GATA1_RAT
ID GATA1_RAT Reviewed; 413 AA.
AC P43429;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Erythroid transcription factor;
DE AltName: Full=Eryf1;
DE AltName: Full=GATA-binding factor 1;
DE Short=GATA-1;
DE Short=GF-1;
DE AltName: Full=NF-E1 DNA-binding protein;
GN Name=Gata1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=Wistar; TISSUE=Fetal liver;
RX PubMed=7957872; DOI=10.1016/0014-5793(94)01062-5;
RA Matsuda K., Kobune Y., Noda C., Ichihara A.;
RT "Expression of GATA-binding transcription factors in rat hepatocytes.";
RL FEBS Lett. 353:269-272(1994).
CC -!- FUNCTION: Transcriptional activator or repressor which probably serves
CC as a general switch factor for erythroid development. It binds to DNA
CC sites with the consensus sequence 5'-[AT]GATA[AG]-3' within regulatory
CC regions of globin genes and of other genes expressed in erythroid
CC cells. Activates the transcription of genes involved in erythroid
CC differentiation of K562 erythroleukemia cells, including HBB, HBG1/2,
CC ALAS2 and HMBS. {ECO:0000250|UniProtKB:P15976}.
CC -!- SUBUNIT: Interacts (via the N-terminal zinc finger) with ZFPM1.
CC Interacts with GFI1B. Interacts with PIAS4; the interaction enhances
CC sumoylation and represses the transactivational activity in a
CC sumoylation-independent manner. Interacts with LMCD1. Interacts with
CC BRD3 (By similarity). Interacts with CREBBP; the interaction stimulates
CC acetylation and transcriptional activity in vivo. Interacts with MED1,
CC CCAR1 and CALCOCO1 (By similarity). Interacts with EP300 (By
CC similarity). Interacts with CEBPE (By similarity).
CC {ECO:0000250|UniProtKB:P15976, ECO:0000250|UniProtKB:P17679}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Erythrocytes, and fetal hepatocytes.
CC {ECO:0000269|PubMed:7957872}.
CC -!- DOMAIN: The two fingers are functionally distinct and cooperate to
CC achieve specific, stable DNA binding. The first finger is necessary
CC only for full specificity and stability of binding, whereas the second
CC one is required for binding (By similarity). {ECO:0000250}.
CC -!- PTM: Highly phosphorylated on serine residues. Phosphorylation on Ser-
CC 310 is enhanced on erythroid differentiation. Phosphorylation on Ser-
CC 142 promotes sumoylation on Lys-137 (By similarity). {ECO:0000250}.
CC -!- PTM: Sumoylation on Lys-137 is enhanced by phosphorylation on Ser-142
CC and by interaction with PIAS4. Sumoylation with SUMO1 has no effect on
CC transcriptional activity (By similarity). {ECO:0000250}.
CC -!- PTM: Acetylated at 2 conserved lysine-rich motifs by CREBBP in vitro.
CC Acetylation does not affect DNA-binding in vitro but is essential to
CC induce erythroid differentiation and for binding chromatin in vivo.
CC Acetylated on Lys-233, Lys-245 Lys-246 by EP300 (By similarity).
CC {ECO:0000250}.
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DR EMBL; D13518; BAA02735.1; -; mRNA.
DR PIR; S48756; S48756.
DR RefSeq; NP_036896.1; NM_012764.1.
DR RefSeq; XP_017457744.1; XM_017602255.1.
DR AlphaFoldDB; P43429; -.
DR SMR; P43429; -.
DR STRING; 10116.ENSRNOP00000038111; -.
DR PhosphoSitePlus; P43429; -.
DR PaxDb; P43429; -.
DR Ensembl; ENSRNOT00000075082; ENSRNOP00000067336; ENSRNOG00000047663.
DR GeneID; 25172; -.
DR KEGG; rno:25172; -.
DR UCSC; RGD:2663; rat.
DR CTD; 2623; -.
DR RGD; 2663; Gata1.
DR eggNOG; KOG1601; Eukaryota.
DR GeneTree; ENSGT00940000161156; -.
DR HOGENOM; CLU_027524_1_1_1; -.
DR InParanoid; P43429; -.
DR OMA; YSKTGLY; -.
DR OrthoDB; 807790at2759; -.
DR PhylomeDB; P43429; -.
DR TreeFam; TF315391; -.
DR Reactome; R-RNO-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR Reactome; R-RNO-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR Reactome; R-RNO-983231; Factors involved in megakaryocyte development and platelet production.
DR PRO; PR:P43429; -.
DR Proteomes; UP000002494; Chromosome X.
DR Bgee; ENSRNOG00000025534; Expressed in spleen and 3 other tissues.
DR Genevisible; P43429; RN.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0032993; C:protein-DNA complex; ISO:RGD.
DR GO; GO:0005667; C:transcription regulator complex; ISO:RGD.
DR GO; GO:0017053; C:transcription repressor complex; ISO:RGD.
DR GO; GO:0070742; F:C2H2 zinc finger domain binding; ISO:RGD.
DR GO; GO:0003682; F:chromatin binding; IDA:RGD.
DR GO; GO:0031490; F:chromatin DNA binding; ISS:UniProtKB.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0003677; F:DNA binding; IDA:RGD.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:RGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0002039; F:p53 binding; ISO:RGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:RGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:RGD.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:RGD.
DR GO; GO:0001223; F:transcription coactivator binding; ISO:RGD.
DR GO; GO:0001221; F:transcription coregulator binding; ISO:RGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0031100; P:animal organ regeneration; IDA:RGD.
DR GO; GO:0030221; P:basophil differentiation; ISO:RGD.
