GATA4_CANLF
ID GATA4_CANLF Reviewed; 442 AA.
AC Q0Q0E4;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Transcription factor GATA-4;
DE AltName: Full=GATA-binding factor 4;
GN Name=GATA4;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Hyun C., Lee S.-A., Lee S.-G.;
RT "Molecular screening of GATA4 gene in canine atrial septal defects.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transcriptional activator that binds to the consensus
CC sequence 5'-AGATAG-3' and plays a key role in cardiac development. In
CC cooperation with TBX5, it binds to cardiac super-enhancers and promotes
CC cardiomyocyte gene expression, while it down-regulates endocardial and
CC endothelial gene expression. Involved in bone morphogenetic protein
CC (BMP)-mediated induction of cardiac-specific gene expression. Binds to
CC BMP response element (BMPRE) DNA sequences within cardiac activating
CC regions. Acts as a transcriptional activator of ANF in cooperation with
CC NKX2-5. Promotes cardiac myocyte enlargement. Required during
CC testicular development. May play a role in sphingolipid signaling by
CC regulating the expression of sphingosine-1-phosphate degrading enzyme,
CC sphingosine-1-phosphate lyase. {ECO:0000250|UniProtKB:P43694,
CC ECO:0000250|UniProtKB:P46152, ECO:0000250|UniProtKB:Q08369}.
CC -!- SUBUNIT: Interacts with ZNF260 (By similarity). Interacts with the
CC homeobox domain of NKX2-5 through its C-terminal zinc finger. Also
CC interacts with JARID2 which represses its ability to activate
CC transcription of ANF. Interacts (via the second Zn finger) with NFATC4
CC (By similarity). Interacts with LMCD1 (By similarity). Forms a complex
CC made of CDK9, CCNT1/cyclin-T1, EP300 and GATA4 that stimulates
CC hypertrophy in cardiomyocytes. Interacts with NR5A1, ZFPM2 and TBX5.
CC Interacts with TBX18. {ECO:0000250|UniProtKB:P43694,
CC ECO:0000250|UniProtKB:Q08369}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P43694}.
CC -!- PTM: Methylation at Lys-300 attenuates transcriptional activity.
CC {ECO:0000250}.
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DR EMBL; DQ666280; ABG75570.1; -; mRNA.
DR RefSeq; NP_001041577.1; NM_001048112.1.
DR RefSeq; XP_005635679.1; XM_005635622.2.
DR RefSeq; XP_013962935.1; XM_014107460.1.
DR RefSeq; XP_013962936.1; XM_014107461.1.
DR RefSeq; XP_013962937.1; XM_014107462.1.
DR RefSeq; XP_013962938.1; XM_014107463.1.
DR AlphaFoldDB; Q0Q0E4; -.
DR SMR; Q0Q0E4; -.
DR STRING; 9612.ENSCAFP00000038219; -.
DR PaxDb; Q0Q0E4; -.
DR Ensembl; ENSCAFT00030032771; ENSCAFP00030028589; ENSCAFG00030017775.
DR Ensembl; ENSCAFT00845034032; ENSCAFP00845026636; ENSCAFG00845019258.
DR GeneID; 486079; -.
DR KEGG; cfa:486079; -.
DR CTD; 2626; -.
DR VEuPathDB; HostDB:ENSCAFG00845019258; -.
DR eggNOG; KOG1601; Eukaryota.
DR GeneTree; ENSGT00940000158349; -.
DR HOGENOM; CLU_027524_0_0_1; -.
DR InParanoid; Q0Q0E4; -.
DR OMA; GIMTSNH; -.
DR OrthoDB; 807790at2759; -.
DR TreeFam; TF315391; -.
DR Reactome; R-CFA-983231; Factors involved in megakaryocyte development and platelet production.
DR Proteomes; UP000002254; Chromosome 25.
DR Bgee; ENSCAFG00000029087; Expressed in jejunum and 18 other tissues.
DR GO; GO:0016604; C:nuclear body; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IEA:Ensembl.
DR GO; GO:0070410; F:co-SMAD binding; IEA:Ensembl.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
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:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0003180; P:aortic valve morphogenesis; IEA:Ensembl.
DR GO; GO:0003290; P:atrial septum secundum morphogenesis; IEA:Ensembl.
DR GO; GO:0045165; P:cell fate commitment; IBA:GO_Central.
DR GO; GO:0003197; P:endocardial cushion development; IEA:Ensembl.
DR GO; GO:0060575; P:intestinal epithelial cell differentiation; IEA:Ensembl.
DR GO; GO:0008584; P:male gonad development; IEA:Ensembl.
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 GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR CDD; cd00202; ZnF_GATA; 2.
DR Gene3D; 3.30.50.10; -; 2.
DR InterPro; IPR008013; GATA_N.
DR InterPro; IPR016375; TF_GATA_4/5/6.
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 Pfam; PF05349; GATA-N; 1.
DR PIRSF; PIRSF003028; TF_GATA_4/5/6; 1.
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 Activator; DNA-binding; Metal-binding; Methylation; Nucleus;
KW Reference proteome; Repeat; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..442
FT /note="Transcription factor GATA-4"
FT /id="PRO_0000289588"
FT ZN_FING 217..241
FT /note="GATA-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00094"
FT ZN_FING 271..295
FT /note="GATA-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00094"
FT REGION 62..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..362
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 300
FT /note="N6-methyllysine; by EZH2"
FT /evidence="ECO:0000250|UniProtKB:Q08369"
SQ SEQUENCE 442 AA; 44487 MW; 1CF7F807586FC991 CRC64;
MYQSLAMAAN HGPPPGAYEA GGPGAFMHGA GAASSPVYVP TPRVPSSVLG LSYLQGGGGA
AASGASSGGG SGGAPSAAGP GAQQGSPGWS QAGADGAAYT PPPVSPRFSF PGTTGSLAAA
AAAAAAREAA AYGGGGGAAG AGLAGREQYG RAGFAGSYSS PYPAYMADVG ASWAAAAAAS
AGPFDSPVLH SLPGRANPAA RHPNLDMFDD FSEGRECVNC GAMSTPLWRR DGTGHYLCNA
CGLYHKMNGI NRPLIKPQRR LSASRRVGLS CANCQTTTTT LWRRNAEGEP VCNACGLYMK
LHGVPRPLAM RKEGIQTRKR KPKNLNKSKT PAGPSGGESL PPASSASSNS SNVATSSSEE
MRPIKTEPGL SSHYGHSSSM SQTFSVSAMS GHGPSIHPVL SALKLSPQGY TSSVSQSPQA
SSKQDPWNSL ALADSHGDII TA
