PO2F1_XENLA
ID PO2F1_XENLA Reviewed; 758 AA.
AC P16143; Q01236; Q91809;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2009, sequence version 3.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=POU domain, class 2, transcription factor 1;
DE AltName: Full=Octamer-binding protein 1;
DE Short=Oct-1;
DE Short=XOct1;
DE AltName: Full=Octamer-binding transcription factor 1;
DE Short=OTF-1;
DE AltName: Full=Xloct1-32;
GN Name=pou2f1; Synonyms=oct-1, oct1, oct1.32;
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]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Oocyte;
RX PubMed=2326173; DOI=10.1093/nar/18.2.369;
RA Smith D.P., Old R.W.;
RT "Nucleotide sequence of Xenopus laevis Oct-1 cDNA.";
RL Nucleic Acids Res. 18:369-369(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Hinkley C., Leibham D., Perry M.;
RT "Regulated binding specificity of Xenopus OCT-1, a maternal transcription
RT factor.";
RL Submitted (JAN-1991) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 261-335.
RA Schilthuis J.G., Baarends W.M., Peterson-Maduro J., Destre O.H.J.;
RL Submitted (FEB-1990) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 320-433 (ISOFORM 2).
RC TISSUE=Neurula;
RX PubMed=2235499; DOI=10.1093/nar/18.20.6131;
RA Baltzinger M., Stiegler P., Remy P.;
RT "Cloning and sequencing of POU-boxes expressed in Xenopus laevis neurula
RT embryos.";
RL Nucleic Acids Res. 18:6131-6131(1990).
RN [5]
RP FUNCTION.
RX PubMed=1990276; DOI=10.1128/mcb.11.2.641-654.1991;
RA Hinkley C., Perry M.;
RT "A variant octamer motif in a Xenopus H2B histone gene promoter is not
RT required for transcription in frog oocytes.";
RL Mol. Cell. Biol. 11:641-654(1991).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=2017364; DOI=10.1093/nar/19.4.815;
RA Smith D.P., Old R.W.;
RT "Xenopus laevis Oct-1 does not bind to certain histone H2B gene promoter
RT octamer motifs for which a novel octamer-binding factor has high
RT affinity.";
RL Nucleic Acids Res. 19:815-821(1991).
RN [7]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
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 [8]
RP FUNCTION.
RX PubMed=1406629; DOI=10.1128/mcb.12.10.4400-4411.1992;
RA Hinkley C., Perry M.;
RT "Histone H2B gene transcription during Xenopus early development requires
RT functional cooperation between proteins bound to the CCAAT and octamer
RT motifs.";
RL Mol. Cell. Biol. 12:4400-4411(1992).
RN [9]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=7542467; DOI=10.1016/0925-4773(94)00328-k;
RA Veenstra G.J., Beumer T.L., Peterson-Maduro J., Stegeman B.I., Karg H.A.,
RA van der Vliet P.C., Destree O.H.;
RT "Dynamic and differential Oct-1 expression during early Xenopus
RT embryogenesis: persistence of Oct-1 protein following down-regulation of
RT the RNA.";
RL Mech. Dev. 50:103-117(1995).
RN [10]
RP FUNCTION.
RX PubMed=10200537; DOI=10.1038/sj.cdd.4400416;
RA Veenstra G.J., Peterson-Maduro J., Mathu M.T., van der Vliet P.C.,
RA Destree O.H.;
RT "Non-cell autonomous induction of apoptosis and loss of posterior
RT structures by activation domain-specific interactions of Oct-1 in the
RT Xenopus embryo.";
RL Cell Death Differ. 5:774-784(1998).
RN [11]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DOMAIN.
RX PubMed=10195432; DOI=10.1515/bc.1999.033;
RA Veenstra G.J., Mathu M.T., Destree O.H.;
RT "The Oct-1 POU domain directs developmentally regulated nuclear
RT translocation in Xenopus embryos.";
RL Biol. Chem. 380:253-257(1999).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=18241856; DOI=10.1016/j.ydbio.2007.12.013;
RA Kiyota T., Kato A., Altmann C.R., Kato Y.;
RT "The POU homeobox protein Oct-1 regulates radial glia formation downstream
RT of Notch signaling.";
RL Dev. Biol. 315:579-592(2008).
CC -!- FUNCTION: Transcription factor that binds to the octamer motif (5'-
CC ATTTGCAT-3') and activates the promoters of the genes for some small
CC nuclear RNAs (snRNA) and histone H2B. Acts downstream of Notch
CC signaling during radial glia formation. Regulates apoptosis, possibly
CC via an FGF-signaling pathway. {ECO:0000269|PubMed:10200537,
CC ECO:0000269|PubMed:1406629, ECO:0000269|PubMed:1732736,
CC ECO:0000269|PubMed:18241856, ECO:0000269|PubMed:1990276,
CC ECO:0000269|PubMed:2017364}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Retained in the
CC cytoplasm during early development, then gradually translocates to the
CC nucleus around the mid-blastula transition (MBT).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P16143-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P16143-2; Sequence=VSP_038472;
CC -!- TISSUE SPECIFICITY: Abundant in the animal hemisphere of the blastula
CC embryo and during early embryogenesis. Expressed in ectodermal and
CC mesodermal cell lineages where expression becomes spatially restricted
CC to the developing nervous system as development progresses (at protein
CC level). Expressed in the neural plate at late neurula stage (stage 17).