DR GO; GO:0030282; P:bone mineralization; IEA:Ensembl.
DR GO; GO:0048468; P:cell development; ISO:RGD.
DR GO; GO:0045165; P:cell fate commitment; IBA:GO_Central.
DR GO; GO:0007267; P:cell-cell signaling; ISO:RGD.
DR GO; GO:0071320; P:cellular response to cAMP; IEP:RGD.
DR GO; GO:0071372; P:cellular response to follicle-stimulating hormone stimulus; IEP:RGD.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:RGD.
DR GO; GO:0097067; P:cellular response to thyroid hormone stimulus; ISO:RGD.
DR GO; GO:0097028; P:dendritic cell differentiation; ISO:RGD.
DR GO; GO:0035162; P:embryonic hemopoiesis; ISO:RGD.
DR GO; GO:0030222; P:eosinophil differentiation; ISO:RGD.
DR GO; GO:0035854; P:eosinophil fate commitment; ISO:RGD.
DR GO; GO:0048821; P:erythrocyte development; ISO:RGD.
DR GO; GO:0030218; P:erythrocyte differentiation; ISO:RGD.
DR GO; GO:0048873; P:homeostasis of number of cells within a tissue; ISO:RGD.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0008584; P:male gonad development; ISO:RGD.
DR GO; GO:0030219; P:megakaryocyte differentiation; ISO:RGD.
DR GO; GO:0033028; P:myeloid cell apoptotic process; IEA:Ensembl.
DR GO; GO:0030099; P:myeloid cell differentiation; ISO:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
DR GO; GO:0030502; P:negative regulation of bone mineralization; ISO:RGD.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:RGD.
DR GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; ISO:RGD.
DR GO; GO:0033033; P:negative regulation of myeloid cell apoptotic process; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:2000678; P:negative regulation of transcription regulatory region DNA binding; ISO:RGD.
DR GO; GO:0033687; P:osteoblast proliferation; IEA:Ensembl.
DR GO; GO:0070527; P:platelet aggregation; ISO:RGD.
DR GO; GO:0030220; P:platelet formation; ISO:RGD.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IMP:RGD.
DR GO; GO:0045648; P:positive regulation of erythrocyte differentiation; ISO:RGD.
DR GO; GO:0043306; P:positive regulation of mast cell degranulation; IMP:RGD.
DR GO; GO:0033690; P:positive regulation of osteoblast proliferation; ISO:RGD.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0060319; P:primitive erythrocyte differentiation; IEA:Ensembl.
DR GO; GO:0010724; P:regulation of definitive erythrocyte differentiation; ISO:RGD.
DR GO; GO:0010559; P:regulation of glycoprotein biosynthetic process; ISO:RGD.
DR GO; GO:0010725; P:regulation of primitive erythrocyte differentiation; ISO:RGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:RGD.
DR GO; GO:0060009; P:Sertoli cell development; IEP:RGD.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl.
DR CDD; cd00202; ZnF_GATA; 2.
DR Gene3D; 3.30.50.10; -; 2.
DR InterPro; IPR029524; GATA-1.
DR InterPro; IPR039355; Transcription_factor_GATA.
DR InterPro; IPR000679; Znf_GATA.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR PANTHER; PTHR10071; PTHR10071; 1.
DR PANTHER; PTHR10071:SF190; PTHR10071:SF190; 1.
DR Pfam; PF00320; GATA; 2.
DR PRINTS; PR00619; GATAZNFINGER.
DR SMART; SM00401; ZnF_GATA; 2.
DR PROSITE; PS00344; GATA_ZN_FINGER_1; 2.
DR PROSITE; PS50114; GATA_ZN_FINGER_2; 2.
PE 2: Evidence at transcript level;
KW Acetylation; Activator; DNA-binding; Isopeptide bond; Metal-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor;
KW Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..413
FT /note="Erythroid transcription factor"
FT /id="PRO_0000083399"
FT ZN_FING 204..228
FT /note="GATA-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00094"
FT ZN_FING 258..282
FT /note="GATA-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00094"
FT REGION 109..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..330
FT /note="Interaction with MED1 and CCAR1"
FT /evidence="ECO:0000250|UniProtKB:P15976"
FT REGION 203..222
FT /note="Required for interaction with ZFPM1"
FT /evidence="ECO:0000250"
FT REGION 249..315
FT /note="Interaction with CALCOCO1"
FT /evidence="ECO:0000250|UniProtKB:P15976"
FT REGION 297..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 391..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..413
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17679"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17679"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17679"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15976"
FT MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17679"
FT MOD_RES 187
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17679"
FT MOD_RES 233
FT /note="N6-acetyllysine; by EP300"
FT /evidence="ECO:0000250|UniProtKB:P15976"
FT MOD_RES 245
FT /note="N6-acetyllysine; by EP300"
FT /evidence="ECO:0000250|UniProtKB:P15976"
FT MOD_RES 246
FT /note="N6-acetyllysine; by CREBBP"
FT /evidence="ECO:0000250|UniProtKB:P17679"
FT MOD_RES 246
FT /note="N6-acetyllysine; by EP300"
FT /evidence="ECO:0000250"
FT MOD_RES 252
FT /note="N6-acetyllysine; by CREBBP"
FT /evidence="ECO:0000250|UniProtKB:P17679"
FT MOD_RES 308
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P17679"
FT MOD_RES 310
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17679"
FT MOD_RES 312
FT /note="N6-acetyllysine; by CREBBP"
FT /evidence="ECO:0000250|UniProtKB:P17679"
FT MOD_RES 314
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P17679"
FT MOD_RES 315
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P17679"
FT CROSSLNK 137
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
SQ 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
