GATA6_PIG
ID GATA6_PIG Reviewed; 451 AA.
AC Q95JA5;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Transcription factor GATA-6;
DE AltName: Full=GATA-binding factor 6;
DE Flags: Fragment;
GN Name=GATA6;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart;
RA Markmann A., Kresse H.;
RT "Regulation of VSMC differentiation.";
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transcriptional activator that regulates SEMA3C and PLXNA2.
CC May regulate genes that protect epithelial cells from bacterial
CC infection. Involved in gene regulation specifically in the gastric
CC epithelium. Involved in bone morphogenetic protein (BMP)-mediated
CC cardiac-specific gene expression. Binds to BMP response element (BMPRE)
CC DNA sequences within cardiac activating regions.
CC {ECO:0000250|UniProtKB:Q61169}.
CC -!- SUBUNIT: Interacts with LMCD1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- DOMAIN: The GATA-type zinc fingers mediate interaction with LMCD1.
CC {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL09304.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF295687; AAL09304.1; ALT_INIT; mRNA.
DR RefSeq; NP_999493.2; NM_214328.2.
DR AlphaFoldDB; Q95JA5; -.
DR SMR; Q95JA5; -.
DR STRING; 9823.ENSSSCP00000004009; -.
DR PaxDb; Q95JA5; -.
DR PRIDE; Q95JA5; -.
DR GeneID; 397600; -.
DR KEGG; ssc:397600; -.
DR CTD; 2627; -.
DR eggNOG; KOG1601; Eukaryota.
DR InParanoid; Q95JA5; -.
DR OrthoDB; 807790at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
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:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045165; P:cell fate commitment; IBA:GO_Central.
DR GO; GO:0030855; P:epithelial cell differentiation; IBA:GO_Central.
DR GO; GO:0007507; P:heart development; IEA:UniProt.
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 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; IPR028437; TF_GATA_6.
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:SF23; PTHR10071:SF23; 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; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN <1..451
FT /note="Transcription factor GATA-6"
FT /id="PRO_0000083425"
FT ZN_FING 246..270
FT /note="GATA-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00094"
FT ZN_FING 300..324
FT /note="GATA-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00094"
FT REGION 69..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 338..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92908"
FT CROSSLNK 285
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q92908"
FT CROSSLNK 329
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q92908"
FT CROSSLNK 340
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q92908"
FT NON_TER 1
SQ SEQUENCE 451 AA; 45410 MW; 95607C32BD837E03 CRC64;
EQPEEMYQTL AALSSQGPAA YDGAPGGFVH SAAAAAAAAA AASSPVYVPT TRVGSMLPGL
PYLQGAGSGP ANHAGGAGSH PGWPQASADS PPYGSGGGTA GGGAAGPGSA GSAAAHVSAR
FPYSPSPPMA NGAARDPGGY AAAGGGGAGG VSGGSGGGLA AMGSREHQYS SLSAARPLNG
TYHHHHHHHP SAYSPYVGAP LTPAWPAGPF ETPVLHSLQS RAGAPLPVPR GPSADLLEDL
PESRECVNCG SIQTPLWRRD GTGHYLCNRC GLYSKMNGLS GPLIKPQKPV PSSRRLGLSC
ANCHTTTTTL WRRNAEGEPV CNACGLYMKL HGVPRPLAMK KEGIQTRKRK PKSINKSKAC
SGNSNNSVPM TPTSTSSNSD DCSKNTSPTT QTPASGAGAS VMSGTGESAN PENSELKYSG
QDGLYIGVSL ASPAEVTSSV RQDSWCALAL A