P5F11_XENLA
ID P5F11_XENLA Reviewed; 449 AA.
AC Q7T103; A9CDQ2; Q99293;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=POU domain, class 5, transcription factor 1.1;
DE AltName: Full=POU class V protein oct-25 {ECO:0000312|EMBL:ABH07383.1};
DE Short=XOct-25 {ECO:0000312|EMBL:AAH55964.1};
GN Name=pou5f1.1; Synonyms=oct-25 {ECO:0000312|EMBL:CAG27841.1};
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:AAA49996.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC TISSUE=Gastrula {ECO:0000269|PubMed:1732736};
RX PubMed=1732736; DOI=10.1128/mcb.12.2.638-649.1992;
RA Hinkley C.S., Martin J.F., Leibham D., Perry M.;
RT "Sequential expression of multiple POU proteins during amphibian early
RT development.";
RL Mol. Cell. Biol. 12:638-649(1992).
RN [2] {ECO:0000305, ECO:0000312|EMBL:CAG27841.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH VENT2; SMAD1 AND
RP SMAD4, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Gastrula {ECO:0000269|PubMed:15292233};
RX PubMed=15292233; DOI=10.1074/jbc.m407544200;
RA Cao Y., Knochel S., Donow C., Miethe J., Kaufmann E., Knochel W.;
RT "The POU factor Oct-25 regulates the Xvent-2B gene and counteracts terminal
RT differentiation in Xenopus embryos.";
RL J. Biol. Chem. 279:43735-43743(2004).
RN [3] {ECO:0000305, ECO:0000312|EMBL:ABH07383.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Gastrula {ECO:0000269|PubMed:17950579};
RX PubMed=17950579; DOI=10.1016/j.mod.2007.09.005;
RA Takebayashi-Suzuki K., Arita N., Murasaki E., Suzuki A.;
RT "The Xenopus POU class V transcription factor XOct-25 inhibits ectodermal
RT competence to respond to bone morphogenetic protein-mediated embryonic
RT induction.";
RL Mech. Dev. 124:840-855(2007).
RN [4] {ECO:0000312|EMBL:AAH55964.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Gastrula {ECO:0000312|EMBL:AAH55964.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305}
RP FUNCTION.
RX PubMed=16860542; DOI=10.1016/j.mod.2006.06.004;
RA Cao Y., Siegel D., Knochel W.;
RT "Xenopus POU factors of subclass V inhibit activin/nodal signaling during
RT gastrulation.";
RL Mech. Dev. 123:614-625(2006).
RN [6] {ECO:0000305}
RP FUNCTION, INTERACTION WITH TCF7L1 AND VEGT, AND TISSUE SPECIFICITY.
RX PubMed=17541407; DOI=10.1038/sj.emboj.7601736;
RA Cao Y., Siegel D., Donow C., Knochel S., Yuan L., Knochel W.;
RT "POU-V factors antagonize maternal VegT activity and beta-Catenin signaling
RT in Xenopus embryos.";
RL EMBO J. 26:2942-2954(2007).
RN [7] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH FOXH1; GTF2IRD1 AND SMAD2.
RX PubMed=18922797; DOI=10.1074/jbc.m803532200;
RA Cao Y., Siegel D., Oswald F., Knochel W.;
RT "Oct25 represses transcription of nodal/activin target genes by interaction
RT with signal transducers during Xenopus gastrulation.";
RL J. Biol. Chem. 283:34168-34177(2008).
CC -!- FUNCTION: Transcription factor that binds to the octamer motif (5'-
CC ATTTGCAT-3'). Activates transcription when directly bound to the
CC octamer DNA sequence, but can form repression complexes with other
CC proteins at the promoter site to inhibit transcription. Binds to the
CC promoter of the vent2-B gene to activate transcription when in the
CC presence of other BMP signaling factors also bound to the promoter.
CC Inhibits the competence of ectodermal cells to respond to BMP during
CC embryogenesis thereby inhibiting epidermal differentiation and
CC promoting neural induction. Antagonizes the activity of nodal/activin
CC signaling by forming a transcriptional repression complex on the gsc
CC and mix2 gene promoters to inhibit their transcription, and thus
CC maintain the undifferentiated state of embryonic cells to prevent them
CC from differentiating prematurely. Acts maternally to inhibit vegt and
CC beta-catenin-activated gene transcription by forming a transcriptional
CC repression complex on the nodal/nr1 and siamois promoters to inhibit
CC their transcription. {ECO:0000269|PubMed:15292233,
CC ECO:0000269|PubMed:16860542, ECO:0000269|PubMed:1732736,
CC ECO:0000269|PubMed:17541407, ECO:0000269|PubMed:17950579,
CC ECO:0000269|PubMed:18922797}.
CC -!- SUBUNIT: Interacts with components of the transcription complex that
CC assembles on the vent2-B gene, including vent2 (via C-terminus), smad1
CC and smad4. Forms a repression complex on the promoters of the gsc and
CC mix2 genes via interactions with the nodal/activin signaling pathway
CC transducers foxh1/fast1, gtf2ird1/wbscr11 and smad2. Forms a repression
CC complex on the promoters of the nodal/nr1 and siamois genes with the
CC maternal factors tcf7l1/tcf3 and vegt. {ECO:0000269|PubMed:15292233,
CC ECO:0000269|PubMed:17541407, ECO:0000269|PubMed:18922797}.
CC -!- INTERACTION:
CC Q7T103; Q90ZB6: tcf7l1-b; NbExp=3; IntAct=EBI-7438970, EBI-7439087;
CC Q7T103; P87377: vegt-a; NbExp=3; IntAct=EBI-7438970, EBI-7439000;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q01860,
CC ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000255|PROSITE-
CC ProRule:PRU00530}.
