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Erythroid transcription factor (Eryf1) (GATA-binding factor 1) (GATA-1) (GF-1) (NF-E1 DNA-binding protein)

 GATA1_RAT               Reviewed;         413 AA.
P43429;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 1.
12-SEP-2018, entry version 146.
RecName: Full=Erythroid transcription factor;
AltName: Full=Eryf1;
AltName: Full=GATA-binding factor 1;
Short=GATA-1;
Short=GF-1;
AltName: Full=NF-E1 DNA-binding protein;
Name=Gata1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
STRAIN=Wistar; TISSUE=Fetal liver;
PubMed=7957872; DOI=10.1016/0014-5793(94)01062-5;
Matsuda K., Kobune Y., Noda C., Ichihara A.;
"Expression of GATA-binding transcription factors in rat
hepatocytes.";
FEBS Lett. 353:269-272(1994).
-!- FUNCTION: Transcriptional activator or repressor which probably
serves as a general switch factor for erythroid development. It
binds to DNA sites with the consensus sequence 5'-[AT]GATA[AG]-3'
within regulatory regions of globin genes and of other genes
expressed in erythroid cells. Activates the transcription of genes
involved in erythroid differentiation of K562 erythroleukemia
cells, including HBB, HBG1/2, ALAS2 and HMBS.
{ECO:0000250|UniProtKB:P15976}.
-!- SUBUNIT: Interacts (via the N-terminal zinc finger) with ZFPM1.
Interacts with GFI1B. Interacts with PIAS4; the interaction
enhances sumoylation and represses the transactivational activity
in a sumoylation-independent manner. Interacts with LMCD1.
Interacts with BRD3 (By similarity). Interacts with CREBBP; the
interaction stimulates acetylation and transcriptional activity in
vivo. Interacts with MED1, CCAR1 and CALCOCO1 (By similarity).
Interacts with EP300 (By similarity). Interacts with CEBPE (By
similarity). {ECO:0000250|UniProtKB:P15976,
ECO:0000250|UniProtKB:P17679}.
-!- SUBCELLULAR LOCATION: Nucleus.
-!- TISSUE SPECIFICITY: Erythrocytes, and fetal hepatocytes.
{ECO:0000269|PubMed:7957872}.
-!- DOMAIN: The two fingers are functionally distinct and cooperate to
achieve specific, stable DNA binding. The first finger is
necessary only for full specificity and stability of binding,
whereas the second one is required for binding (By similarity).
{ECO:0000250}.
-!- PTM: Highly phosphorylated on serine residues. Phosphorylation on
Ser-310 is enhanced on erythroid differentiation. Phosphorylation
on Ser-142 promotes sumoylation on Lys-137 (By similarity).
{ECO:0000250}.
-!- PTM: Sumoylation on Lys-137 is enhanced by phosphorylation on Ser-
142 and by interaction with PIAS4. Sumoylation with SUMO1 has no
effect on transcriptional activity (By similarity). {ECO:0000250}.
-!- PTM: Acetylated at 2 conserved lysine-rich motifs by CREBBP in
vitro. Acetylation does not affect DNA-binding in vitro but is
essential to induce erythroid differentiation and for binding
chromatin in vivo. Acetylated on Lys-233, Lys-245 Lys-246 by EP300
(By similarity). {ECO:0000250}.
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EMBL; D13518; BAA02735.1; -; mRNA.
PIR; S48756; S48756.
RefSeq; NP_036896.1; NM_012764.1.
RefSeq; XP_017457744.1; XM_017602255.1.
UniGene; Rn.10024; -.
ProteinModelPortal; P43429; -.
SMR; P43429; -.
STRING; 10116.ENSRNOP00000067336; -.
PhosphoSitePlus; P43429; -.
PaxDb; P43429; -.
PRIDE; P43429; -.
Ensembl; ENSRNOT00000029272; ENSRNOP00000038111; ENSRNOG00000025534.
Ensembl; ENSRNOT00000075082; ENSRNOP00000067336; ENSRNOG00000047663.
GeneID; 108348091; -.
GeneID; 25172; -.
KEGG; rno:108348091; -.
KEGG; rno:25172; -.
UCSC; RGD:2663; rat.
CTD; 2623; -.
RGD; 2663; Gata1.
eggNOG; KOG1601; Eukaryota.
eggNOG; COG5641; LUCA.
GeneTree; ENSGT00760000119221; -.
HOGENOM; HOG000047701; -.
HOVERGEN; HBG051705; -.
InParanoid; P43429; -.
KO; K09182; -.
OMA; TLKTERM; -.
OrthoDB; EOG091G0AUR; -.
PhylomeDB; P43429; -.
TreeFam; TF315391; -.
Reactome; R-RNO-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
Reactome; R-RNO-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
Reactome; R-RNO-983231; Factors involved in megakaryocyte development and platelet production.
PRO; PR:P43429; -.
Proteomes; UP000002494; Chromosome X.
Bgee; ENSRNOG00000025534; Expressed in 4 organ(s), highest expression level in spleen.
Genevisible; P43429; RN.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0005667; C:transcription factor complex; IBA:GO_Central.
GO; GO:0003682; F:chromatin binding; IDA:RGD.
GO; GO:0031490; F:chromatin DNA binding; ISS:UniProtKB.
GO; GO:0003677; F:DNA binding; IDA:RGD.
