ID A0A1S3F925_DIPOR Unreviewed; 160 AA.
AC A0A1S3F925;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Protein max {ECO:0000256|ARBA:ARBA00017633};
DE AltName: Full=Myc-associated factor X {ECO:0000256|ARBA:ARBA00029944};
GN Name=Max {ECO:0000313|RefSeq:XP_012872554.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012872554.1};
RN [1] {ECO:0000313|RefSeq:XP_012872554.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012872554.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the MAX family. {ECO:0000256|ARBA:ARBA00007628}.
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DR RefSeq; XP_012872554.1; XM_013017100.1.
DR AlphaFoldDB; A0A1S3F925; -.
DR STRING; 10020.ENSDORP00000018722; -.
DR GeneID; 105986278; -.
DR KEGG; dord:105986278; -.
DR CTD; 4149; -.
DR InParanoid; A0A1S3F925; -.
DR OMA; YMDAHEL; -.
DR OrthoDB; 5398829at2759; -.
DR Proteomes; UP000081671; Unplaced.
DR GO; GO:0000785; C:chromatin; IEA:Ensembl.
DR GO; GO:0070443; C:Mad-Max complex; IEA:Ensembl.
DR GO; GO:0071339; C:MLL1 complex; IEA:Ensembl.
DR GO; GO:0071943; C:Myc-Max complex; IEA:Ensembl.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IEA:Ensembl.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0070888; F:E-box binding; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR CDD; cd11406; bHLHzip_Max; 1.
DR Gene3D; 4.10.280.10; Helix-loop-helix DNA-binding domain; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR PANTHER; PTHR10328:SF3; PROTEIN MAX; 1.
DR PANTHER; PTHR10328; PROTEIN MAX MYC-ASSOCIATED FACTOR X; 1.
DR Pfam; PF00010; HLH; 1.
DR SMART; SM00353; HLH; 1.
DR SUPFAM; SSF47459; HLH, helix-loop-helix DNA-binding domain; 1.
DR PROSITE; PS50888; BHLH; 1.
PE 3: Inferred from homology;
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000081671};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 23..74
FT /note="BHLH"
FT /evidence="ECO:0000259|PROSITE:PS50888"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 103..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..45
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 160 AA; 18265 MW; EB10F31374D46A50 CRC64;
MSDNDDIEVE SDEEQPRFQS AADKRAHHNA LERKRRDHIK DSFHSLRDSV PSLQGEKASR
AQILDKATEY IQYMRRKNHT HQQDIDDLKR QNALLEQQVR ALEKARSSAQ LQTNYSSSDN
SLYTNAKGST ISAFDGGSDS SSESEPEEPQ SRKKLRMEAS
//
