PO5F1_PANTR
ID PO5F1_PANTR Reviewed; 360 AA.
AC Q7YR49; Q1XHV2;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 129.
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, OTF3;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12799463; DOI=10.1073/pnas.1230533100;
RA Anzai T., Shiina T., Kimura N., Yanagiya K., Kohara S., Shigenari A.,
RA Yamagata T., Kulski J.K., Naruse T.K., Fujimori Y., Fukuzumi Y.,
RA Yamazaki M., Tashiro H., Iwamoto C., Umehara Y., Imanishi T., Meyer A.,
RA Ikeo K., Gojobori T., Bahram S., Inoko H.;
RT "Comparative sequencing of human and chimpanzee MHC class I regions unveils
RT insertions/deletions as the major path to genomic divergence.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7708-7713(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16702430; DOI=10.1534/genetics.106.057034;
RA Shiina T., Ota M., Shimizu S., Katsuyama Y., Hashimoto N., Takasu M.,
RA Anzai T., Kulski J.K., Kikkawa E., Naruse T., Kimura N., Yanagiya K.,
RA Watanabe A., Hosomichi K., Kohara S., Iwamoto C., Umehara Y., Meyer A.,
RA Wanner V., Sano K., Macquin C., Ikeo K., Tokunaga K., Gojobori T.,
RA Inoko H., Bahram S.;
RT "Rapid evolution of major histocompatibility complex class I genes in
RT primates generates new disease alleles in humans via hitchhiking
RT diversity.";
RL Genetics 173:1555-1570(2006).
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 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 -!- SIMILARITY: Belongs to the POU transcription factor family. Class-5
CC subfamily. {ECO:0000305}.
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DR EMBL; BA000041; BAC78165.1; -; Genomic_DNA.
DR EMBL; AB210197; BAE92816.1; -; Genomic_DNA.
DR EMBL; AB210198; BAE92818.1; -; Genomic_DNA.
DR RefSeq; NP_001238970.1; NM_001252041.1.
DR AlphaFoldDB; Q7YR49; -.
DR SMR; Q7YR49; -.
DR STRING; 9598.ENSPTRP00000030631; -.
DR PaxDb; Q7YR49; -.
DR GeneID; 744263; -.
DR KEGG; ptr:744263; -.
DR CTD; 5460; -.
DR eggNOG; KOG3802; Eukaryota.
DR InParanoid; Q7YR49; -.
DR OrthoDB; 841019at2759; -.
DR TreeFam; TF316413; -.
DR Proteomes; UP000002277; 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 3: Inferred from homology;
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_0000100750"
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..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 88..114
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"
FT CONFLICT 6
FT /note="T -> A (in Ref. 2; BAE92816/BAE92818)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 360 AA; 38601 MW; 375D4ADB3C01348C CRC64;
MAGHLTSDFA FSPPPGGGGD GPGGPEPGWV DPRTWLSFQG PPGGPGIGPG VGPGSEVWGI
PPCPPPYEFC GGMAYCGPQV GVGLVPQGGL ETSQPEGEAG VGVESNSDGA SPEPCTVTPG
AVKLEKEKLE QNPEESQDIK ALQKELEQFA KLLKQKRITL GYTQADVGLT LGVLFGKVFS
QTTICRFEAL QLSFKNMCKL RPLLQKWVEE ADNNENLQEI CKAETLVQAR KRKRTSIENR
VRGNLENLFL QCPKPTLQQI SHIAQQLGLE KDVVRVWFCN RRQKGKRSSS DYAQREDFEA
AGSPFSGGPV SFPLAPGPHF GTPGYGSPHF TALYSSVPFP EGEAFPPVSV TTLGSPMHSN
