MXL2_CAEEL
ID MXL2_CAEEL Reviewed; 205 AA.
AC Q9TZ70;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Max-like protein homolog 2 {ECO:0000312|WormBase:F40G9.11};
GN Name=mxl-2 {ECO:0000312|WormBase:F40G9.11};
GN ORFNames=F40G9.11 {ECO:0000312|WormBase:F40G9.11};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF
RP 65-SER--PRO-205.
RX PubMed=17826759; DOI=10.1016/j.ydbio.2007.07.034;
RA Pickett C.L., Breen K.T., Ayer D.E.;
RT "A C. elegans Myc-like network cooperates with semaphorin and Wnt signaling
RT pathways to control cell migration.";
RL Dev. Biol. 310:226-239(2007).
RN [3] {ECO:0000305}
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF 65-SER--PRO-205.
RX PubMed=24699255; DOI=10.1371/journal.pgen.1004278;
RA Johnson D.W., Llop J.R., Farrell S.F., Yuan J., Stolzenburg L.R.,
RA Samuelson A.V.;
RT "The Caenorhabditis elegans Myc-Mondo/Mad complexes integrate diverse
RT longevity signals.";
RL PLoS Genet. 10:e1004278-e1004278(2014).
RN [4] {ECO:0000305}
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF 65-SER--PRO-205.
RX PubMed=27402359; DOI=10.1534/g3.116.029983;
RA Botts M.R., Cohen L.B., Probert C.S., Wu F., Troemel E.R.;
RT "Microsporidia Intracellular Development Relies on Myc Interaction Network
RT Transcription Factors in the Host.";
RL G3 (Bethesda) 6:2707-2716(2016).
RN [5] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=27001890; DOI=10.1038/ncomms10944;
RA Nakamura S., Karalay O., Jaeger P.S., Horikawa M., Klein C., Nakamura K.,
RA Latza C., Templer S.E., Dieterich C., Antebi A.;
RT "Mondo complexes regulate TFEB via TOR inhibition to promote longevity in
RT response to gonadal signals.";
RL Nat. Commun. 7:10944-10944(2016).
CC -!- FUNCTION: Transcription factor (PubMed:17826759). Binds to the E box
CC motif 5'-CACGTG-3', probably in a heterodimeric complex with mml-1
CC (PubMed:17826759). Involved in modulating longevity in response to TOR
CC signaling, dietary restriction, the decline in protein homeostasis
CC associated with normal aging, germline signaling and the insulin-like
CC signaling pathway (PubMed:24699255, PubMed:27001890). Plays a role in
CC autophagy (PubMed:27001890). Involved in regulating migration of the
CC ray 1 precursor cells in the male tail, acting in concert with Wnt and
CC semaphorin signaling pathways (PubMed:17826759). Regulates
CC transcription of genes encoding extracellular matrix (ECM) components
CC which may contribute to the substratum required for migration of the
CC neighboring ray 1 precursor cells (PubMed:17826759). Required for
CC resistance to oxidative stress (PubMed:24699255). Involved in promoting
CC infection by the microsporidian pathogen N.parisii, probably acting
CC independently of its canonical partner, mml-1 (PubMed:27402359).
CC {ECO:0000269|PubMed:17826759, ECO:0000269|PubMed:24699255,
CC ECO:0000269|PubMed:27001890, ECO:0000269|PubMed:27402359}.
CC -!- INTERACTION:
CC Q9TZ70; P41846: mml-1; NbExp=3; IntAct=EBI-2408874, EBI-2408887;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981,
CC ECO:0000269|PubMed:17826759}. Cytoplasm {ECO:0000269|PubMed:27001890}.
CC Mitochondrion {ECO:0000269|PubMed:27001890}. Note=Only sporadic
CC mitochondrial localization. {ECO:0000269|PubMed:27001890}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:27001890}.
CC -!- DEVELOPMENTAL STAGE: Expressed in non-migratory, syncytial epidermis at
CC larval stage L1. {ECO:0000269|PubMed:17826759}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown reduces lifespan and is
CC further reduced on a daf-2 mutant background (PubMed:24699255). RNAi-
CC mediated knockdown causes premature onset of polyglutamine-mediated
CC paralysis (PubMed:24699255). RNAi-mediated knockdown reduces spore
CC levels of the microsporidian pathogen N.parisii during infection,
CC further reduced on an mdl-1 mutant background (PubMed:27402359).
CC {ECO:0000269|PubMed:24699255, ECO:0000269|PubMed:27402359}.
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DR EMBL; BX284603; CCD70935.1; -; Genomic_DNA.
DR PIR; T33628; T33628.
DR RefSeq; NP_497173.1; NM_064772.4.
DR AlphaFoldDB; Q9TZ70; -.
DR SMR; Q9TZ70; -.
DR IntAct; Q9TZ70; 1.
DR STRING; 6239.F40G9.11; -.
DR EPD; Q9TZ70; -.
DR PaxDb; Q9TZ70; -.
DR EnsemblMetazoa; F40G9.11.1; F40G9.11.1; WBGene00003510.
DR GeneID; 175184; -.
DR KEGG; cel:CELE_F40G9.11; -.
DR UCSC; F40G9.11; c. elegans.
DR CTD; 175184; -.
DR WormBase; F40G9.11; CE19858; WBGene00003510; mxl-2.
DR eggNOG; KOG1319; Eukaryota.
DR HOGENOM; CLU_115095_0_0_1; -.
DR InParanoid; Q9TZ70; -.
DR OMA; AHNTEDE; -.
DR OrthoDB; 1395792at2759; -.
DR PhylomeDB; Q9TZ70; -.
DR Reactome; R-CEL-163765; ChREBP activates metabolic gene expression.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00003510; Expressed in embryo and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
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:0008340; P:determination of adult lifespan; IGI:WormBase.
DR GO; GO:0010629; P:negative regulation of gene expression; IGI:WormBase.
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 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 Coiled coil; Cytoplasm; DNA-binding; Mitochondrion; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..205
FT /note="Max-like protein homolog 2"
FT /id="PRO_0000453379"
FT DOMAIN 47..101
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 47..60
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 61..101
FT /note="Helix-loop-helix motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT COILED 98..132
FT /evidence="ECO:0000255"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 65..205
FT /note="Missing: In tm1516; significant anterior
FT displacement of the first sensory ray of the male tail.
FT Anterior displacement of ray 1 is enhanced on a bar-1
FT mutant background. Reduced lifespan, further reduced on a
FT daf-2 mutant background. Reduced N.parisii spore levels,
FT further reduced on an mdl-1 mutant background."
FT /evidence="ECO:0000269|PubMed:17826759,
FT ECO:0000269|PubMed:24699255, ECO:0000269|PubMed:27402359"
SQ SEQUENCE 205 AA; 22060 MW; D03A21CBE007F542 CRC64;
MSRSRSAAAS SSQKPDDMDL MSPDGSASSP SAPNTPATNS GGFSSDRKKA THLRCERQRR
EAINSGYSDL KDLIPQTTTS LGCKTTNAAI LFRACDFMSQ LKTDISDADK QLAQLNAQAA
ALEMIASEYE QMASSVPDAG QSTIQVKMLQ LLLDDCFTSF SSQVDFTTYA TITRTLLSWV
ESLAPNAEPF KSTAGKMVTM PFTSP
