GATA1_CHICK
ID GATA1_CHICK Reviewed; 304 AA.
AC P17678;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Erythroid transcription factor;
DE AltName: Full=Eryf1;
DE AltName: Full=GATA-binding factor 1;
DE Short=GATA-1;
DE AltName: Full=NF-E1 DNA-binding protein;
DE Short=NF-E1a;
GN Name=GATA1; Synonyms=ERYF1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2776214; DOI=10.1016/0092-8674(89)90940-9;
RA Evans T., Felsenfeld G.;
RT "The erythroid-specific transcription factor Eryf1: a new finger protein.";
RL Cell 58:877-885(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2249770; DOI=10.1101/gad.4.10.1650;
RA Yamamoto M., Ko L.J., Leonard M.W., Beug H., Orkin S.H., Engel J.D.;
RT "Activity and tissue-specific expression of the transcription factor NF-E1
RT multigene family.";
RL Genes Dev. 4:1650-1662(1990).
RN [3]
RP INTERACTION WITH EP300, ACETYLATION AT LYS-151; LYS-152; LYS-158; LYS-214;
RP LYS-218 AND LYS-220, AND MUTAGENESIS OF 151-LYS-LYS-152 AND LYS-158.
RX PubMed=9859997; DOI=10.1038/25166;
RA Boyes J., Byfield P., Nakatani Y., Ogryzko V.;
RT "Regulation of activity of the transcription factor GATA-1 by
RT acetylation.";
RL Nature 396:594-598(1998).
RN [4]
RP STRUCTURE BY NMR OF 158-223.
RX PubMed=8332909; DOI=10.1126/science.8332909;
RA Omichinski J.G., Clore G.M., Schaad O., Felsenfeld G., Trainor C.,
RA Appella E., Stahl S.J., Gronenborn A.M.;
RT "NMR structure of a specific DNA complex of Zn-containing DNA binding
RT domain of GATA-1.";
RL Science 261:438-446(1993).
RN [5]
RP STRUCTURE BY NMR OF 158-223.
RX PubMed=9303001; DOI=10.1038/nsb0997-732;
RA Tjandra N., Omichinski J.G., Gronenborn A.M., Clore G.M., Bax A.;
RT "Use of dipolar 1H-15N and 1H-13C couplings in the structure determination
RT of magnetically oriented macromolecules in solution.";
RL Nat. Struct. Biol. 4:732-738(1997).
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.
CC -!- SUBUNIT: Interacts with EP300; the interaction enhances transcriptional
CC activity as a direct result of acetylation.
CC {ECO:0000269|PubMed:9859997}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Erythrocytes.
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: Acetylated on Lys-158, Lys-214, Lys-218 and Lys-220 by EP300.
CC Acetylation increases DNA binding and stimulates transcriptional
CC activity. {ECO:0000269|PubMed:9859997}.
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DR EMBL; M26209; AAA49055.1; -; mRNA.
DR PIR; A32993; A32993.
DR RefSeq; NP_990795.1; NM_205464.1.
DR PDB; 1GAT; NMR; -; A=158-217.
DR PDB; 1GAU; NMR; -; A=158-217.
DR PDB; 2GAT; NMR; -; A=158-223.
DR PDB; 3GAT; NMR; -; A=158-223.
DR PDBsum; 1GAT; -.
DR PDBsum; 1GAU; -.
DR PDBsum; 2GAT; -.
DR PDBsum; 3GAT; -.
DR AlphaFoldDB; P17678; -.
DR SMR; P17678; -.
DR BioGRID; 676699; 3.
DR iPTMnet; P17678; -.
DR GeneID; 107050548; -.
DR CTD; 2623; -.
DR VEuPathDB; HostDB:geneid_416018; -.
DR InParanoid; P17678; -.
DR OrthoDB; 807790at2759; -.
DR EvolutionaryTrace; P17678; -.
DR PRO; PR:P17678; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0001223; F:transcription coactivator binding; IPI:BHF-UCL.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045165; P:cell fate commitment; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd00202; ZnF_GATA; 2.
DR Gene3D; 3.30.50.10; -; 2.
DR InterPro; IPR039355; Transcription_factor_GATA.
DR InterPro; IPR000679; Znf_GATA.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR PANTHER; PTHR10071; PTHR10071; 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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..304
FT /note="Erythroid transcription factor"
FT /id="PRO_0000083400"
FT ZN_FING 110..134
FT /note="GATA-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00094"
FT ZN_FING 164..188
FT /note="GATA-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00094"
FT REGION 77..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..100
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..260
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 151
FT /note="N6-acetyllysine; by EP300"
FT /evidence="ECO:0000305|PubMed:9859997"
FT MOD_RES 152
FT /note="N6-acetyllysine; by EP300"
FT /evidence="ECO:0000305|PubMed:9859997"
FT MOD_RES 158
FT /note="N6-acetyllysine; by EP300"
FT /evidence="ECO:0000269|PubMed:9859997"
FT MOD_RES 214
FT /note="N6-acetyllysine; by EP300"
FT /evidence="ECO:0000269|PubMed:9859997"
FT MOD_RES 218
FT /note="N6-acetyllysine; by EP300"
FT /evidence="ECO:0000269|PubMed:9859997"
FT MOD_RES 220
FT /note="N6-acetyllysine; by EP300"
FT /evidence="ECO:0000269|PubMed:9859997"
FT MUTAGEN 151..152
FT /note="KK->RR: Reduces acetylation and activation by
FT EP300."
FT /evidence="ECO:0000269|PubMed:9859997"
FT MUTAGEN 158
FT /note="K->R: Reduces acetylation and activation by EP300."
FT /evidence="ECO:0000269|PubMed:9859997"
FT TURN 165..167
FT /evidence="ECO:0007829|PDB:1GAT"
FT STRAND 173..178
FT /evidence="ECO:0007829|PDB:1GAT"
FT TURN 179..181
FT /evidence="ECO:0007829|PDB:1GAT"
FT STRAND 182..185
FT /evidence="ECO:0007829|PDB:1GAT"
FT HELIX 186..195
FT /evidence="ECO:0007829|PDB:1GAT"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:1GAT"
SQ SEQUENCE 304 AA; 31417 MW; 64C9D6FDB58CE83F CRC64;
MEFVALGGPD AGSPTPFPDE AGAFLGLGGG ERTEAGGLLA SYPPSGRVSL VPWADTGTLG
TPQWVPPATQ MEPPHYLELL QPPRGSPPHP SSGPLLPLSS GPPPCEAREC VNCGATATPL
WRRDGTGHYL CNACGLYHRL NGQNRPLIRP KKRLLVSKRA GTVCSNCQTS TTTLWRRSPM
GDPVCNACGL YYKLHQVNRP LTMRKDGIQT RNRKVSSKGK KRRPPGGGNP SATAGGGAPM
GGGGDPSMPP PPPPPAAAPP QSDALYALGP VVLSGHFLPF GNSGGFFGGG AGGYTAPPGL
SPQI
