FXA2A_XENLA
ID FXA2A_XENLA Reviewed; 434 AA.
AC Q91765;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Forkhead box protein A2-A;
DE Short=FoxA2-A;
DE Short=FoxA2a;
DE AltName: Full=Fork head domain-related protein 3;
DE Short=xFD-3;
DE AltName: Full=Hepatocyte nuclear factor 3-beta homolog A;
DE Short=HNF-3-beta-A;
DE Short=HNF3-beta homolog A;
DE Short=HNF3-beta-A;
DE Short=xHNF3-beta-A;
DE Short=xbeta-1;
GN Name=foxa2-a;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAA20679.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC TISSUE=Gastrula {ECO:0000269|PubMed:8155584};
RX PubMed=8155584; DOI=10.1016/0925-4773(93)90060-b;
RA Ruiz i Altaba A., Prezioso V.R., Darnell J.E., Jessell T.M.;
RT "Sequential expression of HNF-3beta and HNF-3alpha by embryonic organizing
RT centers: the dorsal lip/node, notochord and floor plate.";
RL Mech. Dev. 44:91-108(1993).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Gastrula {ECO:0000269|PubMed:8735935};
RX PubMed=8735935;
RA Lef J., Dege P., Scheucher M., Forsbach-Birk V., Clement J.H., Knoechel W.;
RT "A fork head related multigene family is transcribed in Xenopus laevis
RT embryos.";
RL Int. J. Dev. Biol. 40:245-253(1996).
RN [3] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 140-250.
RC TISSUE=Gastrula {ECO:0000269|PubMed:1358174};
RX PubMed=1358174; DOI=10.1016/0925-4773(92)90007-7;
RA Knoechel S., Lef J., Clement J.H., Klocke B., Hille S., Koester M.,
RA Knoechel W.;
RT "Activin A induced expression of a fork head related gene in posterior
RT chordamesoderm (notochord) of Xenopus laevis embryos.";
RL Mech. Dev. 38:157-165(1992).
RN [4] {ECO:0000305}
RP DNA-BINDING.
RX PubMed=7739038; DOI=10.1016/s0022-2836(95)80047-6;
RA Kaufmann E., Mueller D., Knoechel W.;
RT "DNA recognition site analysis of Xenopus winged helix proteins.";
RL J. Mol. Biol. 248:239-254(1995).
RN [5] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF
RP ASN-195; HIS-199 AND ARG-241.
RX PubMed=14697355; DOI=10.1016/j.ydbio.2003.09.017;
RA Suri C., Haremaki T., Weinstein D.C.;
RT "Inhibition of mesodermal fate by Xenopus HNF3beta/FoxA2.";
RL Dev. Biol. 265:90-104(2004).
RN [6] {ECO:0000305}
RP REVIEW.
RX PubMed=15656969; DOI=10.1016/j.gene.2004.09.037;
RA Pohl B.S., Knoechel W.;
RT "Of fox and frogs: fox (fork head/winged helix) transcription factors in
RT Xenopus development.";
RL Gene 344:21-32(2005).
CC -!- FUNCTION: Acts as a transcriptional activator during early development,
CC limiting the extent of mesoderm formation in the gastrula. Binds to DNA
CC via the target sequence 5'-GT[AC]AACA-3', with 5'-GTAAACA-3' being the
CC preferred binding site. {ECO:0000269|PubMed:14697355}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255, ECO:0000305}.
CC -!- TISSUE SPECIFICITY: At gastrula stage, expressed in both the anterior
CC and posterior endoderm, with endodermal expression persisting into
CC early tailbud stages. Expression is absent in gastrula stage ectoderm.
CC During tailbud stages, expressed in the pharyngeal region, the neural
CC floor plate, the midbrain, hindbrain and in cranial neural crest cells.
CC Expressed in the foregut of hatching larvae. In tadpoles, expressed in
CC the pharyngeal pouches and in other anterior endodermal regions. Within
CC the tadpole nervous system, expressed in the neural floor plate, at
CC high levels in the ventral midbrain and hindbrain, and at lower levels
CC in the spinal cord. Expressed in the adult lung and brain.
CC {ECO:0000269|PubMed:14697355, ECO:0000269|PubMed:8155584,
CC ECO:0000269|PubMed:8735935}.
CC -!- DEVELOPMENTAL STAGE: First detected in early gastrula stage embryos.
CC Abundant at the neurula stage, becoming less abundant at later stages.
CC {ECO:0000269|PubMed:14697355, ECO:0000269|PubMed:8155584,
CC ECO:0000269|PubMed:8735935}.
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DR EMBL; L25637; AAA20679.1; -; Genomic_DNA.
DR PIR; I51436; I51436.
DR RefSeq; NP_001165629.1; NM_001172158.1.
DR AlphaFoldDB; Q91765; -.
DR SMR; Q91765; -.
DR ChEMBL; CHEMBL3350224; -.
DR GeneID; 100127318; -.
DR KEGG; xla:100127318; -.
DR CTD; 100127318; -.
DR Xenbase; XB-GENE-865381; foxa2.L.
DR OrthoDB; 1181467at2759; -.
DR Proteomes; UP000186698; Chromosome 5L.
DR Bgee; 100127318; Expressed in lung and 8 other tissues.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0019904; F:protein domain specific binding; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0001707; P:mesoderm formation; IMP:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR CDD; cd00059; FH; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR013638; Fork-head_N.
DR InterPro; IPR001766; Fork_head_dom.
DR InterPro; IPR018533; Forkhead_box_C.
DR InterPro; IPR018122; TF_fork_head_CS_1.
DR InterPro; IPR030456; TF_fork_head_CS_2.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00250; Forkhead; 1.
DR Pfam; PF08430; Forkhead_N; 1.
DR Pfam; PF09354; HNF_C; 1.
DR PRINTS; PR00053; FORKHEAD.
DR SMART; SM00339; FH; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS00657; FORK_HEAD_1; 1.
DR PROSITE; PS00658; FORK_HEAD_2; 1.
DR PROSITE; PS50039; FORK_HEAD_3; 1.
PE 1: Evidence at protein level;
KW Activator; Developmental protein; DNA-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..434
FT /note="Forkhead box protein A2-A"
FT /id="PRO_0000248856"
FT DNA_BIND 149..243
FT /note="Fork-head"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00089"
FT REGION 249..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 195
FT /note="N->D: Abolishes DNA-binding activity and reduces
FT ability to inhibit mesoderm formation; when associated with
FT C-199 and E-241."
FT /evidence="ECO:0000269|PubMed:14697355"
FT MUTAGEN 199
FT /note="H->C: Abolishes DNA-binding activity and reduces
FT ability to inhibit mesoderm formation; when associated with
FT D-195 and E-241."
FT /evidence="ECO:0000269|PubMed:14697355"
FT MUTAGEN 241
FT /note="R->E: Abolishes DNA-binding activity and reduces
FT ability to inhibit mesoderm formation; when associated with
FT D-195 and C-199."
FT /evidence="ECO:0000269|PubMed:14697355"
FT CONFLICT 50
FT /note="R -> S (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 102
FT /note="I -> S (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 311
FT /note="K -> E (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 434 AA; 47986 MW; B6C58F40F2D3D705 CRC64;
MLGAVKMEGH EATDWSSYYG EAEAYSSVGN MNAGLSMNPM NTYMSMSAMR TSANMTASSM
NMSYVNTGMS PSLTGMSPGT GAMTGMGTGV PSMASHLSPS MIPMSAQTTA MNALAPYTNI
NSMSPIYGQS NINRSRDPKT YRRSYTHAKP PYSYISLITM AIQQSPNKML TLSEIYQWIM
DLFPFYRQNQ QRWQNSIRHS LSFNDCFLKV PRSPDKPGKG SFWTLHPDSG NMFENGCYLR
RQKRFKCEKK PSLREGGGKK LSEGASSVGS AANSSSESSV GNESPHSSSS PCQEQKRSLV
DMKSSQGLSP KHATSPASQA QHLLSQHHSV LSHEAQSHLK PEHHYSFNHP FSINNLMSSE
QQHHHHHHHN HHHHHKMDLK AYEQVMHYSS YGSPMAGSLA MSTVTNKSGL ESSPITSDTS
YYQGGYSRPI MNSS