POU domain, class 5, transcription factor 1

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Reviewed, UniProtKB/Swiss-Prot P20263 (PO5F1_MOUSE)

Last modified November 3, 2009. Version 101. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    POU domain, class 5, transcription factor 1
Alternative name(s):
    Octamer-binding transcription factor 3
      Short name=Oct-3
    Oct-4
    NF-A3

Gene names

Name:	Pou5f1
Synonyms:	Oct-3, Oct-4, Otf-3, Otf3

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length	352 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Transcription factor that binds to the octamer motif (5'-ATTTGCAT-3'). Forms a trimeric complex with SOX2 on DNA and controls the expression of a number of genes involved in embryonic development such as YES1, FGF4, UTF1 and ZFP206. Critical for early embryogenesis and for embryonic stem cell pluripotency. Ref.7 Ref.8
Subunit structure	Interacts with PKM2 By similarity. Interacts with UBE2I.
Subcellular location	Nucleus. Note: Expressed in a diffuse and slightly punctuate pattern. Ref.7 Ref.8
Tissue specificity	Expressed the totipotent and pluripotent stem cells of the pregastrulation embryo. Also expressed in primordial germ cells and in the female germ line. Absent from adult tissues. Ref.1 Ref.2
Developmental stage	Down-regulated during differentiation to endoderm and mesoderm. Ref.1
Induction	Repressed by retinoic acid (RA). Ref.2 Ref.4
Domain	The POU-specific domain mediates interaction with PKM2 By similarity.
Post-translational modification	Sumoylation enhances the protein stability, DNA binding and transactivation activity. Sumoylation is required for enhanced YES1 expression.
Sequence similarities	Belongs to the POU transcription factor family. Class-5 subfamily. Contains 1 homeobox DNA-binding domain. Contains 1 POU-specific domain.

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Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Domain	Homeobox
Ligand	DNA-binding
PTM	Isopeptide bond Ubl conjugation
Technical term	3D-structure
Gene Ontology (GO)
Biological process	ectodermal cell fate commitment Inferred from direct assay. Source: MGI endodermal cell fate commitment Inferred from direct assay. Source: MGI germ-line stem cell maintenance Inferred from mutant phenotype. Source: MGI mesodermal cell fate commitment Inferred from direct assay. Source: MGI negative regulation of calcium ion-dependent exocytosis Inferred from direct assay. Source: MGI negative regulation of transcription from RNA polymerase II promoter Inferred from genetic interaction. Source: MGI positive regulation of transcription from RNA polymerase II promoter Ref.1 Ref.6 Inferred from direct assay. Source: MGI response to retinoic acid Inferred from direct assay. Source: MGI transcription from RNA polymerase II promoter Ref.3 Inferred from direct assay. Source: MGI trophectodermal cell differentiation Inferred from genetic interaction. Source: MGI
Cellular component	cytoplasm Inferred from direct assay. Source: MGI transcription factor complex Inferred from direct assay. Source: MGI transcriptional repressor complex Inferred from direct assay. Source: MGI
Molecular function	chromatin binding Inferred from direct assay. Source: MGI sequence-specific DNA binding Ref.2 Inferred from direct assay. Source: MGI transcription corepressor activity Inferred from direct assay. Source: MGI transcription factor activity Ref.1 Ref.3 Inferred from direct assay. Source: MGI
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct
Ewsr1	Q61545	7	EBI-1606219,EBI-1606991
Nanog	Q80Z64	3	EBI-1606219,EBI-2312517
Nr0b1	Q61066	1	EBI-1606219,EBI-2312665
Pkm2	P52480	4	EBI-1606219,EBI-647785

