ID G5AM15_HETGA Unreviewed; 498 AA.
AC G5AM15;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=Runt-related transcription factor {ECO:0000256|PIRNR:PIRNR009374};
GN ORFNames=GW7_16276 {ECO:0000313|EMBL:EHA98075.1};
OS Heterocephalus glaber (Naked mole rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Heterocephalus.
OX NCBI_TaxID=10181 {ECO:0000313|EMBL:EHA98075.1, ECO:0000313|Proteomes:UP000006813};
RN [1] {ECO:0000313|EMBL:EHA98075.1, ECO:0000313|Proteomes:UP000006813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993625; DOI=10.1038/nature10533;
RA Kim E.B., Fang X., Fushan A.A., Huang Z., Lobanov A.V., Han L.,
RA Marino S.M., Sun X., Turanov A.A., Yang P., Yim S.H., Zhao X.,
RA Kasaikina M.V., Stoletzki N., Peng C., Polak P., Xiong Z., Kiezun A.,
RA Zhu Y., Chen Y., Kryukov G.V., Zhang Q., Peshkin L., Yang L., Bronson R.T.,
RA Buffenstein R., Wang B., Han C., Li Q., Chen L., Zhao W., Sunyaev S.R.,
RA Park T.J., Zhang G., Wang J., Gladyshev V.N.;
RT "Genome sequencing reveals insights into physiology and longevity of the
RT naked mole rat.";
RL Nature 479:223-227(2011).
CC -!- FUNCTION: Forms the heterodimeric complex core-binding factor (CBF)
CC with CBFB. RUNX members modulate the transcription of their target
CC genes through recognizing the core consensus binding sequence 5'-
CC TGTGGT-3', or very rarely, 5'-TGCGGT-3', within their regulatory
CC regions via their runt domain, while CBFB is a non-DNA-binding
CC regulatory subunit that allosterically enhances the sequence-specific
CC DNA-binding capacity of RUNX. {ECO:0000256|PIRNR:PIRNR009374}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PIRNR:PIRNR009374}.
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DR EMBL; JH165919; EHA98075.1; -; Genomic_DNA.
DR AlphaFoldDB; G5AM15; -.
DR STRING; 10181.G5AM15; -.
DR eggNOG; KOG3982; Eukaryota.
DR InParanoid; G5AM15; -.
DR Proteomes; UP000006813; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IEA:UniProt.
DR GO; GO:0051094; P:positive regulation of developmental process; IEA:UniProt.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:UniProt.
DR Gene3D; 2.60.40.720; -; 2.
DR InterPro; IPR000040; AML1_Runt.
DR InterPro; IPR008967; p53-like_TF_DNA-bd_sf.
DR InterPro; IPR012346; p53/RUNT-type_TF_DNA-bd_sf.
DR InterPro; IPR013524; Runt_dom.
DR InterPro; IPR027384; Runx_central_dom_sf.
DR InterPro; IPR013711; RunxI_C_dom.
DR InterPro; IPR016554; TF_Runt-rel_RUNX.
DR PANTHER; PTHR11950; RUNT RELATED; 1.
DR PANTHER; PTHR11950:SF40; RUNT-RELATED TRANSCRIPTION FACTOR 1; 1.
DR Pfam; PF00853; Runt; 2.
DR Pfam; PF08504; RunxI; 1.
DR PIRSF; PIRSF009374; TF_Runt-rel_RUNX; 2.
DR PRINTS; PR00967; ONCOGENEAML1.
DR SUPFAM; SSF49417; p53-like transcription factors; 2.
DR PROSITE; PS51062; RUNT; 2.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PIRNR:PIRNR009374};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000006813};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|PIRNR:PIRNR009374};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW ECO:0000256|PIRNR:PIRNR009374}.
FT DOMAIN 26..154
FT /note="Runt"
FT /evidence="ECO:0000259|PROSITE:PS51062"
FT DOMAIN 190..225
FT /note="Runt"
FT /evidence="ECO:0000259|PROSITE:PS51062"
FT REGION 217..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 445..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..233
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..485
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 88
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR009374-1"
FT BINDING 92
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR009374-1"
FT BINDING 115
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR009374-1"
FT BINDING 217
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR009374-1"
SQ SEQUENCE 498 AA; 53668 MW; D498D78F18412830 CRC64;
MSEAVPLGAP DAGAALAGKL RSGDRSMVEV LADHPGELVR TDSPNFLCSV LPTHWRCNKT
LPIAFKVVAL GEVPDGTLVT VMAGNDENYS AELRNATAAM KNQVARFNDL RFVGRSGRVS
PWDSSSSQIR RRGGQFYVRP FMTAGTQQHR ILAEQSRLPH PDSGSFYGSA TVAALDRIAG
ILAAALEAFG KSFTLTITVF TNPPQVATYH RAIKITVDGP REPRRHRQKL DDQTKPGSLS
FSERLSELEQ LRRTAMRVSP HHPAPTPNPR VNHSTAFNPQ PQSQMQDTRQ IQPSPPWSYD
QSYQYLGSIT TPSVHPATPI SPGRASGMTS LSAELSSRLS TAPDLAAFGD PRQFPALPSI
SDPRMHYPGA FTYSPTPVTS GIGIGMSAMS SASRYHTYLP PPYPGSSQAQ GGPFQASSPS
YHLYYGASAG SYQFSMVGGE RSPPRILPPC TNASTGSALL NPSLPNQSDV VEAEGSHSNS
PTNMAPAARL EEAVWRPY
//
