FOXH1_XENTR
ID FOXH1_XENTR Reviewed; 515 AA.
AC Q28GC4;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Forkhead box protein H1;
DE AltName: Full=Forkhead activin signal transducer 1;
DE Short=Fast-1;
GN Name=foxh1 {ECO:0000312|EMBL:CAJ81979.1}; ORFNames=TGas103n06.1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1] {ECO:0000312|EMBL:CAJ81979.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Gastrula {ECO:0000312|EMBL:CAJ81979.1};
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transcriptional activator. Recognizes and binds to the DNA
CC sequence 5'-TGT[GT][GT]ATT-3'. Upon TGF-beta induction, forms a
CC transcriptionally active complex with smad2 and smad4 called activin-
CC responsive factor 1 (ARF1), 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 lower affinity than fast3. Necessary for
CC the first steps in mesoderm specification, directly inducing mesodermal
CC genes. Acts with fast3 to control the convergent extension movements of
CC gastrulation. Binds to the proximal element (PE) of the gsc gene and
CC cooperates with gtf2ird1/wbscr11 and SMAD proteins to regulate gsc
CC transcription (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: ARF1 contains 2 smad2s, 1 smad4 and 1 foxh1/fast-1 protein.
CC Interaction with smad4 is most likely indirect through interaction with
CC the MH2 domain of smad2. Binds to the MH2 domain of smad3, which can
CC incorporate into the ARF1 complex. The ARF1 and ARF2 complexes are
CC activated by distinct TGF-beta family members; formation of ARF1 is
CC promoted by activin. Interacts (via Fork-head domain) with
CC gtf2ird1/wbscr11 (via repeats 4-5) (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255, ECO:0000305}.
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 (By similarity).
CC {ECO:0000250|UniProtKB:P70056}.
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DR EMBL; CR761447; CAJ81979.1; -; mRNA.
DR RefSeq; NP_001017084.1; NM_001017084.1.
DR AlphaFoldDB; Q28GC4; -.
DR SMR; Q28GC4; -.
DR STRING; 8364.ENSXETP00000045081; -.
DR PaxDb; Q28GC4; -.
DR GeneID; 549838; -.
DR KEGG; xtr:549838; -.
DR CTD; 8928; -.
DR Xenbase; XB-GENE-1194372; foxh1.
DR eggNOG; KOG2294; Eukaryota.
DR InParanoid; Q28GC4; -.
DR OrthoDB; 1270467at2759; -.
DR Proteomes; UP000008143; Chromosome 6.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISS:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR GO; GO:0032924; P:activin receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0071345; P:cellular response to cytokine stimulus; ISS:UniProtKB.
DR GO; GO:0007369; P:gastrulation; IEA:UniProtKB-KW.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Activator; Developmental protein; DNA-binding; Gastrulation; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..515
FT /note="Forkhead box protein H1"
FT /id="PRO_0000271179"
FT DNA_BIND 110..206
FT /note="Fork-head"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00089"
FT REGION 55..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 307..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..503
FT /note="SMAD-interaction domain (SID)"
FT MOTIF 402..406
FT /note="Fast/FoxH1 motif 1 (FM1)"
FT /evidence="ECO:0000255"
FT MOTIF 412..418
FT /note="Fast/FoxH1 motif 2 (FM2)"
FT /evidence="ECO:0000255"
FT MOTIF 467..488
FT /note="SMAD-interaction motif (SIM)"
FT COMPBIAS 72..88
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 515 AA; 56741 MW; FAEF54ED27D63714 CRC64;
MRDPSSLYAG FPVGSQYESV EPPSLALLSS IYQEQVPAAP GHSYEQCAQP WPPLYREGGT
WSPDRGSMHG LSPGTQEGSC TQAEGTKDSL GGDETLSRKS KKKNYHRYAK PPYSYLAMIA
LVIQNSPEKR LKLSQILKEV STLFPFFKGD YMGWKDSIRH NLSSNDCFKK VLKDPGKPQA
KGNFWTVDVS RIPLDAMKLQ NTALTRGGSD YFVQDLAPYI LHNYKYEHNV VVYAPHHMPS
HASSLPLAED PHQTNTGGKL NTSFMIDSLL NDLQDVDLPD VPRNIESQRI SPAVAINNMW
SSAPLLYPQS KPTRNGRGPG FSASHSTYSS SSSSISTISP VGFQETQERS EDLLGRQTQR
LGFPTKRPRE DDGCSTPSSD TDAGNYSPTE PPKKMPLLSL DLPTSYTKSV APNVVAPPSV
LPFFHFPRFT YYNYGPSPYM TPPYWGFPRP TNPGGDSPRG PQTSLDLDNM LKTVPPNKSV
FDVLTSHPGD LVHPSFLGQC LGSSGSPYPS RQGLM
