P5F13_XENLA
ID P5F13_XENLA Reviewed; 426 AA.
AC Q91989; Q03916;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=POU domain, class 5, transcription factor 1.3;
DE AltName: Full=POU class V protein oct-60 {ECO:0000303|PubMed:16860542};
DE Short=XOct-60 {ECO:0000303|PubMed:1732736};
DE Short=XlPOU-60;
GN Name=pou5f1.3; Synonyms=oct-60 {ECO:0000312|EMBL:AAA49997.1};
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:AAA49997.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DNA-BINDING, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL 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:CAA60136.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Oocyte {ECO:0000269|PubMed:8432392};
RX PubMed=8432392; DOI=10.1006/dbio.1993.1035;
RA Whitfield T., Heasman J., Wylie C.;
RT "XLPOU-60, a Xenopus POU-domain mRNA, is oocyte-specific from very early
RT stages of oogenesis, and localised to presumptive mesoderm and ectoderm in
RT the blastula.";
RL Dev. Biol. 155:361-370(1993).
RN [3] {ECO:0000312|EMBL:AAH70557.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney {ECO:0000312|EMBL:AAH70557.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305}
RP FUNCTION, DNA-BINDING, AND RNA-BINDING.
RX PubMed=7582913; DOI=10.1017/s0967199400002483;
RA Guttridge K.L., Smith L.D.;
RT "Xenopus interspersed RNA families, Ocr and XR, bind DNA-binding
RT proteins.";
RL Zygote 3:111-122(1995).
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).
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. Acts maternally
CC to inhibit vegt and beta-catenin-activated gene transcription, probably
CC by forming a transcriptional repression complex on the promoters of
CC target genes. Binds to an octamer motif in interspersed RNA.
CC {ECO:0000269|PubMed:16860542, ECO:0000269|PubMed:1732736,
CC ECO:0000269|PubMed:17541407, ECO:0000269|PubMed:7582913}.
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: Expressed in the animal half of oocytes and remains
CC localized to the animal cap and marginal zone of blastula embryos.
CC Expressed in the adult ovary and at a very low level in the adult
CC kidney. Absent from primordial germ cells (PGCs).
CC {ECO:0000269|PubMed:1732736, ECO:0000269|PubMed:17541407,
CC ECO:0000269|PubMed:8432392}.
CC -!- DEVELOPMENTAL STAGE: Expressed maternally. Most abundant in oocytes and
CC fertilized eggs, with expression maintained through the cleavage stages
CC of development until early gastrulation. Expression levels drop
CC abruptly during gastrulation (stage 11) but remain at very low levels
CC through larval stages. {ECO:0000269|PubMed:1732736,
CC ECO:0000269|PubMed:8432392}.
CC -!- SIMILARITY: Belongs to the POU transcription factor family. Class-5
CC subfamily. {ECO:0000255}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M60075; AAA49997.1; -; mRNA.
DR EMBL; X86377; CAA60136.1; -; mRNA.
DR EMBL; BC070557; AAH70557.1; -; mRNA.
DR PIR; A48829; A48829.
DR RefSeq; NP_001081583.1; NM_001088114.1.
DR AlphaFoldDB; Q91989; -.
DR SMR; Q91989; -.
DR DNASU; 397936; -.
DR GeneID; 397936; -.
DR KEGG; xla:397936; -.
DR CTD; 397936; -.
DR Xenbase; XB-GENE-5903594; pou5f3.3.L.
DR OrthoDB; 668779at2759; -.
DR Proteomes; UP000186698; Chromosome 8L.
DR Bgee; 397936; Expressed in blastula and 9 other 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:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA 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:0032926; P:negative regulation of activin receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
DR CDD; cd00086; homeodomain; 1.
DR CDD; cd00093; HTH_XRE; 1.
DR Gene3D; 1.10.260.40; -; 1.
DR InterPro; IPR001387; Cro/C1-type_HTH.
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 Developmental protein; Differentiation; DNA-binding; Homeobox; Nucleus;
KW Reference proteome; RNA-binding; Transcription; Transcription regulation.
FT CHAIN 1..426
FT /note="POU domain, class 5, transcription factor 1.3"
FT /id="PRO_0000390934"
FT DOMAIN 202..276
FT /note="POU-specific"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00530"
FT DNA_BIND 296..355
FT /note="Homeobox"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 82..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 140..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 140
FT /note="A -> P (in Ref. 1; AAA49997)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 426 AA; 47253 MW; D8C2D596B3BD56C7 CRC64;
MDQPILYSQT SFPNFTYSPG VVQDGGNYQY LGNYNAPSYP QPFFHVPVIK SEFGAHEEET
PGSCHAASFD WNLYPHFQIS NQAASNSSGD PSPEGRTEED GSVSEGRSSS SPSPNSPLVP
SFAQYWHYPS WQQGNLTNQA HTLFDGGDEK PQQSRHSPTA SLGSGASNTE DEEVPSAISS
RAERGLCSPS PNNASCGPGT EEDGMTLEEM EEFAKELKQK RVALGYTQGD IGHALGILYG
KMFSQTTICR FESLQLTFKN MCKLKPLLEQ WLGEAENNDN LQEMIHKAQI EEQNRKRKMR
TCFDTVLKGQ LEGHFMCNQK PGARELTEIA KELSLEKDVV RVWFCNRRQK EKSKFRMSKG
HEFVGGASPG SIQSEHISFT PIPANSQDYG LASLHPNRAP FYPPPFPRNE LFPHMAPGIS
MGVLTG