GO; GO:0000980; F:RNA polymerase II distal enhancer sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IBA:GO_Central.
GO; GO:0001085; F:RNA polymerase II transcription factor binding; IBA:GO_Central.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:RGD.
GO; GO:0001228; F:transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0031100; P:animal organ regeneration; IDA:RGD.
GO; GO:0030221; P:basophil differentiation; IEA:InterPro.
GO; GO:0071320; P:cellular response to cAMP; IEP:RGD.
GO; GO:0071372; P:cellular response to follicle-stimulating hormone stimulus; IEP:RGD.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:RGD.
GO; GO:0030222; P:eosinophil differentiation; IEA:InterPro.
GO; GO:0048821; P:erythrocyte development; IEA:InterPro.
GO; GO:0030219; P:megakaryocyte differentiation; IEA:InterPro.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IMP:RGD.
GO; GO:0043306; P:positive regulation of mast cell degranulation; IMP:RGD.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:RGD.
GO; GO:0060009; P:Sertoli cell development; IEP:RGD.
CDD; cd00202; ZnF_GATA; 2.
Gene3D; 3.30.50.10; -; 2.
InterPro; IPR029524; GATA-1.
InterPro; IPR039355; Transcription_factor_GATA.
InterPro; IPR000679; Znf_GATA.
InterPro; IPR013088; Znf_NHR/GATA.
PANTHER; PTHR10071; PTHR10071; 1.
PANTHER; PTHR10071:SF190; PTHR10071:SF190; 1.
Pfam; PF00320; GATA; 2.
PRINTS; PR00619; GATAZNFINGER.
SMART; SM00401; ZnF_GATA; 2.
PROSITE; PS00344; GATA_ZN_FINGER_1; 2.
PROSITE; PS50114; GATA_ZN_FINGER_2; 2.
2: Evidence at transcript level;
Acetylation; Activator; Complete proteome; DNA-binding;
Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
Reference proteome; Repeat; Repressor; Transcription;
Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 413 Erythroid transcription factor.
/FTId=PRO_0000083399.
ZN_FING 204 228 GATA-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00094}.
ZN_FING 258 282 GATA-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00094}.
REGION 200 330 Interaction with MED1 and CCAR1.
{ECO:0000250|UniProtKB:P15976}.
REGION 203 222 Required for interaction with ZFPM1.
{ECO:0000250}.
REGION 249 315 Interaction with CALCOCO1.
{ECO:0000250|UniProtKB:P15976}.
MOD_RES 26 26 Phosphoserine.
{ECO:0000250|UniProtKB:P17679}.
MOD_RES 49 49 Phosphoserine.
{ECO:0000250|UniProtKB:P17679}.
MOD_RES 72 72 Phosphoserine.
{ECO:0000250|UniProtKB:P17679}.
MOD_RES 142 142 Phosphoserine.
{ECO:0000250|UniProtKB:P15976}.
MOD_RES 178 178 Phosphoserine.
{ECO:0000250|UniProtKB:P17679}.
MOD_RES 187 187 Phosphoserine.
{ECO:0000250|UniProtKB:P17679}.
MOD_RES 233 233 N6-acetyllysine; by EP300.
{ECO:0000250|UniProtKB:P15976}.
MOD_RES 245 245 N6-acetyllysine; by EP300.
{ECO:0000250|UniProtKB:P15976}.
MOD_RES 246 246 N6-acetyllysine; by CREBBP.
{ECO:0000250|UniProtKB:P17679}.
MOD_RES 246 246 N6-acetyllysine; by EP300. {ECO:0000250}.
MOD_RES 252 252 N6-acetyllysine; by CREBBP.
{ECO:0000250|UniProtKB:P17679}.
MOD_RES 308 308 N6-acetyllysine.
{ECO:0000250|UniProtKB:P17679}.
MOD_RES 310 310 Phosphoserine.
{ECO:0000250|UniProtKB:P17679}.
MOD_RES 312 312 N6-acetyllysine; by CREBBP.
{ECO:0000250|UniProtKB:P17679}.
MOD_RES 314 314 N6-acetyllysine.
{ECO:0000250|UniProtKB:P17679}.
MOD_RES 315 315 N6-acetyllysine.
{ECO:0000250|UniProtKB:P17679}.
CROSSLNK 137 137 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250}.
SEQUENCE 413 AA; 42871 MW; 9BE4120FCF8269BB CRC64;
MDFPGLGALG TSEPLPQFVD SALVSSTSDS AGFFSSGPES LDTASSSTSP NAATAAATAL
AYYREAEAYR HSPVFQVYPL LNSMEGIPGS SPYASWAYSK TALYPASTVC PSHEDAPSQT
LEDPDGKNNN TFLETLKTER LSPDLLTLGT ALPTSLPVTS SAYGGADFPS PFFSPTGSPL
SSAAYSSPKF HGSLPLAPCE ARECVNCGAT ATPLWRRDRT GHYLCNACGL YHKMNGQNRP
LIRPKKRMIV SKRAGTQCTN CQTTTTTLWR RNASGDPVCN ACGLYYKLHQ VNRPLTMRKD
GIQTRNRKAS GKGKKKRGSS LAGAGAAEGP AGGFMVVAGG SSSGNCGEVA PGLTLGTAGT
AHLYQGLGPV VLSGPVSHLM SFPGPLLGSP TASFPTGPVP TTTSTSVVSP LSS


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