PO5F1_MACMU
ID PO5F1_MACMU Reviewed; 360 AA.
AC Q5TM49;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
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 protein 4;
DE Short=Oct-4;
DE AltName: Full=Octamer-binding transcription factor 3;
DE Short=OTF-3;
GN Name=POU5F1; Synonyms=OCT3, OCT4;
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15269276; DOI=10.1093/molbev/msh216;
RA Kulski J.K., Anzai T., Shiina T., Inoko H.;
RT "Rhesus macaque class I duplicon structures, organization, and evolution
RT within the alpha block of the major histocompatibility complex.";
RL Mol. Biol. Evol. 21:2079-2091(2004).
RN [2]
RP BIOTECHNOLOGY, AND FUNCTION.
RX PubMed=19041774; DOI=10.1016/j.stem.2008.10.014;
RA Liu H., Zhu F., Yong J., Zhang P., Hou P., Li H., Jiang W., Cai J., Liu M.,
RA Cui K., Qu X., Xiang T., Lu D., Chi X., Gao G., Ji W., Ding M., Deng H.;
RT "Generation of induced pluripotent stem cells from adult rhesus monkey
RT fibroblasts.";
RL Cell Stem Cell 3:587-590(2008).
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 (By similarity).
CC Critical for early embryogenesis and for embryonic stem cell
CC pluripotency. {ECO:0000250|UniProtKB:Q01860,
CC ECO:0000269|PubMed:19041774}.
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 ZNF322. Interacts with
CC MAPK8 and MAPK9; the interaction allows MAPK8 and MAPK9 to
CC phosphorylate POU5F1 on Ser-355. Interacts (when phosphorylated on Ser-
CC 355) with FBXW8. Interacts with FBXW4. Interacts with SOX2 and SOX15;
CC binds synergistically with either SOX2 or SOX15 to DNA (By similarity).
CC {ECO:0000250|UniProtKB:P20263, 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 -!- 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 -!- BIOTECHNOLOGY: POU5F1/OCT4, SOX2, MYC/c-Myc and KLF4 are the four
CC Yamanaka factors. When combined, these factors are sufficient to
CC reprogram differentiated cells to an embryonic-like state designated
CC iPS (induced pluripotent stem) cells. iPS cells exhibit the morphology
CC and growth properties of ES cells and express ES cell marker genes.
CC {ECO:0000269|PubMed:19041774}.
CC -!- SIMILARITY: Belongs to the POU transcription factor family. Class-5
CC subfamily. {ECO:0000305}.
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DR EMBL; AB128049; BAD69745.1; -; Genomic_DNA.
DR RefSeq; NP_001108427.1; NM_001114955.1.
DR AlphaFoldDB; Q5TM49; -.
DR SMR; Q5TM49; -.
DR STRING; 9544.ENSMMUP00000020598; -.
DR GeneID; 714760; -.
DR KEGG; mcc:714760; -.
DR CTD; 5460; -.
DR eggNOG; KOG3802; Eukaryota.
DR InParanoid; Q5TM49; -.
DR OrthoDB; 841019at2759; -.
DR Proteomes; UP000006718; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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 1: Evidence at protein 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_0000100748"
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..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 87..117
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 MOTIF 4..12
FT /note="9aaTAD"
FT /evidence="ECO:0000250|UniProtKB:Q01860"
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; 38530 MW; C41EDDB07A3980AF CRC64;
MAGHLASDFA FSPPPGGGGD GPGGPETGWV DPRTWLSFQG PPGGPGIGPG VGPGSEVWGI
PPCPPPYEFC GGMAYCGPQV GVGLVPQGGL ETSQPEGEAG AGVESNSDGA SPEPCTVPTG
AVKLEKEKLE QNPEESQDIK ALQKELEQFA KLLKQKRITL GYTQADVGLT LGVLFGKVFS
QTTICRFEAL QLSFKNMCKL RPLLQKWVEE ADNNENLQEI CKAETLVQAR KRKRTSIENR
VRGSLENLFL QCPKPTLQQI SHIAQQLGLE KDVVRVWFCN RRQKGKRSSS DYAQREDFEA
AGSPFSGGPV SFPLAPGPHF GTPGYGSPHF TALYSSVPFP EGEAFPPVPV TTLGSPMHSN
