FXD5B_XENLA
ID FXD5B_XENLA Reviewed; 353 AA.
AC Q9PT68; Q91763;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Forkhead box protein D5-B;
DE Short=FoxD5-B;
DE Short=FoxD5b;
DE AltName: Full=Fork head domain protein 3;
DE AltName: Full=Fork head domain-related protein 12';
DE Short=xFD-12';
DE AltName: Full=Forkhead-like;
DE Short=xFLIP;
DE AltName: Full=XlFoxD5b;
GN Name=foxd5-b;
GN Synonyms=fhd3 {ECO:0000312|EMBL:AAA85023.1},
GN fkh-l {ECO:0000303|PubMed:10781939}, foxd5b {ECO:0000312|EMBL:CAH64538.1};
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:CAB44729.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Gastrula {ECO:0000269|PubMed:10559492};
RX PubMed=10559492; DOI=10.1016/s0925-4773(99)00195-1;
RA Soelter M., Koester M., Hollemann T., Brey A., Pieler T., Knoechel W.;
RT "Characterization of a subfamily of related winged helix genes, XFD-
RT 12/12'/12'' (XFLIP), during Xenopus embryogenesis.";
RL Mech. Dev. 89:161-165(1999).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAF34705.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RC TISSUE=Dorsal lip {ECO:0000269|PubMed:10781939};
RX PubMed=10781939; DOI=10.1016/s0925-4773(00)00265-3;
RA Fetka I., Doederlein G., Bouwmeester T.;
RT "Neuroectodermal specification and regionalization of the Spemann organizer
RT in Xenopus.";
RL Mech. Dev. 93:49-58(2000).
RN [3] {ECO:0000305, ECO:0000312|EMBL:CAH64538.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX PubMed=15555577; DOI=10.1016/j.bbrc.2004.10.177;
RA Schoen C., Koester M., Knoechel W.;
RT "A downstream enhancer is essential for Xenopus FoxD5 transcription.";
RL Biochem. Biophys. Res. Commun. 325:1360-1366(2004).
RN [4] {ECO:0000305, ECO:0000312|EMBL:AAA85023.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 112-142, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Embryo {ECO:0000269|PubMed:7937122};
RX PubMed=7937122; DOI=10.1093/nar/22.19.3990;
RA King M.W., Moore M.J.;
RT "Novel HOX, POU and FKH genes expressed during bFGF-induced mesodermal
RT differentiation in Xenopus.";
RL Nucleic Acids Res. 22:3990-3996(1994).
RN [5] {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 repressor (By similarity). Controls the
CC convergence and extension movements of medial neural plate precursors
CC during gastrulation. {ECO:0000250|UniProtKB:Q9PRJ8,
CC ECO:0000269|PubMed:10781939}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255, ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expression is initiated at the late blastula stage
CC in the presumptive dorsal marginal zone, prior to blastopore lip
CC formation. At the onset of gastrulation, expressed in the superficial
CC layer of cells in the dorsal blastopore lip (Spemann organizer). In the
CC open neural plate, expressed dynamically in a row of cells along the
CC dorsal midline that are destined to become the floor plate of the
CC neural tube. Only weakly expressed in the posterior region of the newly
CC forming notochord. After neural tube closure, expression is detected
CC only in the tailtip and a small area located at the midbrain/hindbrain
CC boundary. {ECO:0000269|PubMed:10559492, ECO:0000269|PubMed:10781939,
CC ECO:0000269|PubMed:15555577, ECO:0000269|PubMed:7937122}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC Maternal expression levels are low and become further reduced after
CC fertilization. Zygotic expression begins at the mid-blastula transition
CC and peaks during the gastrula/neurula stages before declining again by
CC stage 34. {ECO:0000269|PubMed:10559492, ECO:0000269|PubMed:7937122}.
CC -!- INDUCTION: By FGF-signaling. Inhibited by bmp-signaling.
CC {ECO:0000269|PubMed:10781939}.
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DR EMBL; AJ242677; CAB44729.1; -; mRNA.
DR EMBL; AF223426; AAF34705.1; -; mRNA.
DR EMBL; AJ850136; CAH64538.1; -; Genomic_DNA.
DR EMBL; U04872; AAA85023.1; -; mRNA.
DR PIR; S50124; S50124.
DR RefSeq; NP_001081722.1; NM_001088253.1.
DR RefSeq; NP_001091898.1; NM_001098428.1.
DR AlphaFoldDB; Q9PT68; -.
DR SMR; Q9PT68; -.
DR PRIDE; Q9PT68; -.
DR GeneID; 394316; -.
DR GeneID; 398016; -.
DR KEGG; xla:398016; -.
DR CTD; 394316; -.
DR CTD; 398016; -.
DR Xenbase; XB-GENE-6252054; foxd4l1.1.L.
DR OrthoDB; 1270467at2759; -.
DR Proteomes; UP000186698; Chromosome 1L.
DR Bgee; 398016; Expressed in gastrula and 2 other tissues.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; NAS:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; NAS:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0001840; P:neural plate development; IEP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB.
DR CDD; cd00059; FH; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR001766; Fork_head_dom.
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 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 2: Evidence at transcript level;
KW Developmental protein; Differentiation; DNA-binding; Neurogenesis; Nucleus;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..353
FT /note="Forkhead box protein D5-B"
FT /id="PRO_0000259616"
FT DNA_BIND 97..191
FT /note="Fork-head"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00089"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 48..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 254..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..85
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 353 AA; 39682 MW; 78EC222484367B8F CRC64;
MSFSQESGTH HNSLDYAGVS DEEDEIDILG EDDPCSLKSH FYLQPTHSDM GDSGMLSPSK
LSCTESESDS SGESEGGTSK DSPATSPGGK AKRALVKPPY SYIALITMAI LQSPHKKLTL
SGICDFISSK FPYYKDKFPA WQNSIRHNLS LNDCFIKIPR EPGNPGKGNY WTLDPASEDM
FDNGSFLRRR KRFKRHQQEF FKDGLMMYNS LPYYRPYSAL QPQPMLQQTP LACMAIPETL
SMPTNLTPYP DIKRKAHYPD QGAHRGFEGQ DANNHPNKSQ SKCSFSIENI MKKPKEPEPS
FPSFNSHWNY NNHLLQRPSS CFLPAVLNLS TGPLLANVQG TRQYNLIKFP GSY