MAX_DANRE
ID MAX_DANRE Reviewed; 165 AA.
AC P52161;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Protein max;
DE AltName: Full=Myc-associated factor X;
GN Name=max;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT), TISSUE SPECIFICITY,
RP AND DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RX PubMed=8474440; DOI=10.1128/mcb.13.5.2765-2775.1993;
RA Schreiber-Agus N., Horner J., Torres R., Chiu F.-C., DePinho R.A.;
RT "Zebra fish myc family and max genes: differential expression and oncogenic
RT activity throughout vertebrate evolution.";
RL Mol. Cell. Biol. 13:2765-2775(1993).
CC -!- FUNCTION: Transcription regulator. Forms a sequence-specific DNA-
CC binding protein complex with MYC or MAD which recognizes the core
CC sequence 5'-CAC[GA]TG-3'. The MYC-MAX complex is a transcriptional
CC activator, whereas the MAD-MAX complex is a repressor (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC protein. Binds DNA as a heterodimer with MYC or MAD. Component of some
CC MLL1/MLL complex (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=P52161-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=P52161-2; Sequence=VSP_002121;
CC -!- TISSUE SPECIFICITY: High levels are seen in the kidney, gills and
CC uterus. It is also found in the brain and heart.
CC {ECO:0000269|PubMed:8474440}.
CC -!- DEVELOPMENTAL STAGE: Expressed at relatively constant levels up to the
CC end of the embryonic stage (72 hours), with a moderate decrease between
CC the 12 and 24 hours stages marked by the formation of somites and organ
CC rudiments. {ECO:0000269|PubMed:8474440}.
CC -!- PTM: Phosphorylated. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the MAX family. {ECO:0000305}.
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DR EMBL; L11711; AAA02483.1; -; mRNA.
DR PIR; B48059; B48059.
DR PIR; C48059; C48059.
DR AlphaFoldDB; P52161; -.
DR SMR; P52161; -.
DR STRING; 7955.ENSDARP00000044461; -.
DR PaxDb; P52161; -.
DR ZFIN; ZDB-GENE-990415-152; max.
DR eggNOG; KOG2483; Eukaryota.
DR InParanoid; P52161; -.
DR PhylomeDB; P52161; -.
DR Reactome; R-DRE-8953750; Transcriptional Regulation by E2F6.
DR PRO; PR:P52161; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0071339; C:MLL1 complex; ISS:UniProtKB.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IBA:GO_Central.
DR GO; GO:0071141; C:SMAD protein complex; IPI:ZFIN.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IEA:InterPro.
DR GO; GO:0048264; P:determination of ventral identity; IMP:ZFIN.
DR GO; GO:0009953; P:dorsal/ventral pattern formation; IDA:ZFIN.
DR GO; GO:0030097; P:hemopoiesis; IMP:ZFIN.
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 PANTHER; PTHR10328; PTHR10328; 1.
DR Pfam; PF00010; HLH; 1.
DR SMART; SM00353; HLH; 1.
DR SUPFAM; SSF47459; SSF47459; 1.
DR PROSITE; PS50888; BHLH; 1.
PE 2: Evidence at transcript level;
KW Activator; Alternative splicing; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..165
FT /note="Protein max"
FT /id="PRO_0000127273"
FT DOMAIN 23..79
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 47..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 86..107
FT /note="Leucine-zipper"
FT REGION 119..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..165
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 13..21
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:8474440"
FT /id="VSP_002121"
SQ SEQUENCE 165 AA; 18728 MW; 227A31C7C415821A CRC64;
MSDNDDIEVD SDADSPRFHG VADKRAHHNA LERKRRDHIK DSFHSLRDSV PALQGEKQSI
KQASRAQILD KATEYIQYMR RKNHTHQQDI DDLKRQNALL EQQVRALEKV KGTTQLQANY
SSSDSSLYTN PKGQAVSAFD GGSDSSSGSE PEEQRTRKKH RPEDS
