ID   RUNX1_XENLA             Reviewed;         462 AA.
AC   Q6PF39; O73725;
DT   23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 2.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Runt-related transcription factor 1 {ECO:0000250|UniProtKB:Q01196};
DE   AltName: Full=Acute myeloid leukemia 1 protein {ECO:0000303|PubMed:9502719};
DE            Short=XAML {ECO:0000312|EMBL:AAC41269.1};
DE   AltName: Full=Core-binding factor subunit alpha-2 {ECO:0000303|PubMed:9502719};
DE            Short=CBF-alpha-2 {ECO:0000303|PubMed:11105897, ECO:0000303|PubMed:9502719};
GN   Name=runx1 {ECO:0000250|UniProtKB:Q01196};
GN   Synonyms=aml {ECO:0000312|EMBL:AAC41269.1},
GN   cbfa2 {ECO:0000303|PubMed:9502719};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAC41269.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
RP   DEVELOPMENTAL STAGE, AND INDUCTION.
RC   TISSUE=Neurula {ECO:0000269|PubMed:9502719};
RX   PubMed=9502719; DOI=10.1242/dev.125.8.1371;
RA   Tracey W.D.T. Jr., Pepling M.E., Horb M.E., Thomsen G.H., Gergen J.P.;
RT   "A Xenopus homologue of aml-1 reveals unexpected patterning mechanisms
RT   leading to the formation of embryonic blood.";
RL   Development 125:1371-1380(1998).
RN   [2] {ECO:0000312|EMBL:AAH57739.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Spleen {ECO:0000312|EMBL:AAH57739.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000305}
RP   INDUCTION.
RX   PubMed=17942750; DOI=10.1182/blood-2007-03-081323;
RA   Walmsley M., Cleaver D., Patient R.K.;
RT   "Fibroblast growth factor controls the timing of Scl, Lmo2, and Runx1
RT   expression during embryonic blood development.";
RL   Blood 111:1157-1166(2008).
RN   [4] {ECO:0000305}
RP   REVIEW.
RX   PubMed=11105897; DOI=10.1006/scdb.2000.0186;
RA   Tracey W.D.T. Jr., Speck N.A.;
RT   "Potential roles for RUNX1 and its orthologs in determining hematopoietic
RT   cell fate.";
RL   Semin. Cell Dev. Biol. 11:337-342(2000).
CC   -!- FUNCTION: Involved in primitive hematopoiesis in the embryo.
CC       {ECO:0000269|PubMed:9502719}.
CC   -!- SUBUNIT: Heterodimer with cbfb. runx1 binds DNA as a monomer and
CC       through the Runt domain. DNA-binding is increased by heterodimerization
CC       (By similarity). {ECO:0000250|UniProtKB:Q01196}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q01196,
CC       ECO:0000255|PROSITE-ProRule:PRU00399}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1 {ECO:0000269|PubMed:9502719};
CC         IsoId=Q6PF39-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6PF39-2; Sequence=VSP_052947;
CC   -!- TISSUE SPECIFICITY: Shows a complex and dynamic expression pattern. In
CC       stage 14-24 embryos, expressed in a subset of neuroblasts in the
CC       lateral stripe of the neural plate. In late neurula stages, expression
CC       begins in the olfactory placodes. Also expressed in structures that
CC       play a role in blood formation: at stage 14, expressed on the anterior
CC       ventral side of the embryo in the anterior endomesoderm. As the embryo
CC       elongates, expression shifts gradually to a V-shaped expression pattern
CC       in the presumptive ventral blood island. {ECO:0000269|PubMed:9502719}.
CC   -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically. Shows a
CC       small amount of maternal expression. Zygotic expression begins at stage
CC       8 and steadily increases after this point.
CC       {ECO:0000269|PubMed:9502719}.
CC   -!- INDUCTION: By low levels of the dorsalizing factor LiCl. Inhibited by
CC       high doses of LiCl. In order to temporally control hematopoiesis, fgf-
CC       signaling inhibits expression in posterior regions of the embryo by
CC       antagonizing bmp-signaling. {ECO:0000269|PubMed:17942750,
CC       ECO:0000269|PubMed:9502719}.
