Forkhead box protein P3 - Mus musculus (Mouse)

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Q99JB6 (FOXP3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 109. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Forkhead box protein P3

Alternative name(s):
Scurfin

Gene names

Name:

Foxp3

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	429 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Probable transcription factor. Plays a critical role in the control of immune response.
Subunit structure	Interacts with IKZF3 By similarity.
Subcellular location	Nucleus Potential.
Tissue specificity	High level of expression in thymus and spleen.
Post-translational modification	Acetylation on lysine residues stabilizes FOXP3 and promotes differentiation of T-cells into induced regulatory T-cells (iTregs) associated with suppressive functions. Deacetylated by SIRT1.
Involvement in disease	Defects in Foxp3 are the cause of the scurfy phenotype (sf). It results in a lethal disorder of immunoregulation, characterized by infections, diarrhea, anemia, thrombocytopenia, hypogonadism, gastrointestinal bleeding, lymphadenopathy and leukocytosis.
Sequence similarities	Contains 1 C2H2-type zinc finger. Contains 1 fork-head DNA-binding domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Domain	Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
PTM	Acetylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	B cell homeostasis Inferred from mutant phenotype PubMed 10072494. Source: MGI CD4-positive, CD25-positive, alpha-beta regulatory T cell differentiation Inferred from mutant phenotype PubMed 12612578 PubMed 18573908. Source: MGI T cell mediated immunity Inferred from mutant phenotype PubMed 11714795. Source: MGI T cell receptor signaling pathway Inferred from mutant phenotype PubMed 10072494 PubMed 11265635. Source: MGI cerebellum development Inferred from Biological aspect of Ancestor. Source: RefGenome cytokine production Inferred from direct assay PubMed 15790681. Source: MGI embryo development Inferred from Biological aspect of Ancestor. Source: RefGenome myeloid cell homeostasis Inferred from mutant phenotype PubMed 10072494. Source: MGI negative regulation of CREB transcription factor activity Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of NF-kappaB transcription factor activity Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of T cell cytokine production Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of T cell proliferation Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of chronic inflammatory response Inferred from direct assay PubMed 16769892. Source: MGI negative regulation of cytokine secretion Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of histone acetylation Inferred from direct assay PubMed 17028180. Source: MGI negative regulation of histone deacetylation Inferred from Biological aspect of Ancestor. Source: RefGenome negative regulation of interferon-gamma biosynthetic process Inferred from direct assay PubMed 17028180. Source: MGI negative regulation of interferon-gamma production Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of interleukin-10 production Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of interleukin-2 biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of interleukin-2 production Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of interleukin-4 production Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of interleukin-5 production Inferred from direct assay PubMed 16769892. Source: MGI negative regulation of interleukin-6 production Inferred from mutant phenotype PubMed 16275384. Source: MGI negative regulation of isotype switching to IgE isotypes Inferred from mutant phenotype PubMed 16275384. Source: MGI negative regulation of transcription from RNA polymerase II promoter Inferred from direct assay PubMed 16230479 PubMed 16769892 PubMed 17028180. Source: MGI negative regulation of tumor necrosis factor production Inferred from mutant phenotype PubMed 16275384. Source: MGI pattern specification process Inferred from Biological aspect of Ancestor. Source: RefGenome positive regulation of CD4-positive, CD25-positive, alpha-beta regulatory T cell differentiation Inferred from mutant phenotype PubMed 16275384 PubMed 16301745. Source: MGI positive regulation of T cell anergy Inferred from mutant phenotype PubMed 16945588. Source: MGI positive regulation of histone acetylation Inferred from direct assay PubMed 17028180. Source: MGI positive regulation of immature T cell proliferation in thymus Inferred from mutant phenotype PubMed 16230479. Source: MGI positive regulation of interleukin-4 production Inferred from mutant phenotype PubMed 20944002. Source: MGI positive regulation of peripheral T cell tolerance induction Inferred from mutant phenotype PubMed 16532000. Source: MGI positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay PubMed 17028180. Source: MGI positive regulation of transforming growth factor beta1 production Inferred from direct assay PubMed 17028180. Source: MGI post-embryonic development Inferred from Biological aspect of Ancestor. Source: RefGenome regulation of isotype switching to IgG isotypes Inferred from mutant phenotype PubMed 16275384. Source: MGI response to virus Inferred from electronic annotation. Source: Compara tolerance induction to self antigen Inferred from mutant phenotype PubMed 15780990. Source: MGI
Cellular_component	cytoplasm Inferred from direct assay PubMed 17028180. Source: MGI transcription factor complex Inferred from Biological aspect of Ancestor. Source: RefGenome
Molecular_function	DNA binding, bending Inferred from Biological aspect of Ancestor. Source: RefGenome NFAT protein binding Inferred from sequence or structural similarity. Source: UniProtKB RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity Inferred from direct assay PubMed 17028180. Source: MGI chromatin binding Inferred from Biological aspect of Ancestor. Source: RefGenome double-stranded DNA binding Inferred from Biological aspect of Ancestor. Source: RefGenome histone acetyltransferase binding Inferred from Biological aspect of Ancestor. Source: RefGenome histone deacetylase binding Inferred from Biological aspect of Ancestor. Source: RefGenome protein heterodimerization activity Inferred from Biological aspect of Ancestor. Source: RefGenome protein homodimerization activity Inferred from sequence or structural similarity. Source: UniProtKB sequence-specific DNA binding Inferred from sequence or structural similarity. Source: UniProtKB transcription corepressor activity Inferred from direct assay PubMed 15790681. Source: MGI zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 429

