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MXL1_CAEEL
ID   MXL1_CAEEL              Reviewed;         124 AA.
AC   G5EEH5;
DT   10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Max-like protein 1 {ECO:0000303|PubMed:9764821};
GN   Name=mxl-1 {ECO:0000312|WormBase:T19B10.11};
GN   ORFNames=T19B10.11 {ECO:0000312|WormBase:T19B10.11};
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|EMBL:AAB40926.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, AND DEVELOPMENTAL STAGE.
RC   STRAIN=Bristol N2 {ECO:0000312|EMBL:AAB40926.1};
RX   PubMed=9764821; DOI=10.1038/sj.onc.1202036;
RA   Yuan J., Tirabassi R.S., Bush A.B., Cole M.D.;
RT   "The C. elegans MDL-1 and MXL-1 proteins can functionally substitute for
RT   vertebrate MAD and MAX.";
RL   Oncogene 17:1109-1118(1998).
RN   [2] {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   [3] {ECO:0000305}
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
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.
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).
CC   -!- FUNCTION: Transcriptional regulator which binds to the E box motif 5'-
CC       CACGTG-3', when in a heterodimeric complex with mdl-1 (PubMed:9764821).
CC       Involved in the control of lifespan in response to dietary restriction,
CC       the decline in protein homeostasis associated with normal aging and may
CC       overlap with the insulin-like signaling pathway (PubMed:24699255).
CC       Involved in promoting infection by the microsporidian pathogen
CC       N.parisii (PubMed:27402359). {ECO:0000269|PubMed:24699255,
CC       ECO:0000269|PubMed:27402359, ECO:0000269|PubMed:9764821}.
CC   -!- SUBUNIT: Heterodimer with mdl-1 in presence and absence of DNA.
CC       {ECO:0000269|PubMed:9764821}.
CC   -!- INTERACTION:
CC       G5EEH5; G5EG44: mdl-1; NbExp=5; IntAct=EBI-1182982, EBI-1182971;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
CC   -!- DEVELOPMENTAL STAGE: Expressed weakly in L1 animals and strongly
CC       throughout the remainder of larval development (PubMed:9764821).
CC       Expressed in posterior intestinal cells, neurons, hypodermal cells and
CC       body wall muscles (PubMed:9764821). {ECO:0000269|PubMed:9764821}.
CC   -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown increases lifespan, which
CC       is abolished on an mxl-2 or mml-1 mutant background, or by simultaneous
CC       RNAi-mediated knockdown of daf-16 or pha-4 (PubMed:24699255). RNAi-
CC       mediated knockdown causes delayed onset of polyglutamine-mediated
CC       paralysis (PubMed:24699255). {ECO:0000269|PubMed:24699255}.
CC   -!- SIMILARITY: Belongs to the MAX family. {ECO:0000305}.
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DR   EMBL; U82967; AAB40926.1; -; mRNA.
DR   EMBL; BX284605; CAA98543.1; -; Genomic_DNA.
DR   PIR; T24979; T24979.
DR   RefSeq; NP_505856.1; NM_073455.4.
DR   AlphaFoldDB; G5EEH5; -.
DR   SMR; G5EEH5; -.
DR   IntAct; G5EEH5; 1.
DR   STRING; 6239.T19B10.11; -.
DR   EPD; G5EEH5; -.
DR   PaxDb; G5EEH5; -.
DR   EnsemblMetazoa; T19B10.11.1; T19B10.11.1; WBGene00003509.
DR   GeneID; 179557; -.
DR   KEGG; cel:CELE_T19B10.11; -.
DR   CTD; 179557; -.
DR   WormBase; T19B10.11; CE16417; WBGene00003509; mxl-1.
DR   eggNOG; KOG2483; Eukaryota.
DR   GeneTree; ENSGT00530000064011; -.
DR   HOGENOM; CLU_109424_1_1_1; -.
DR   InParanoid; G5EEH5; -.
DR   OMA; PALHINE; -.
DR   OrthoDB; 1588329at2759; -.
DR   PhylomeDB; G5EEH5; -.
DR   Proteomes; UP000001940; Chromosome V.
DR   Bgee; WBGene00003509; Expressed in embryo and 3 other tissues.
DR   GO; GO:0071339; C:MLL1 complex; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IDA:WormBase.
DR   GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IBA:GO_Central.
DR   GO; GO:0005667; C:transcription regulator complex; IPI:WormBase.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR   GO; GO:0019904; F:protein domain specific binding; IPI:WormBase.
DR   GO; GO:0046982; F:protein heterodimerization activity; IPI:WormBase.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IEA:InterPro.
DR   GO; GO:0007568; P:aging; IMP:UniProtKB.
DR   GO; GO:0008340; P:determination of adult lifespan; IGI:WormBase.
DR   GO; GO:0045944; P:positive 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; IPR037933; MAX-like.
DR   InterPro; IPR002418; Tscrpt_reg_Myc.
DR   PANTHER; PTHR10328; PTHR10328; 1.
DR   Pfam; PF00010; HLH; 1.
DR   PRINTS; PR00044; LEUZIPPRMYC.
DR   SMART; SM00353; HLH; 1.
DR   SUPFAM; SSF47459; SSF47459; 1.
DR   PROSITE; PS50888; BHLH; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; DNA-binding; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..124
FT                   /note="Max-like protein 1"
FT                   /id="PRO_0000451994"
FT   DOMAIN          29..82
FT                   /note="bHLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT   REGION          1..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          29..42
FT                   /note="Basic motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT   REGION          43..82
FT                   /note="Helix-loop-helix motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT   COILED          86..113
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        7..44
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   124 AA;  13843 MW;  8E780B9D00B82B0D CRC64;
     MSDMSDLEDD QTGHCGSGEH SGPFDPKRHA REQHNALERR RRDNIKDMYT SLREVVPDAN
     GERVQASRAV ILKKAIESIE KGQSDSATLS VDVAEQESKN AKLREEIARL KAKKDPSSSQ
     SIIQ
 
 
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