ID   P5F12_XENLA             Reviewed;         445 AA.
AC   B7ZQA9; Q03917; Q9PSI7;
DT   15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   RecName: Full=POU domain, class 5, transcription factor 1.2;
DE   AltName: Full=POU class V protein oct-91 {ECO:0000303|PubMed:16860542};
DE            Short=XlPOU91;
DE            Short=Xoct-91 {ECO:0000312|EMBL:AAI69741.1};
GN   Name=pou5f1.2; Synonyms=oct-91 {ECO:0000312|EMBL:AAI69741.1};
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:AAA49999.1}
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:0000312|EMBL:AAI69741.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Gastrula {ECO:0000312|EMBL:AAI69741.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 236-362, TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RC   TISSUE=Gastrula {ECO:0000269|PubMed:1358592};
RX   PubMed=1358592; DOI=10.1242/dev.115.2.439;
RA   Frank D., Harland R.M.;
RT   "Localized expression of a Xenopus POU gene depends on cell-autonomous
RT   transcriptional activation and induction-dependent inactivation.";
RL   Development 115:439-448(1992).
RN   [4] {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   [5] {ECO:0000305}
RP   INTERACTION WITH TCF7L1 AND VEGT.
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).
CC   -!- FUNCTION: Transcription factor that binds to the octamer motif (5'-
CC       ATTTGCAT-3'). Antagonizes the activity of nodal/activin signaling
CC       during gastrulation to suppress mesendoderm formation.
CC       {ECO:0000269|PubMed:16860542, ECO:0000269|PubMed:1732736}.
CC   -!- SUBUNIT: Interacts with the transcription factors tcf7l1/tcf3 and vegt.
CC       {ECO:0000269|PubMed:17541407}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q01860,
CC       ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000255|PROSITE-
CC       ProRule:PRU00530}.
CC   -!- TISSUE SPECIFICITY: Initially (stage 9) expressed in all regions of the
CC       embryo, becoming localized to the ventroposterior regions by early
CC       neurula stages. In adults, expressed at a low level in the brain.
CC       {ECO:0000269|PubMed:1358592, ECO:0000269|PubMed:1732736}.
CC   -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC       Expressed at low levels in oocytes, with expression increasing rapidly
CC       during gastrulation and peaking during late gastrulation before
CC       declining through neurulation. {ECO:0000269|PubMed:1358592,
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; M60077; AAA49999.1; -; mRNA.
DR   EMBL; BC169741; AAI69741.1; -; mRNA.
DR   EMBL; BC169743; AAI69743.1; -; mRNA.
DR   PIR; C42022; C42022.
DR   RefSeq; NP_001081342.1; NM_001087873.1.
DR   AlphaFoldDB; B7ZQA9; -.
DR   SMR; B7ZQA9; -.
DR   IntAct; B7ZQA9; 2.
DR   MINT; B7ZQA9; -.
DR   GeneID; 397784; -.
DR   KEGG; xla:397784; -.
DR   AGR; Xenbase:XB-GENE-6252587; -.
DR   CTD; 397784; -.
DR   Xenbase; XB-GENE-6252587; pou5f3.L.
DR   OMA; KNDMFPQ; -.
DR   OrthoDB; 4250502at2759; -.
DR   Proteomes; UP000186698; Chromosome 8L.
DR   Bgee; 397784; Expressed in gastrula and 11 other cell types or tissues.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0007369; P:gastrulation; IMP: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   1: Evidence at protein level;
KW   DNA-binding; Homeobox; Nucleus; Reference proteome.
FT   CHAIN           1..445
FT                   /note="POU domain, class 5, transcription factor 1.2"
FT                   /id="PRO_0000390497"
FT   DOMAIN          218..292
FT                   /note="POU-specific"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00530"
FT   DNA_BIND        312..371
FT                   /note="Homeobox"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT   REGION          76..116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          139..227
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        90..107
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        165..219
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        248
FT                   /note="G -> A (in Ref. 3)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        295
FT                   /note="E -> K (in Ref. 1; AAA49999)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        333
FT                   /note="Q -> G (in Ref. 3)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   445 AA;  49036 MW;  C981C1F3A2EDA93C CRC64;
     MYNQQTYPSF THNPALMPDG SGQYNLGTYT GMARHPHQAQ AFFPFSGVKS DYGDLGGQTT
     SVGDTSAWNP LTSLDSANQL GISGQGNPFK NLKREREDDE EKSESPEPKC SPPSLPPAYY
     THAWNPTTTF WSQVSSSGTT VVSKPLPTPL QPGDKCDPVE ANKIFTSSPD KSGESGISSL
     DNSRCSSATS SSSGGTNVGT PRSLSRGASD GLSSDSEEEA PNSGEMEQFA KDLKHKRITM
     GYTQADVGYA LGVLFGKTFS QTTICRFESL QLSFKNMCKL KPLLRSWLHE VENNENLQEI
     ISRGQIIPQV QKRKHRTSIE NNVKCTLENY FMQCSKPSAQ EIAQIARELN MEKDVVRVWF
     CNRRQKGKRQ VYPYIRENGG EPYDAPQTLT PPSQGPFPLP QVMPSQVFPT VPLGANPTIY
     VPTYHKNDMF PQAMHHGIGM GNQGN
//