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   27-MAR-2024, entry version 92.
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 Neurula
RC   {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   PaxDb; 8364-ENSXETP00000008656; -.
DR   GeneID; 100170181; -.
DR   KEGG; xtr:100170181; -.
DR   AGR; Xenbase:XB-GENE-919841; -.
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   OMA; HMTHSPL; -.
DR   OrthoDB; 4250502at2759; -.
DR   PhylomeDB; B3DM25; -.
DR   TreeFam; TF316413; -.
DR   Proteomes; UP000008143; Chromosome 8.
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; IEA:InterPro.
DR   GO; GO:0140297; F:DNA-binding transcription factor binding; ISS:UniProtKB.
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:0045892; P:negative regulation of DNA-templated transcription; ISS:UniProtKB.
DR   GO; GO:0045605; P:negative regulation of epidermal cell differentiation; ISS:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISS:UniProtKB.
DR   GO; GO:0050767; P:regulation of neurogenesis; ISS:UniProtKB.
DR   CDD; cd00086; homeodomain; 1.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR   Gene3D; 1.10.260.40; lambda repressor-like DNA-binding domains; 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   PANTHER; PTHR11636:SF137; NETRIN-1-RELATED; 1.
DR   PANTHER; PTHR11636; POU DOMAIN; 1.
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; Homeodomain-like; 1.
DR   SUPFAM; SSF47413; lambda repressor-like DNA-binding domains; 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
//