FXI1A_XENLA
ID FXI1A_XENLA Reviewed; 370 AA.
AC Q91904; Q68F03;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Forkhead box protein I1-A;
DE Short=FoxI1-A;
DE Short=FoxI1a;
DE Short=xFoxI1a;
DE AltName: Full=Fork head domain-related protein 2;
DE Short=xFD-2;
DE Short=xFD2;
GN Name=foxi1-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:CAA52364.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Gastrula {ECO:0000269|PubMed:8199048};
RX PubMed=8199048; DOI=10.1016/0925-4773(94)90025-6;
RA Lef J., Clement J.H., Oschwald R., Koester M., Knoechel W.;
RT "Spatial and temporal transcription patterns of the forkhead related XFD-
RT 2/XFD-2' genes in Xenopus laevis embryos.";
RL Mech. Dev. 45:117-126(1994).
RN [2] {ECO:0000312|EMBL:AAH80044.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo {ECO:0000312|EMBL:AAH80044.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 118-228.
RC TISSUE=Gastrula {ECO:0000305};
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 SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
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 [6] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=16079156; DOI=10.1242/dev.01959;
RA Matsuo-Takasaki M., Matsumura M., Sasai Y.;
RT "An essential role of Xenopus Foxi1a for ventral specification of the
RT cephalic ectoderm during gastrulation.";
RL Development 132:3885-3894(2005).
RN [7] {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: Transcription factor. Essential for ventral specification of
CC the early cephalic (head) ectoderm during gastrulation, playing a role
CC in the non-neural versus neural cell fate choice. Binds to DNA via the
CC target sequence 5'-[AG]TAAA[CT]A-3', with 5'-ATAAACA-3' being the
CC preferred binding site. {ECO:0000269|PubMed:16079156}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00089,
CC ECO:0000269|PubMed:8735935}.
CC -!- TISSUE SPECIFICITY: Initially localized to the animal hemisphere (the
CC presumptive ectoderm) of early-mid blastula embryos. Becomes restricted
CC to head placodes, excluding the otic placodes, by the tailbud stages.
CC {ECO:0000269|PubMed:16079156, ECO:0000269|PubMed:8199048,
CC ECO:0000269|PubMed:8735935}.
CC -!- DEVELOPMENTAL STAGE: Expression begins at the early-mid blastula stage.
CC Levels are highest during the blastula and gastrula stages, after which
CC levels decreases until somite segregation. At later developmental
CC stages, expressed at a slightly lower level than foxi1-B.
CC {ECO:0000269|PubMed:16079156, ECO:0000269|PubMed:8199048,
CC ECO:0000269|PubMed:8735935}.
CC -!- INDUCTION: Induced by Bmp-signaling. Suppressed by Wnt-signaling.
CC {ECO:0000269|PubMed:16079156, ECO:0000269|PubMed:8735935}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH80044.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X74315; CAA52364.1; -; mRNA.
DR EMBL; BC080044; AAH80044.1; ALT_INIT; mRNA.
DR PIR; S49008; S49008.
DR RefSeq; NP_001081617.1; NM_001088148.1.
DR AlphaFoldDB; Q91904; -.
DR SMR; Q91904; -.
DR DNASU; 397954; -.
DR GeneID; 397954; -.
DR KEGG; xla:397954; -.
DR CTD; 397954; -.
DR Xenbase; XB-GENE-865722; foxi4.2.S.
DR OrthoDB; 1270467at2759; -.
DR Proteomes; UP000186698; Chromosome 1S.
DR Bgee; 397954; Expressed in gastrula and 3 other tissues.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0048264; P:determination of ventral identity; IMP:UniProtKB.
DR GO; GO:0007398; P:ectoderm development; IMP:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS: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 Developmental protein; Differentiation; DNA-binding; Neurogenesis; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..370
FT /note="Forkhead box protein I1-A"
FT /id="PRO_0000258001"
FT DNA_BIND 127..221
FT /note="Fork-head"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00089"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..243
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..269
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 167
FT /note="S -> C (in Ref. 2; AAH80044)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 370 AA; 41388 MW; 6CC5A3F6B285E327 CRC64;
MNPVQQPAQH KCPASSLNPP HPKRAQEAPD MGLYCDNFMY QQHNLHPSHR ATNFSIGDFT
HQANPYLWLG GPGVNNSPSY SPTPAPYIPP AFSAPQRQFL ANSAAFGGAD LGWMSAASQE
ELLKRVRPPY SYSALIAMSI QNATDKRLTL SQIYQYVAEN FPFYKKSKAG WQNSIRHNLS
LNDCFKKMPR DENDPGKGNY WTLDSNCEKM FDNGNFRRKR KPKSETNNIK IAKREEDHVS
PKGKESPPMI TPSSPKELSP TGHSKCPSPP TVTYTPCLTN FIGSMTAVDS ATMNRQGPLG
LLNELSQRNL NGLSSFISGS AVDQSPEHQD SSLFYNRSPY YSSLPTSNQK QPPYLQQLHP
QQSPLYQGRY
