GATA6_RAT
ID GATA6_RAT Reviewed; 587 AA.
AC P46153;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Transcription factor GATA-6;
DE AltName: Full=DNA-binding protein GATA-GT2;
DE AltName: Full=GATA-binding factor 6;
GN Name=Gata6;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 108-587, AND TISSUE SPECIFICITY.
RC STRAIN=Wistar; TISSUE=Stomach;
RX PubMed=8248184; DOI=10.1073/pnas.90.22.10876;
RA Tamura S., Wang X.H., Maeda M., Futai M.;
RT "Gastric DNA-binding proteins recognize upstream sequence motifs of
RT parietal cell-specific genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:10876-10880(1993).
RN [3]
RP ERRATUM OF PUBMED:8248184.
RX PubMed=8183957; DOI=10.1073/pnas.91.10.4609;
RA Tamura S., Wang X.H., Maeda M., Futai M.;
RL Proc. Natl. Acad. Sci. U.S.A. 91:4609-4609(1994).
RN [4]
RP IDENTIFICATION OF PROBABLE FRAMESHIFTS.
RX PubMed=8083222; DOI=10.1016/s0021-9258(17)31636-8;
RA Laverriere A.C., Macneill C., Mueller C., Poelmann R.E., Burch J.B.E.,
RA Evans T.;
RT "GATA-4/5/6, a subfamily of three transcription factors transcribed in
RT developing heart and gut.";
RL J. Biol. Chem. 269:23177-23184(1994).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=28167758; DOI=10.1073/pnas.1621425114;
RA Lee D.Y., Lin T.E., Lee C.I., Zhou J., Huang Y.H., Lee P.L., Shih Y.T.,
RA Chien S., Chiu J.J.;
RT "MicroRNA-10a is crucial for endothelial response to different flow
RT patterns via interaction of retinoid acid receptors and histone
RT deacetylases.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:2072-2077(2017).
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.
CC -!- TISSUE SPECIFICITY: Expressed in aortic endothelial cells, with low
CC expression in the descending thoracic aorta and the outer curvature of
CC the aortic arch, where pulsatory shear stress exists, and high in the
CC inner curvature of the aortic arch, where oscillatory shear stress
CC prevails (at protein level) (PubMed:28167758). Expressed predominantly
CC in gastric mucosa and at much lower levels in the intestine
CC (PubMed:8248184). {ECO:0000269|PubMed:28167758,
CC ECO:0000269|PubMed:8248184}.
CC -!- DOMAIN: The GATA-type zinc fingers mediate interaction with LMCD1.
CC {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA92577.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AABR03109887; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03111467; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03111603; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03112401; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03112926; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03113211; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; L22760; AAA92577.1; ALT_FRAME; mRNA.
DR PIR; A49645; A49645.
DR RefSeq; NP_062058.2; NM_019185.2.
DR AlphaFoldDB; P46153; -.
DR SMR; P46153; -.
DR BioGRID; 247966; 1.
DR STRING; 10116.ENSRNOP00000036967; -.
DR iPTMnet; P46153; -.
DR PhosphoSitePlus; P46153; -.
DR PaxDb; P46153; -.
DR PRIDE; P46153; -.
DR Ensembl; ENSRNOT00000081399; ENSRNOP00000070439; ENSRNOG00000023433.
DR GeneID; 29300; -.
DR KEGG; rno:29300; -.
DR UCSC; RGD:2666; rat.
DR CTD; 2627; -.
DR RGD; 2666; Gata6.
DR eggNOG; KOG1601; Eukaryota.
DR GeneTree; ENSGT00940000160814; -.
DR InParanoid; P46153; -.
DR OrthoDB; 807790at2759; -.
DR PhylomeDB; P46153; -.
DR Reactome; R-RNO-5683826; Surfactant metabolism.
DR Reactome; R-RNO-983231; Factors involved in megakaryocyte development and platelet production.
DR PRO; PR:P46153; -.
DR Proteomes; UP000002494; Chromosome 18.
DR GO; GO:0031965; C:nuclear membrane; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0005667; C:transcription regulator complex; ISO:RGD.
DR GO; GO:0003682; F:chromatin binding; ISO:RGD.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; 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; ISO:RGD.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:RGD.
DR GO; GO:0051525; F:NFAT protein binding; ISO:RGD.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0000978; F:RNA polymerase II cis-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; IDA:BHF-UCL.
DR GO; GO:0001223; F:transcription coactivator binding; ISO:RGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0048645; P:animal organ formation; ISO:RGD.
DR GO; GO:0055007; P:cardiac muscle cell differentiation; ISO:RGD.
DR GO; GO:0060038; P:cardiac muscle cell proliferation; IEA:Ensembl.
DR GO; GO:0014898; P:cardiac muscle hypertrophy in response to stress; ISO:RGD.
DR GO; GO:0048738; P:cardiac muscle tissue development; ISO:RGD.
DR GO; GO:0060947; P:cardiac vascular smooth muscle cell differentiation; ISO:RGD.
DR GO; GO:0045165; P:cell fate commitment; IBA:GO_Central.
DR GO; GO:0071773; P:cellular response to BMP stimulus; ISO:RGD.
DR GO; GO:0071371; P:cellular response to gonadotropin stimulus; ISO:RGD.
DR GO; GO:0071456; P:cellular response to hypoxia; ISO:RGD.
DR GO; GO:0060486; P:club cell differentiation; ISO:RGD.
DR GO; GO:0035987; P:endodermal cell differentiation; ISO:RGD.
