P5F11_XENTR
ID P5F11_XENTR Reviewed; 459 AA.
AC B3DM25; B3DM50;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=POU domain, class 5, transcription factor 1.1;
DE AltName: Full=POU class V protein oct-25 {ECO:0000250|UniProtKB:Q7T103};
GN Name=pou5f1.1 {ECO:0000312|EMBL:AAI67674.1};
GN Synonyms=oct25 {ECO:0000250|UniProtKB:Q7T103};
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:AAI67674.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Gastrula {ECO:0000312|EMBL:AAI67674.1}, and
RC Neurula {ECO:0000312|EMBL:AAI67702.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250|UniProtKB:Q7T103}.
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 (By similarity).
CC {ECO:0000250|UniProtKB:Q7T103}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q01860,
CC ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000255|PROSITE-
CC ProRule:PRU00530}.
CC -!- SIMILARITY: Belongs to the POU transcription factor family. Class-5
CC subfamily. {ECO:0000255}.
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DR EMBL; BC167674; AAI67674.1; -; mRNA.
DR EMBL; BC167702; AAI67702.1; -; mRNA.
DR RefSeq; NP_001123406.1; NM_001129934.1.
DR AlphaFoldDB; B3DM25; -.
DR SMR; B3DM25; -.
DR STRING; 8364.ENSXETP00000008656; -.
DR PaxDb; B3DM25; -.
DR GeneID; 100170181; -.
DR KEGG; xtr:100170181; -.
DR CTD; 100170181; -.
DR Xenbase; XB-GENE-919841; pou5f3.2.
DR eggNOG; KOG3802; Eukaryota.
DR HOGENOM; CLU_043154_0_0_1; -.
DR InParanoid; B3DM25; -.
DR OrthoDB; 668779at2759; -.
DR PhylomeDB; B3DM25; -.
DR TreeFam; TF316413; -.
DR Proteomes; UP000008143; Chromosome 8.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005667; C:transcription regulator complex; ISS:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISS:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0046332; F:SMAD binding; ISS:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007369; P:gastrulation; ISS:UniProtKB.
DR GO; GO:0032926; P:negative regulation of activin receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; ISS:UniProtKB.
DR GO; GO:0045605; P:negative regulation of epidermal cell differentiation; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0050767; P:regulation of neurogenesis; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Activator; Developmental protein; Differentiation; DNA-binding; Homeobox;
KW Nucleus; Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..459
FT /note="POU domain, class 5, transcription factor 1.1"
FT /id="PRO_0000390496"
FT DOMAIN 232..306
FT /note="POU-specific"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00530"
FT DNA_BIND 326..385
FT /note="Homeobox"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 78..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 216..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..98
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..117
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 17
FT /note="I -> M (in Ref. 1; AAI67702)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 459 AA; 50320 MW; 1CB1FA5F6F0D39C8 CRC64;
MYSQQPFPPF AFNAGLIQDP ANCHFGGYTG LGHPQPFSFA FSTLKSENGD SGVQGMGDCS
APVMPWNSMA SFDHHGQVET NQQGNPIRAP SPTPTLSDSR IKVKEEVAHE TDSGEESPEP
KYPSPPNPSL YYPNTWTGSP FWQVNPTAGN NSNSTNPMPS QTLVKNGSLP GNTTYPTPAN
QSPNTPVDCV VSSMESSRCS SANSSNGAIN ERATTIPNGG MVDGGQSSDN EEEVPSESEM
EQFAKDLKHK RVSMGYTQAD VGYALGVLYG KMFSQTTICR FESLQLSFKN MCQLKPFLER
WLVEAENNDN LQELINREQV IAQTRKRKRR TNIENIVKGT LESYFMKCSK PGAQEMVQIA
KELNMDKDVV RVWFCNRRQK GKRQGMPTVD ENDGEGYDVG QTMASPPVGH YSLPQVVTSQ
GYMAAPLGST PPLYASAFHK NELFPQPLPH AMPMGGHIG
