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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
 
 
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