DR GO; GO:0007493; P:endodermal cell fate determination; ISO:RGD.
DR GO; GO:0030855; P:epithelial cell differentiation; ISO:RGD.
DR GO; GO:0070315; P:G1 to G0 transition involved in cell differentiation; ISO:RGD.
DR GO; GO:0010467; P:gene expression; ISO:RGD.
DR GO; GO:0060047; P:heart contraction; ISO:RGD.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0060575; P:intestinal epithelial cell differentiation; ISO:RGD.
DR GO; GO:0001889; P:liver development; ISO:RGD.
DR GO; GO:0060430; P:lung saccule development; ISO:RGD.
DR GO; GO:0008584; P:male gonad development; ISO:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
DR GO; GO:1902894; P:negative regulation of miRNA transcription; IMP:BHF-UCL.
DR GO; GO:1904003; P:negative regulation of sebum secreting cell proliferation; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0032911; P:negative regulation of transforming growth factor beta1 production; ISO:RGD.
DR GO; GO:0032912; P:negative regulation of transforming growth factor beta2 production; ISO:RGD.
DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEP:RGD.
DR GO; GO:0003148; P:outflow tract septum morphogenesis; ISO:RGD.
DR GO; GO:0031016; P:pancreas development; ISO:RGD.
DR GO; GO:0003310; P:pancreatic A cell differentiation; ISO:RGD.
DR GO; GO:0006644; P:phospholipid metabolic process; ISO:RGD.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISO:RGD.
DR GO; GO:0030513; P:positive regulation of BMP signaling pathway; IDA:BHF-UCL.
DR GO; GO:0010666; P:positive regulation of cardiac muscle cell apoptotic process; IMP:BHF-UCL.
DR GO; GO:0060045; P:positive regulation of cardiac muscle cell proliferation; ISO:RGD.
DR GO; GO:0110024; P:positive regulation of cardiac muscle myoblast proliferation; ISO:RGD.
DR GO; GO:0051891; P:positive regulation of cardioblast differentiation; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:1901390; P:positive regulation of transforming growth factor beta activation; ISO:RGD.
DR GO; GO:0002759; P:regulation of antimicrobial humoral response; ISO:RGD.
DR GO; GO:0010468; P:regulation of gene expression; ISO:RGD.
DR GO; GO:0051591; P:response to cAMP; IEP:RGD.
DR GO; GO:0043627; P:response to estrogen; ISO:RGD.
DR GO; GO:0070848; P:response to growth factor; ISO:RGD.
DR GO; GO:0032526; P:response to retinoic acid; ISO:RGD.
DR GO; GO:0009636; P:response to toxic substance; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0001949; P:sebaceous gland cell differentiation; ISO:RGD.
DR GO; GO:0003163; P:sinoatrial node development; ISO:RGD.
DR GO; GO:0098773; P:skin epidermis development; ISO:RGD.
DR GO; GO:0051145; P:smooth muscle cell differentiation; ISO:RGD.
DR GO; GO:0048863; P:stem cell differentiation; IEA:Ensembl.
DR GO; GO:0035239; P:tube morphogenesis; ISO:RGD.
DR GO; GO:0003309; P:type B pancreatic cell differentiation; ISO:RGD.
DR GO; GO:0060510; P:type II pneumocyte differentiation; ISO:RGD.
DR CDD; cd00202; ZnF_GATA; 2.
DR Gene3D; 3.30.50.10; -; 2.
DR InterPro; IPR008013; GATA_N.
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 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 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..587
FT /note="Transcription factor GATA-6"
FT /id="PRO_0000083426"
FT ZN_FING 384..408
FT /note="GATA-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00094"
FT ZN_FING 438..462
FT /note="GATA-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00094"
FT REGION 17..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 209..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 480..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..532
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 266
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CROSSLNK 423
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q92908"
FT CROSSLNK 467
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q92908"
FT CROSSLNK 478
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q92908"
FT CONFLICT 431
FT /note="S -> I (in Ref. 2; AAA92577)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 587 AA; 59168 MW; 2D1C1515B66B1BCE CRC64;
MALTDGGWCL PKRFGAAAAD AGDSGPFPAR EPSSPLSPIS SSSSSCSRGG DRGPCGASNC
RTPQLDTEAV AGPPGRSLLL SPYTSHPFAA AHGAAAPGVA GPGSALSTWE DLLLFTDLDQ
AATASKLLWS SRGAKLSPFA AEQPEEMYQT LAALSSQGPA AYDGAPGGFV HSAAAAAAAA
AAASSPVYVP TTRVGSMLPG LPYLQGAGSG PSNHAGGAGA HPGWPQASAD SPPYGGGGAA
GGGAAGPGGA GSATAHASAR FPYSPSPPMA NGAARDPGGY VAAGGAGAGS VSGGGGSLAA
MGGREHQYSS LSAARPLNGT YHHHHHHHPT YSPYMGAPLT PAWPAGPFET PVLHSLQSRA
GAPLPVPRGP SADLLEDLSE SRECVNCGSI QTPLWRRDGT GHYLCNACGL YSKMNGLSRP
LIKPQKRVPS SRRLGLSCAN CHTTTTTLWR RNAEGEPVCN ACGLYMKLHG VPRPLAMKKE
GIQTRKRKPK NINKSKACSG NSSVPMTPTS SSSNSDDCTK NTSPPTQSTA SGVGASVMSA
VGESANPENS DLKYSGQDGL YIGVSLSSPA EVTSSVRQDS WCALALA