CC At early tailbud stage (stage 25), expression continues in the neural
CC tube and begins in the eyes. At late tailbud stages (stage 30),
CC expressed broadly in the CNS. {ECO:0000269|PubMed:10195432,
CC ECO:0000269|PubMed:18241856, ECO:0000269|PubMed:7542467}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC {ECO:0000269|PubMed:1732736, ECO:0000269|PubMed:2017364,
CC ECO:0000269|PubMed:7542467}.
CC -!- DOMAIN: The POU domain controls nuclear translocation.
CC {ECO:0000269|PubMed:10195432}.
CC -!- SIMILARITY: Belongs to the POU transcription factor family. Class-2
CC subfamily. {ECO:0000305}.
CC -!- CAUTION: PubMed:2017364 and PubMed:1990276 show that although pou2f1
CC binds well to a perfect octamer motif, it does not bind to the variant
CC octamer motif most often found in Xenopus laevis histone H2B gene
CC promoters. PubMed:1406629 therefore suggest that interactions between
CC pou2f1 and other factors bound to the H2B octamer are required for
CC octamer-dependent H2B transcription. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA36119.1; Type=Miscellaneous discrepancy; Note=Unidentified sequence at N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X17190; CAA35051.1; -; mRNA.
DR EMBL; X57165; CAA40454.1; -; mRNA.
DR EMBL; X51819; CAA36119.1; ALT_SEQ; Genomic_DNA.
DR EMBL; X54683; CAA38497.1; -; mRNA.
DR PIR; S07896; S07896.
DR RefSeq; NP_001095255.1; NM_001101785.1. [P16143-1]
DR AlphaFoldDB; P16143; -.
DR SMR; P16143; -.
DR GeneID; 399316; -.
DR KEGG; xla:399316; -.
DR CTD; 399316; -.
DR Xenbase; XB-GENE-853997; pou2f1.S.
DR OrthoDB; 873012at2759; -.
DR Proteomes; UP000186698; Chromosome 2S.
DR Bgee; 399316; Expressed in blastula and 12 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
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:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0007219; P:Notch signaling pathway; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0060019; P:radial glial cell differentiation; IMP:UniProtKB.
DR GO; GO:0042981; P:regulation of apoptotic process; 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; IPR045703; POU2F1_C.
DR InterPro; IPR000327; POU_dom.
DR InterPro; IPR000972; TF_octamer.
DR Pfam; PF00046; Homeodomain; 1.
DR Pfam; PF00157; Pou; 1.
DR Pfam; PF19536; POU2F1_C; 1.
DR PRINTS; PR00029; OCTAMER.
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; PS00035; POU_1; 1.
DR PROSITE; PS00465; POU_2; 1.
DR PROSITE; PS51179; POU_3; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Cytoplasm; Developmental protein;
KW DNA-binding; Homeobox; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..758
FT /note="POU domain, class 2, transcription factor 1"
FT /id="PRO_0000100713"
FT DOMAIN 294..368
FT /note="POU-specific"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00530"
FT DNA_BIND 395..454
FT /note="Homeobox"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 271..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 450..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 534..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..472
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 368
FT /note="E -> VLE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:2235499,
FT ECO:0000303|PubMed:2326173"
FT /id="VSP_038472"
FT CONFLICT 157
FT /note="S -> N (in Ref. 1; CAA35051)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 758 AA; 78858 MW; 807E21D83DA1985F CRC64;
MKLHSSSKIQ NHAWLSDARM NNPSETSKSP ESGDGNTGTQ TNGLDFQKQA VPIGAITSAQ
AQALLGHLHQ VQLAGTSLQA AAHSLNVQTK FKEEPGEPMQ VVQPSQQPSL QAAIPQTQLM
VAGGQIAGLT LTPAQQQMLL QQAQAQLLAA AVQHSASQQH NAAGATISAS AATPMTQIPL
SQPIQIAQDL QQLQQLQQQN LNLQQYVLVH PTTNLQSAQF IISQTPQGQQ GLLQAQNLLT
QLPQQSQANL LQSQPSITLT SQPATPTRTI AATPVQQLPQ SQTTPKRIDT PSLEEPSDLE
ELEQFAKTFK QRRIKLGFTQ GDVGLAMGKL YGNDFSQTTI SRFEALNLSF KNMCKLKPLL
EKWLNDAENI TSDSTLTNQS VLNSPGHGME GLNRRRKKRT SIETNIRVAL EKSFLENQKP
TSEEITMIAD QLNMEKEVIR VWFCNRRQKE KRINPPSSGG SSSSPIKSLF SSPNPLVAST
PSLVTSSPAT TLTVNPVLPL TSAAAITSFH IPGTTGTSSA NTATVISTAP PVSSVLTSPS
LSSSPSATAA SSEASTAGET STTQTTSTPM TSSLNTGQVM VTASGIHTAA ATALQGAAQL
PTNASLAAMA AAAGLNPGLM APSQFAAGGA LFSLNPGALG SALSPALMSN STLATIQALA
SSGSLPITSL DAAGNLVFAN AGGTPNIVTA PLFLNPQNLS LFTSNPVSLI SAASAGATGP
ITSLHATTSS IDSIQNALFT MASASGAAST TTSASKAQ