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 352

352

POU domain, class 5, transcription factor 1

PRO_0000100749

Regions

Domain

131 – 205

POU-specific

DNA binding

223 – 282

Homeobox

Amino acid modifications

Cross-link

118

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.7 Ref.8 Ref.6

Experimental info

Mutagenesis

118

K → R: Absence of sumoylation. Enhanced protein degradation. Reduced self-renewal ability in ES cells. 70% lower expression of YES1. Reduced DNA binding. No change in nuclear location. No change in nuclear localization. Absence of sumoylation; when associated with R-215 and R-244. Ref.7 Ref.8 Ref.6

Mutagenesis

120

E → A: Absence of sumoylation. Enhanced protein degradation. Reduced self-renewal ability in ES cells. 55% lower expression of YES1. Ref.7

Mutagenesis

215

K → R: No change in sumoylation; when associated with R-244. Loss of sumoylation. No change in nuclear localization; when associated with R-118 and R-244. Ref.7

Mutagenesis

244

K → R: No change in sumoylation. No change in sumoylation; when associated with R-215. Loss of sumoylation; when associated with R-118 and R-215. No change in nuclear localization; when associated with R-118 and R-215. Ref.7

Sequence conflict

1 – 28

Missing in CAA36682. Ref.2

Sequence conflict

V → M in CAA36682. Ref.2

Sequence conflict

P → S in AAA39844. Ref.4

Sequence conflict

P → S in AAB19896. Ref.4

Secondary structure

352

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P20263-1 [UniParc].

Last modified February 1, 1991. Version 1.
Checksum: 757E41DF52286714
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FASTA

352

38,216

        10         20         30         40         50         60 
MAGHLASDFA FSPPPGGGDG SAGLEPGWVD PRTWLSFQGP PGGPGIGPGS EVLGISPCPP 

        70         80         90        100        110        120 
AYEFCGGMAY CGPQVGLGLV PQVGVETLQP EGQAGARVES NSEGTSSEPC ADRPNAVKLE 

       130        140        150        160        170        180 
KVEPTPEESQ DMKALQKELE QFAKLLKQKR ITLGYTQADV GLTLGVLFGK VFSQTTICRF 

       190        200        210        220        230        240 
EALQLSLKNM CKLRPLLEKW VEEADNNENL QEICKSETLV QARKRKRTSI ENRVRWSLET 

       250        260        270        280        290        300 
MFLKCPKPSL QQITHIANQL GLEKDVVRVW FCNRRQKGKR SSIEYSQREE YEATGTPFPG 

       310        320        330        340        350 
GAVSFPLPPG PHFGTPGYGS PHFTTLYSVP FPEGEAFPSV PVTALGSPMH SN

« Hide

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A POU-domain transcription factor in early stem cells and germ cells of the mammalian embryo." Rosner M.H., Vigano M.A., Ozato K., Timmons P.M., Poirier F., Rigby P.W.J., Staudt L. Nature 345:686-692(1990) [PubMed: 1972777] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE. Tissue: Embryonic carcinoma.
[2]	"New type of POU domain in germ line-specific protein Oct-4." Schoeler H.R., Ruppert S., Suzuki N., Chowdhury K., Gruss P. Nature 344:435-439(1990) [PubMed: 1690859] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION. Tissue: Embryonic carcinoma.
[3]	"A novel octamer binding transcription factor is differentially expressed in mouse embryonic cells." Okamoto K., Okazawa H., Okuda A., Sakai M., Muramatsu M., Hamada H. Cell 60:461-472(1990) [PubMed: 1967980] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"The oct3 gene, a gene for an embryonic transcription factor, is controlled by a retinoic acid repressible enhancer." Okazawa H., Okamoto K., Ishino F., Ishino-Kaneko T., Takeda S., Toyoda Y., Muramatsu M., Hamada H. EMBO J. 10:2997-3005(1991) [PubMed: 1915274] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SEQUENCE REVISION, INDUCTION.
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Embryo.
[6]	"Inhibition of DNA binding of Sox2 by the SUMO conjugation." Tsuruzoe S., Ishihara K., Uchimura Y., Watanabe S., Sekita Y., Aoto T., Saitoh H., Yuasa Y., Niwa H., Kawasuji M., Baba H., Nakao M. Biochem. Biophys. Res. Commun. 351:920-926(2006) [PubMed: 17097055] [Abstract] Cited for: SUMOYLATION AT LYS-118, MUTAGENESIS OF LYS-118.
[7]	"Post-translational modification of POU domain transcription factor Oct-4 by SUMO-1." Zhang Z., Liao B., Xu M., Jin Y. FASEB J. 21:3042-3051(2007) [PubMed: 17496161] [Abstract] Cited for: SUMOYLATION AT LYS-118, MUTAGENESIS OF LYS-118; GLU-120; LYS-215 AND LYS-244, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH UBE2I.
[8]	"Sumoylation of Oct4 enhances its stability, DNA binding, and transactivation." Wei F., Schoeler H.R., Atchison M.L. J. Biol. Chem. 282:21551-21560(2007) [PubMed: 17525163] [Abstract] Cited for: SUMOYLATION AT LYS-118, MUTAGENESIS OF LYS-118, FUNCTION, SUBCELLULAR LOCATION.
[9]	"Secondary structure of the oct-3 POU homeodomain as determined by 1H-15N NMR spectroscopy." Morita E.H., Shirakawa M., Hayashi F., Imagawa M., Kyogoku Y. FEBS Lett. 321:107-110(1993) [PubMed: 8097478] [Abstract] Cited for: STRUCTURE BY NMR OF POU DOMAIN.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