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DR   EMBL; AF035446; AAC41269.1; -; mRNA.
DR   EMBL; BC057739; AAH57739.1; -; mRNA.
DR   RefSeq; NP_001079966.1; NM_001086497.1. [Q6PF39-2]
DR   RefSeq; XP_018100278.1; XM_018244789.1. [Q6PF39-2]
DR   AlphaFoldDB; Q6PF39; -.
DR   SMR; Q6PF39; -.
DR   ELM; Q6PF39; -.
DR   DNASU; 379657; -.
DR   GeneID; 379657; -.
DR   KEGG; xla:379657; -.
DR   CTD; 379657; -.
DR   Xenbase; XB-GENE-864949; runx1.L.
DR   OMA; YLENTHT; -.
DR   OrthoDB; 562214at2759; -.
DR   Proteomes; UP000186698; Chromosome 2L.
DR   Bgee; 379657; Expressed in spleen and 15 other tissues.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
DR   GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR   GO; GO:0043565; F:sequence-specific 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   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   Gene3D; 2.60.40.720; -; 1.
DR   Gene3D; 4.10.770.10; -; 1.
DR   InterPro; IPR000040; AML1_Runt.
DR   InterPro; IPR008967; p53-like_TF_DNA-bd.
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; PTHR11950; 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; SSF49417; 1.
DR   PROSITE; PS51062; RUNT; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Chloride; Developmental protein; DNA-binding;
KW   Nucleus; Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..462
FT                   /note="Runt-related transcription factor 1"
FT                   /id="PRO_0000351207"
FT   DOMAIN          50..178
FT                   /note="Runt"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00399"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          80..84
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000250|UniProtKB:Q01196"
FT   REGION          135..143
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000250|UniProtKB:Q01196"
FT   REGION          168..177
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000250|UniProtKB:Q01196"
FT   REGION          399..462
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..25
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        412..451
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         112
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q01196,
FT                   ECO:0000255|PROSITE-ProRule:PRU00399"
FT   BINDING         116
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q01196,
FT                   ECO:0000255|PROSITE-ProRule:PRU00399"
FT   BINDING         139
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q01196,
FT                   ECO:0000255|PROSITE-ProRule:PRU00399"
FT   BINDING         170
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q01196,
FT                   ECO:0000255|PROSITE-ProRule:PRU00399"
FT   VAR_SEQ         1..5
FT                   /note="MRIPV -> MASHSAFQSFPLYPPCFFR (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.2"
FT                   /id="VSP_052947"
FT   CONFLICT        74
FT                   /note="V -> L (in Ref. 1; AAC41269)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        195
FT                   /note="S -> P (in Ref. 1; AAC41269)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   462 AA;  50369 MW;  E6A38D9B8ED07B3A CRC64;
     MRIPVDTSTS RRFTPPSTTL SPGKMSEPIP LNIADSSAAL VGKLRSTDRN MVEVLSDHPG
     ELVRTDSPNF LCSVLPTHWR CNKTLPIAFK VVALGEVPDG TLVTVMAGND ENYSAELRNA
     TAAMKSQVAR FNDLRFVGRS GRGKSFTLTI TVFTNPPQVA TYHRAIKITV DGPREPRRHR
     QKLDEQTKPG NLSFSERLSE LEHFRRTAMR VSPHHPNPMP NPRATLNHSA AFNPQPQGQI
     QVADTRQVQA SPPWSYDQSY QYLGSIATQS VHPATPISPG RASSMTSLSA ELSSRLSGAS
     DLTAFSDPRV GIDRQFSTLP SISDPRMHYP GAFTYTPTPV TSGIGIGMSA MTSATRYHTY
     LPPPYPGSSQ AQSNPFQTSS PSYHLYYGTS AGSYHQFSMM SGGERSPPRI LPPCTNASTG
     STLLNPNLPN QSDVVEAEGS HSNSPTNMGS TPRLEEAVWR PY