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   08-NOV-2023, entry version 133.
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       Interacts with DDX56 (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   -!- 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; 9598-ENSPTRP00000030631; -.
DR   GeneID; 744263; -.
DR   KEGG; ptr:744263; -.
DR   CTD; 5460; -.
DR   eggNOG; KOG3802; Eukaryota.
DR   InParanoid; Q7YR49; -.
DR   OrthoDB; 4250502at2759; -.
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: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; 1.10.10.60; Homeodomain-like; 1.
DR   Gene3D; 1.10.260.40; lambda repressor-like DNA-binding domains; 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   PANTHER; PTHR11636; POU DOMAIN; 1.
DR   PANTHER; PTHR11636:SF86; POU DOMAIN, CLASS 5, TRANSCRIPTION FACTOR 1-RELATED; 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; Homeodomain-like; 1.
DR   SUPFAM; SSF47413; lambda repressor-like DNA-binding domains; 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
//