M34381 mRNA. Translation: AAA39844.1. Sequence problems.
X52437 mRNA. Translation: CAA36682.1.
S58426

S58425 Genomic DNA. Translation: AAB19896.1.
BC068268 mRNA. Translation: AAH68268.1.

IPI

IPI00117218.

PIR

A34672.
S17313.

RefSeq

NP_038661.2.

UniGene

Mm.17031

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1OCP	NMR	-	A	217-282	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P20263. 5 interactions.

PTM databases

PhosphoSite

P20263.

Proteomic databases

PRIDE

P20263.

Genome annotation databases

Ensembl

ENSMUST00000025271; ENSMUSP00000025271; ENSMUSG00000024406; Mus musculus. [Genome view]

GeneID

18999.

KEGG

mmu:18999.

UCSC

uc008chu.1. mouse.

Organism-specific databases

CTD

18999.

MGI

MGI:101893. Pou5f1.

Phylogenomic databases

HOVERGEN

P20263.

OMA

LENMFLQ.

Gene expression databases

ArrayExpress

P20263.

Bgee

P20263.

CleanEx

MM_POU5F1.

Genevestigator

P20263.

Family and domain databases

InterPro

IPR001356. Homeobox.
IPR017970. Homeobox_CS.
IPR012287. Homeodomain-rel.
IPR013847. POU.
IPR015585. POU_dom_5.
IPR000327. POU_specific.
[Graphical view]

Gene3D

G3DSA:1.10.10.60. Homeodomain-rel. 1 hit.

PANTHER

PTHR11636:SF15. POU_5. 1 hit.

Pfam

PF00046. Homeobox. 1 hit.
PF00157. Pou. 1 hit.
[Graphical view]

PRINTS

PR00028. POUDOMAIN.

ProDom

PD000010. Homeobox. 1 hit.
PD000583. POU. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00389. HOX. 1 hit.
SM00352. POU. 1 hit.
[Graphical view]

PROSITE

PS00027. HOMEOBOX_1. 1 hit.
PS50071. HOMEOBOX_2. 1 hit.
PS00035. POU_1. 1 hit.
PS00465. POU_2. 1 hit.
PS51179. POU_3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

295410.

SOURCE

Search...

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Entry information

Entry name

PO5F1_MOUSE

Accession

Primary (citable) accession number: P20263
Secondary accession number(s): Q63843

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	February 1, 1991
Last modified:	November 3, 2009
This is version 101 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents