PO5F1_BOVIN
ID PO5F1_BOVIN Reviewed; 360 AA.
AC O97552;
DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=POU domain, class 5, transcription factor 1;
DE AltName: Full=Octamer-binding protein 3;
DE Short=Oct-3;
DE AltName: Full=Octamer-binding transcription factor 3;
DE Short=OTF-3;
GN Name=POU5F1; Synonyms=OCT3;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX PubMed=10208969; DOI=10.1095/biolreprod60.5.1093;
RA van Eijk M.J.T., van Rooijen M.A., Modina S., Scesi L., Folkers G.,
RA van Tol H.T.A., Bevers M.M., Fisher S.R., Lewin H.A., Shehu D., Galli C.,
RA de Vaureix C., Trounson A.O., Mummery C.L., Gandolfi F.;
RT "Molecular cloning, genetic mapping, and developmental expression of bovine
RT POU5F1.";
RL Biol. Reprod. 60:1093-1103(1999).
CC -!- FUNCTION: Transcription factor that binds to the octamer motif (5'-
CC ATTTGCAT-3'). Forms a trimeric complex with SOX2 or SOX15 on DNA and
CC controls the expression of a number of genes involved in embryonic
CC development such as YES1, FGF4, UTF1 and ZFP206. Critical for early
CC embryogenesis and for embryonic stem cell pluripotency (By similarity).
CC {ECO:0000250|UniProtKB:Q01860}.
CC -!- SUBUNIT: Interacts with PKM. Interacts with WWP2. Interacts with UBE2I
CC and ZSCAN10. Interacts with PCGF1. Interacts with ESRRB; recruits ESRRB
CC near the POU5F1-SOX2 element in the NANOG proximal promoter; the
CC interaction is DNA independent. Interacts with MAPK8 and MAPK9; the
CC interaction allows MAPK8 and MAPK9 to phosphorylate POU5F1 on Ser-355.
CC Interacts (when phosphorylated on Ser-355) with FBXW8. Interacts with
CC FBXW4. Interacts with SOX2 and SOX15; binds synergistically with either
CC SOX2 or SOX15 to DNA (By similarity). {ECO:0000250|UniProtKB:P20263,
CC ECO:0000250|UniProtKB:Q01860}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Expressed in a diffuse
CC and slightly punctuate pattern. Colocalizes with MAPK8 and MAPK9 in the
CC nucleus. {ECO:0000250|UniProtKB:P20263, ECO:0000250|UniProtKB:Q01860}.
CC -!- TISSUE SPECIFICITY: Expressed in immature oocytes.
CC {ECO:0000269|PubMed:10208969}.
CC -!- DOMAIN: The POU-specific domain mediates interaction with PKM.
CC {ECO:0000250|UniProtKB:Q01860}.
CC -!- DOMAIN: The 9aaTAD motif is a transactivation domain present in a large
CC number of yeast and animal transcription factors.
CC {ECO:0000250|UniProtKB:Q01860}.
CC -!- PTM: Sumoylation enhances the protein stability, DNA binding and
CC transactivation activity. Sumoylation is required for enhanced YES1
CC expression. {ECO:0000250|UniProtKB:P20263}.
CC -!- PTM: Ubiquitinated; undergoes 'Lys-63'-linked polyubiquitination by
CC WWP2 leading to proteasomal degradation.
CC {ECO:0000250|UniProtKB:P20263}.
CC -!- PTM: ERK1/2-mediated phosphorylation at Ser-111 promotes nuclear
CC exclusion and proteasomal degradation. Phosphorylation at Thr-235 and
CC Ser-236 decrease DNA-binding and alters ability to activate
CC transcription. {ECO:0000250|UniProtKB:Q01860}.
CC -!- SIMILARITY: Belongs to the POU transcription factor family. Class-5
CC subfamily. {ECO:0000305}.
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DR EMBL; AF022987; AAD01757.1; -; Genomic_DNA.
DR EMBL; AF022986; AAD01757.1; JOINED; Genomic_DNA.
DR AlphaFoldDB; O97552; -.
DR SMR; O97552; -.
DR STRING; 9913.ENSBTAP00000028122; -.
DR PaxDb; O97552; -.
DR PRIDE; O97552; -.
DR eggNOG; KOG3802; Eukaryota.
DR InParanoid; O97552; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
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 InterPro; IPR015585; POU_dom_5.
DR PANTHER; PTHR11636:SF86; PTHR11636:SF86; 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; 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 2: Evidence at transcript level;
KW Cytoplasm; Developmental protein; DNA-binding; Homeobox; Isopeptide bond;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..360
FT /note="POU domain, class 5, transcription factor 1"
FT /id="PRO_0000100746"
FT DOMAIN 138..212
FT /note="POU-specific"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00530"
FT DNA_BIND 230..289
FT /note="Homeobox"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 86..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 180..186
FT /note="DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P20263"
FT REGION 193..196
FT /note="DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P20263"
FT REGION 287..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 4..12
FT /note="9aaTAD"
FT /evidence="ECO:0000250|UniProtKB:Q01860"
FT COMPBIAS 123..137
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 157
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000250|UniProtKB:P20263"
FT BINDING 164
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000250|UniProtKB:P20263"
FT MOD_RES 111
FT /note="Phosphoserine; by MAPK"
FT /evidence="ECO:0000250|UniProtKB:Q01860"
FT MOD_RES 235
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q01860"
FT MOD_RES 236
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01860"
FT MOD_RES 289
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01860"
FT MOD_RES 290
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01860"
FT MOD_RES 355
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20263"
FT CROSSLNK 123
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250|UniProtKB:P20263"
SQ SEQUENCE 360 AA; 38289 MW; DF0A326BE6329F08 CRC64;
MAGHLASDFA FSPPPGGGGD GPGGPEPGWV DPRTWMSFQG PPGGSGIGPG VVPGAEVWGL
PPCPPPYDLC GGMAYCAPQV GVGPVPPGGL ETPQPEGEAG AGVESNSEGA SPDPCAAPAG
APKLDKEKLE PNPEESQDIK ALQKDLEQFA KLLKQKRITL GYTQADVGLT LGVLFGKVFS
QTTICRFEAL QLSFKNMCKL RPLLQKWVEE ADNNENLQEI CKAETLVQAR KRKRTSIENR
VRGNLESMFL QCPKPTLQQI SHIAQQLGLE KDVVRVWFCN RRQKGKRSSS DYSQREDFEA
AGSPFTGGPV SSPLAPGPHF GTPGYGGPHF TTLYSSVPFP EGEVFPSVSV TALGSPMHAN
