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Database: UniProt
Entry: G3W825_SARHA
LinkDB: G3W825_SARHA
Original site: G3W825_SARHA 
ID   G3W825_SARHA            Unreviewed;       498 AA.
AC   G3W825;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   07-APR-2021, sequence version 2.
DT   27-MAR-2024, entry version 61.
DE   RecName: Full=Runt-related transcription factor {ECO:0000256|PIRNR:PIRNR009374};
GN   Name=RUNX2 {ECO:0000313|Ensembl:ENSSHAP00000011580.2};
OS   Sarcophilus harrisii (Tasmanian devil) (Sarcophilus laniarius).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Metatheria; Dasyuromorphia; Dasyuridae; Sarcophilus.
OX   NCBI_TaxID=9305 {ECO:0000313|Ensembl:ENSSHAP00000011580.2, ECO:0000313|Proteomes:UP000007648};
RN   [1] {ECO:0000313|Ensembl:ENSSHAP00000011580.2, ECO:0000313|Proteomes:UP000007648}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21709235; DOI=10.1073/pnas.1102838108;
RA   Miller W., Hayes V.M., Ratan A., Petersen D.C., Wittekindt N.E., Miller J.,
RA   Walenz B., Knight J., Qi J., Zhao F., Wang Q., Bedoya-Reina O.C.,
RA   Katiyar N., Tomsho L.P., Kasson L.M., Hardie R.A., Woodbridge P.,
RA   Tindall E.A., Bertelsen M.F., Dixon D., Pyecroft S., Helgen K.M.,
RA   Lesk A.M., Pringle T.H., Patterson N., Zhang Y., Kreiss A., Woods G.M.,
RA   Jones M.E., Schuster S.C.;
RT   "Genetic diversity and population structure of the endangered marsupial
RT   Sarcophilus harrisii (Tasmanian devil).";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:12348-12353(2011).
RN   [2] {ECO:0000313|Ensembl:ENSSHAP00000011580.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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   AlphaFoldDB; G3W825; -.
DR   STRING; 9305.ENSSHAP00000011580; -.
DR   Ensembl; ENSSHAT00000011676.2; ENSSHAP00000011580.2; ENSSHAG00000009950.2.
DR   eggNOG; KOG3982; Eukaryota.
DR   GeneTree; ENSGT00940000160171; -.
DR   InParanoid; G3W825; -.
DR   TreeFam; TF321496; -.
DR   Proteomes; UP000007648; Unassembled WGS sequence.
DR   GO; GO:0000785; C:chromatin; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005667; C:transcription regulator complex; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0043425; F:bHLH transcription factor binding; IEA:Ensembl.
DR   GO; GO:0031490; F:chromatin DNA binding; IEA:Ensembl.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
DR   GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:Ensembl.
DR   GO; GO:0030509; P:BMP signaling pathway; IEA:Ensembl.
DR   GO; GO:0030282; P:bone mineralization; IEA:Ensembl.
DR   GO; GO:0048469; P:cell maturation; IEA:Ensembl.
DR   GO; GO:0002063; P:chondrocyte development; IEA:Ensembl.
DR   GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; IEA:Ensembl.
DR   GO; GO:0035115; P:embryonic forelimb morphogenesis; IEA:Ensembl.
DR   GO; GO:0001958; P:endochondral ossification; IEA:Ensembl.
DR   GO; GO:0050673; P:epithelial cell proliferation; IEA:Ensembl.
DR   GO; GO:0010467; P:gene expression; IEA:Ensembl.
DR   GO; GO:0036076; P:ligamentous ossification; IEA:Ensembl.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; IEA:Ensembl.
DR   GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IEA:Ensembl.
DR   GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEA:Ensembl.
DR   GO; GO:0002076; P:osteoblast development; IEA:Ensembl.
DR   GO; GO:0002051; P:osteoblast fate commitment; IEA:Ensembl.
DR   GO; GO:0032332; P:positive regulation of chondrocyte differentiation; IEA:Ensembl.
DR   GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IEA:Ensembl.
DR   GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR   GO; GO:0045669; P:positive regulation of osteoblast differentiation; IEA:Ensembl.
DR   GO; GO:2000648; P:positive regulation of stem cell proliferation; IEA:Ensembl.
DR   GO; GO:0040036; P:regulation of fibroblast growth factor receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0042487; P:regulation of odontogenesis of dentin-containing tooth; IEA:Ensembl.
DR   GO; GO:0030278; P:regulation of ossification; IEA:Ensembl.
DR   GO; GO:1904383; P:response to sodium phosphate; IEA:Ensembl.
DR   GO; GO:0060395; P:SMAD protein signal transduction; IEA:Ensembl.
DR   GO; GO:0007224; P:smoothened signaling pathway; IEA:Ensembl.
DR   GO; GO:0048863; P:stem cell differentiation; IEA:Ensembl.
DR   GO; GO:0072089; P:stem cell proliferation; IEA:Ensembl.
DR   GO; GO:0030217; P:T cell differentiation; IEA:Ensembl.
DR   Gene3D; 2.60.40.720; -; 1.
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:SF7; RUNT-RELATED TRANSCRIPTION FACTOR 2; 1.
DR   Pfam; PF00853; Runt; 1.
DR   Pfam; PF08504; RunxI; 1.
DR   PIRSF; PIRSF009374; TF_Runt-rel_RUNX; 1.
DR   PRINTS; PR00967; ONCOGENEAML1.
DR   SUPFAM; SSF49417; p53-like transcription factors; 1.
DR   PROSITE; PS51062; RUNT; 1.
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:UP000007648};
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          89..217
FT                   /note="Runt"
FT                   /evidence="ECO:0000259|PROSITE:PS51062"
FT   REGION          21..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          209..316
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          436..498
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        209..230
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        252..316
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        446..489
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         151
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009374-1"
FT   BINDING         155
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009374-1"
FT   BINDING         178
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009374-1"
FT   BINDING         209
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009374-1"
SQ   SEQUENCE   498 AA;  53937 MW;  7F4B6289623EB60C CRC64;
     MASNSLFSTV TPCQQNFFWD PSTSRRFSPP SSSLQPGKMS DVSPVVAAQQ QQQQQRCGGG
     STAAAAAAAA AAAAAAAVPR LRPPHDNRTM VEIIADHPAE LVRTDSPNFL CSVLPSHWRC
     NKTLPVAFKV VALGEVPDGT VVTVMAGNDE NYSAELRNAS AVMKNQVARF NDLRFVGRSG
     RGKSFTLTIT VFTNPPQVAT YHRAIKVTVD GPREPRRHRQ KLDDSKPSLF SERLSDLGRI
     PHPGMRVGVP TQNPRPSLNS TPSPFNPQGQ SQIADPRQAQ SSPPWSYDQS YPSYLSQMTS
     PSIHSTTPLS STRGTGLPAI TDVPRRISDF FPHLLLQFLG ASELGPFSDP RQFTSISSLT
     ESRFSNPRMH YPATFTYTPP VTSGMSLGMS ATTHYHTYLP PPYPGSSQNQ SGPFQTSSTP
     YLYYGTSSGS YQFPMVPGGD RSPSRMLPPC TTTSNGSTLL NPNLPNQNDG VDADGSHSSS
     PTVLNSSGRM DESVWRPY
//
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