CC -!- TISSUE SPECIFICITY: Highly enriched within the animal half of
CC developing embryos within ectodermal and mesodermal regions. Expressed
CC in the neuroectoderm at the early neurula stage, with expression
CC initially extending to the future hindbrain/midbrain boundary, but
CC later shifting toward the posterior pole where it persists within the
CC tip of the tail in hatching embryos. Expressed at very low levels in
CC the adult kidney. {ECO:0000269|PubMed:15292233,
CC ECO:0000269|PubMed:1732736, ECO:0000269|PubMed:17541407}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC Expressed in oocytes and cleavage stage embryos. Expression increases
CC during blastula stages, reaches a maximum at stage 11 during
CC gastrulation, then subsequently declines to be no longer detectable by
CC the end of neurulation. {ECO:0000269|PubMed:15292233,
CC ECO:0000269|PubMed:1732736}.
CC -!- SIMILARITY: Belongs to the POU transcription factor family. Class-5
CC subfamily. {ECO:0000255}.
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DR EMBL; M60074; AAA49996.1; -; mRNA.
DR EMBL; AJ699165; CAG27841.1; -; mRNA.
DR EMBL; DQ825761; ABH07383.1; -; mRNA.
DR EMBL; BC055964; AAH55964.1; -; mRNA.
DR PIR; B42022; B42022.
DR RefSeq; NP_001079832.1; NM_001086363.1.
DR AlphaFoldDB; Q7T103; -.
DR SMR; Q7T103; -.
DR IntAct; Q7T103; 2.
DR MINT; Q7T103; -.
DR PRIDE; Q7T103; -.
DR DNASU; 379522; -.
DR GeneID; 379522; -.
DR KEGG; xla:379522; -.
DR CTD; 379522; -.
DR Xenbase; XB-GENE-919851; pou5f3.2.L.
DR OrthoDB; 668779at2759; -.
DR Proteomes; UP000186698; Chromosome 8L.
DR Bgee; 379522; Expressed in gastrula and 8 other tissues.
DR GO; GO:0005634; C:nucleus; IC:UniProtKB.
DR GO; GO:0005667; C:transcription regulator complex; IPI:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0046332; F:SMAD binding; IDA:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007369; P:gastrulation; IMP:UniProtKB.
DR GO; GO:0032926; P:negative regulation of activin receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; IMP:UniProtKB.
DR GO; GO:0045605; P:negative regulation of epidermal cell differentiation; IMP:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0050767; P:regulation of neurogenesis; IMP:UniProtKB.
DR CDD; cd00086; homeodomain; 1.
DR Gene3D; 1.10.260.40; -; 1.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017970; Homeobox_CS.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR InterPro; IPR013847; POU.
DR InterPro; IPR000327; POU_dom.
DR Pfam; PF00046; Homeodomain; 1.
DR Pfam; PF00157; Pou; 1.
DR PRINTS; PR00028; POUDOMAIN.
DR SMART; SM00389; HOX; 1.
DR SMART; SM00352; POU; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF47413; SSF47413; 1.
DR PROSITE; PS00027; HOMEOBOX_1; 1.
DR PROSITE; PS50071; HOMEOBOX_2; 1.
DR PROSITE; PS00465; POU_2; 1.
DR PROSITE; PS51179; POU_3; 1.
PE 1: Evidence at protein level;
KW Activator; Developmental protein; Differentiation; DNA-binding; Homeobox;
KW Nucleus; Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..449
FT /note="POU domain, class 5, transcription factor 1.1"
FT /id="PRO_0000390495"
FT DOMAIN 227..301
FT /note="POU-specific"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00530"
FT DNA_BIND 321..380
FT /note="Homeobox"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 79..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 170..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..115
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 29
FT /note="T -> A (in Ref. 1; AAA49996)"
FT /evidence="ECO:0000305"
FT CONFLICT 71
FT /note="S -> C (in Ref. 1; AAA49996)"
FT /evidence="ECO:0000305"
FT CONFLICT 186
FT /note="T -> A (in Ref. 3; ABH07383)"
FT /evidence="ECO:0000305"
FT CONFLICT 400..401
FT /note="SP -> R (in Ref. 1; AAA49996)"
FT /evidence="ECO:0000305"
FT CONFLICT 428
FT /note="F -> G (in Ref. 1; AAA49996)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 449 AA; 49676 MW; 38430BD13CF4115F CRC64;
MYSQQPFPAF AFNAGLMQDP ANCHFGGYTG LGHPQPFSFA FSTLKSENGE SGVQGMGDCT
TPVMPWNSLA SFDHQVQMEN NQQGNPPRAP SPTLSDSRIK VKEEVVHETD SGEESPEPKY
PSPPNPSLYY PNAWTGAPFW QVNPTPGNNI NPMPNQTLVK NTSLPGNTTY PTPANQSPNT
PVDCVTSSME SSRCSSTNSP NGAINERATT IPNGEMLDGG QSSDNEEEVP SESEMEQFAK
DLKHKRVSLG YTQADVGYAL GVLYGKMFSQ TTICRFESLQ LSFKNMCQLK PFLERWVVEA
ENNDNLQELI NREQVIAQTR KRKRRTNIEN IVKGTLESYF MKCPKPGAQE MVQIAKELNM
DKDVVRVWFC NRRQKGKRQG MPTVEENDGE GYDVAQTMGS PPVGHYALQQ VVTPQGYMAA
PQIYASAFHK NDLFPQTVPH GMAMGGHIG
