74; X-ray; 2.35 A; B=1-196.
DR PDBsum; 5F74; -.
DR AlphaFoldDB; Q8VIP2; -.
DR SMR; Q8VIP2; -.
DR iPTMnet; Q8VIP2; -.
DR PhosphoSitePlus; Q8VIP2; -.
DR PaxDb; Q8VIP2; -.
DR PRIDE; Q8VIP2; -.
DR GeneID; 171078; -.
DR KEGG; rno:171078; -.
DR CTD; 51085; -.
DR RGD; 620400; Mlxipl.
DR InParanoid; Q8VIP2; -.
DR OrthoDB; 388166at2759; -.
DR PhylomeDB; Q8VIP2; -.
DR Reactome; R-RNO-163358; PKA-mediated phosphorylation of key metabolic factors.
DR Reactome; R-RNO-163765; ChREBP activates metabolic gene expression.
DR PRO; PR:Q8VIP2; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IDA:BHF-UCL.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR GO; GO:0005667; C:transcription regulator complex; ISO:RGD.
DR GO; GO:0035538; F:carbohydrate response element binding; NAS:BHF-UCL.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:RGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:RGD.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:RGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:RGD.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IDA:BHF-UCL.
DR GO; GO:0097009; P:energy homeostasis; IMP:UniProtKB.
DR GO; GO:0055089; P:fatty acid homeostasis; IMP:UniProtKB.
DR GO; GO:0042593; P:glucose homeostasis; ISO:RGD.
DR GO; GO:0010255; P:glucose mediated signaling pathway; ISO:RGD.
DR GO; GO:0090324; P:negative regulation of oxidative phosphorylation; ISO:RGD.
DR GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0045723; P:positive regulation of fatty acid biosynthetic process; ISO:RGD.
DR GO; GO:0045821; P:positive regulation of glycolytic process; ISO:RGD.
DR GO; GO:0046889; P:positive regulation of lipid biosynthetic process; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0006110; P:regulation of glycolytic process; IDA:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:RGD.
DR GO; GO:0009749; P:response to glucose; IDA:RGD.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
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 3D-structure; DNA-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Repressor; Transcription; Transcription regulation.
FT CHAIN 1..865
FT /note="Carbohydrate-responsive element-binding protein"
FT /id="PRO_0000413065"
FT DOMAIN 662..716
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 15..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 53..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 716..737
FT /note="Leucine-zipper"
FT COMPBIAS 342..375
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..539
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..602
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 620..638
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NP71"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 27
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 196
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NP71"
FT MOD_RES 568
FT /note="Phosphoserine; by AMPK"
FT /evidence="ECO:0000269|PubMed:11724780"
FT MOD_RES 615
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 627
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NP71"
FT MOD_RES 644
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NP71"
FT MUTAGEN 568
FT /note="S->A: Impaired DNA-binding and fatty acid
FT sensitivity."
FT /evidence="ECO:0000269|PubMed:11724780"
FT HELIX 118..134
FT /evidence="ECO:0007829|PDB:5F74"
SQ SEQUENCE 865 AA; 94921 MW; 5B818B081B83C641 CRC64;
MARALADLSV NLQVPRVVPS PDSDSDTDLE DPSPRRSAGG LHRSQVIHSG HFMVSSPHSD
SLTRRRDQEG PVGLADFGPR SIDPTLTRLF ECLSLAYSGK LVSPKWKNFK GLKLLCRDKI
RLNNAIWRAW YIQYVQRRKS PVCGFVTPLQ GSEADEHRKP EAVVLEGNYW KRRIEVVMRE
YHKWRIYYKK RLRKSSREGD FLAPKQVEGG WPPPERWCEQ LFSSVVPVLL GGSEEEPGGR
QLLDLDCFLS DISDTLFTMT QPSPSSLQLP SEDAYVGNAD MIQPDLTPLQ PSLDDFMEIS
DFFTNYRPPQ TPTSSNFPEP PSFGPMADSL FSGGILGPEM PSPASASSSS GMTPLSGNTR
LQARNSCSGP LDPSTFPSSE FLLPEDPKTK MPPAPVPTPL LPYPGPVKVH GLEPCTPSPF
PTMAPPPALL SEEPLFSARF PFTTVPPAPG VSTLPAPTTF VPTPQPGPGP GPVPFPVDHL
PHGYLEPVFG PHFTVPQGVQ PRCKPCSPPP GGRKASPPTL TSATASPTAT ATARDNNPCL
TQLLRAAKPE QVLEPSTVPS TLLRPPESPD AVPEIPRVRA FYPPIPAPTP PRPPPGPATL
APPRSLVVPK AERLSPPASS GSERRPSGDL NSIQPPGALS VHLSPPQTVL SRGRVDNNKM
ENRRITHISA EQKRRFNIKL GFDTLHGLVS TLSAQPSLKV SKATTLQKTA EYILMLQQER
AAMQEEAQQL RDEIEELNAA INLCQQQLPA TGVPITHQRF DQMRDMFDDY VRTRTLHNWK
FWVFSILIRP LFESFNGMVS TASLHSLRQT SLAWLDQYCS LPALRPTVLN SLRQLSTSTS
ILTDPSLVPE QATRAVTEGP LGRPL
