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FAST3_XENLA
ID   FAST3_XENLA             Reviewed;         344 AA.
AC   Q8JIT7;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Forkhead activin signal transducer 3;
DE            Short=Fast-3;
DE            Short=xFAST-3;
DE   AltName: Full=Forkhead box protein H1b;
DE   AltName: Full=XFoxH1b;
GN   Name=fast3;
GN   Synonyms=foxh1b {ECO:0000303|PubMed:14729957, ECO:0000303|PubMed:15656969};
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:CAD29460.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, IDENTIFICATION IN ARF2
RP   COMPLEX, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Gastrula {ECO:0000269|PubMed:12050132};
RX   PubMed=12050132; DOI=10.1242/dev.129.12.2823;
RA   Howell M., Inman G.J., Hill C.S.;
RT   "A novel Xenopus Smad-interacting forkhead transcription factor (XFast-3)
RT   cooperates with XFast-1 in regulating gastrulation movements.";
RL   Development 129:2823-2834(2002).
RN   [2] {ECO:0000305}
RP   SUBUNIT.
RX   PubMed=12374795; DOI=10.1074/jbc.m208532200;
RA   Inman G.J., Hill C.S.;
RT   "Stoichiometry of active smad-transcription factor complexes on DNA.";
RL   J. Biol. Chem. 277:51008-51016(2002).
RN   [3] {ECO:0000305}
RP   INTERACTION WITH SMAD2, AND IDENTIFICATION OF FAST/FOXH1 MOTIF.
RX   PubMed=14729957; DOI=10.1128/mcb.24.3.1106-1121.2004;
RA   Randall R.A., Howell M., Page C.S., Daly A., Bates P.A., Hill C.S.;
RT   "Recognition of phosphorylated-Smad2-containing complexes by a novel Smad
RT   interaction motif.";
RL   Mol. Cell. Biol. 24:1106-1121(2004).
RN   [4] {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: Transcriptional activator. Upon TGF-beta induction, forms a
CC       transcriptionally active complex with smad2 and smad4 called activin-
CC       responsive factor 2 (ARF2), which binds a site on the mix-B/mix.2
CC       promoter called the activin response element (ARE). Binds to activated
CC       smads and the ARE with much higher affinity than foxh1/fast-1. Acts
CC       with foxh1/fast-1 to control the convergent extension movements of
CC       gastrulation. {ECO:0000269|PubMed:12050132}.
CC   -!- SUBUNIT: ARF2 contains 2 smad2s, 1 smad4 and 1 fast3 protein. Interacts
CC       with the MH2 domain of smad2. The ARF1 and ARF2 complexes are activated
CC       by distinct TGFbeta family members; formation of ARF2 is promoted by
CC       derriere and vegt. {ECO:0000269|PubMed:12050132,
CC       ECO:0000269|PubMed:12374795, ECO:0000269|PubMed:14729957}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255, ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in the animal cap (prospective
CC       ectoderm) and prospective mesoderm of stage 10.25 embryos.
CC       {ECO:0000269|PubMed:12050132}.
CC   -!- DEVELOPMENTAL STAGE: Expressed only during gastrulation.
CC       {ECO:0000269|PubMed:12050132}.
CC   -!- DOMAIN: The FM region is required for binding smad2/smad4 complexes.
CC       FM2 is more effective than FM1 and only interacts with phosphorylated
CC       smad2 that is in an activated smad complex.
CC       {ECO:0000269|PubMed:14729957}.
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DR   EMBL; AJ440777; CAD29460.1; -; Genomic_DNA.
DR   RefSeq; NP_001165546.1; NM_001172075.1.
DR   AlphaFoldDB; Q8JIT7; -.
DR   SMR; Q8JIT7; -.
DR   GeneID; 100337554; -.
DR   KEGG; xla:100337554; -.
DR   CTD; 100337554; -.
DR   Xenbase; XB-GENE-6461998; foxh1.2.L.
DR   OrthoDB; 1270467at2759; -.
DR   Proteomes; UP000186698; Chromosome 6L.
DR   Bgee; 100337554; Expressed in gastrula and 3 other tissues.
DR   GO; GO:0032444; C:activin responsive factor complex; IDA:UniProtKB.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0046332; F:SMAD binding; IPI:UniProtKB.
DR   GO; GO:0001702; P:gastrulation with mouth forming second; IMP:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IMP:UniProtKB.
DR   CDD; cd00059; FH; 1.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR001766; Fork_head_dom.
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   PRINTS; PR00053; FORKHEAD.
DR   SMART; SM00339; FH; 1.
DR   SUPFAM; SSF46785; SSF46785; 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; Gastrulation; Nucleus;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..344
FT                   /note="Forkhead activin signal transducer 3"
FT                   /id="PRO_0000271180"
FT   DNA_BIND        69..165
FT                   /note="Fork-head"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00089"
FT   REGION          1..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          213..331
FT                   /note="SMAD interaction domain (SID)"
FT                   /evidence="ECO:0000255"
FT   MOTIF           224..228
FT                   /note="Fast/FoxH1 motif 1 (FM1)"
FT                   /evidence="ECO:0000269|PubMed:14729957"
FT   MOTIF           234..240
FT                   /note="Fast/FoxH1 motif 1 (FM2)"
FT                   /evidence="ECO:0000269|PubMed:14729957"
FT   MOTIF           293..316
FT                   /note="SMAD interaction motif (SIM)"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        24..56
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   344 AA;  38658 MW;  17B68EE604A988D2 CRC64;
     MSFGLHPWDV AFRPSPPHNL EKKVVPPGAD REKSLPSPKE DSDGAREPDS TVDLRKKNKK
     KKNYQRYAKP PYSYLAMISL VIQNSPEKRL KLSQILQDIS SLFPFFKGNY QGWKDSIRHN
     LSSNDCFRKV LKDPLKPQAK GNYWTVDVTR IPPDALKLQN TAVTRQDLFP LDLAPYILHG
     QPYRSLERLS ANHTRGRTTP RMEPEVQIPV SDPAVSFPMI LWNLPTSYSK CVAPNVVAPP
     SIHPLLLYSN FPSISIYNYL PPPYGSPVYS DRRDLLASGL HPQIPLTPKP PELKNAPSDF
     PPNKTVFDIP VYTGHPGFLA SQSLFSPHLP TATPPLVGYR PSGL
 
 
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