429

Forkhead box protein P3

PRO_0000091888

Regions

Zinc finger

196 – 221

C2H2-type

DNA binding

337 – 423

Fork-head

Region

238 – 259

Leucine-zipper

Amino acid modifications

Modified residue

N6-acetyllysine Ref.2

Modified residue

262

N6-acetyllysine Ref.2

Modified residue

267

N6-acetyllysine Ref.2

Secondary structure

429

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q99JB6 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 28D5B8E67891840C
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FASTA

429

47,346

        10         20         30         40         50         60 
MPNPRPAKPM APSLALGPSP GVLPSWKTAP KGSELLGTRG SGGPFQGRDL RSGAHTSSSL 

        70         80         90        100        110        120 
NPLPPSQLQL PTVPLVMVAP SGARLGPSPH LQALLQDRPH FMHQLSTVDA HAQTPVLQVR 

       130        140        150        160        170        180 
PLDNPAMISL PPPSAATGVF SLKARPGLPP GINVASLEWV SREPALLCTF PRSGTPRKDS 

       190        200        210        220        230        240 
NLLAAPQGSY PLLANGVCKW PGCEKVFEEP EEFLKHCQAD HLLDEKGKAQ CLLQREVVQS 

       250        260        270        280        290        300 
LEQQLELEKE KLGAMQAHLA GKMALAKAPS VASMDKSSCC IVATSTQGSV LPAWSAPREA 

       310        320        330        340        350        360 
PDGGLFAVRR HLWGSHGNSS FPEFFHNMDY FKYHNMRPPF TYATLIRWAI LEAPERQRTL 

       370        380        390        400        410        420 
NEIYHWFTRM FAYFRNHPAT WKNAIRHNLS LHKCFVRVES EKGAVWTVDE FEFRKKRSQR 


PNKCSNPCP

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References

[1]	"Disruption of a new forkhead/winged-helix protein, scurfin, results in the fatal lymphoproliferative disorder of the scurfy mouse." Brunkow M.E., Jeffery E.W., Hjerrild K.A., Paeper B., Clark L.B., Yasayko S.-A., Wilkinson J.E., Galas D., Ziegler S.F., Ramsdell F. Nat. Genet. 27:68-73(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[2]	"Three novel acetylation sites in the Foxp3 transcription factor regulate the suppressive activity of regulatory T cells." Kwon H.S., Lim H.W., Wu J., Schnolzer M., Verdin E., Ott M. J. Immunol. 188:2712-2721(2012) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION AT LYS-31; LYS-262 AND LYS-267, DEACETYLATION BY SIRT1.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF277994 Genomic DNA. Translation: AAG53608.1.
AF277991 mRNA. Translation: AAG53605.1.
AF277992 mRNA. Translation: AAG53606.1.

IPI

IPI00115123.

RefSeq

NP_001186276.1. NM_001199347.1.
NP_001186277.1. NM_001199348.1.
NP_473380.1. NM_054039.2.

UniGene

Mm.182291.
Mm.288192.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4I1L	X-ray	2.10	A	189-276	[»]

ProteinModelPortal

Q99JB6.

SMR

Q99JB6. Positions 201-262, 336-417.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-59739N.

PTM databases

PhosphoSite

Q99JB6.

Proteomic databases

PRIDE

Q99JB6.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000045566; ENSMUSP00000041953; ENSMUSG00000039521.
ENSMUST00000115738; ENSMUSP00000111403; ENSMUSG00000039521.
ENSMUST00000115739; ENSMUSP00000111404; ENSMUSG00000039521.
ENSMUST00000115740; ENSMUSP00000111405; ENSMUSG00000039521.

GeneID

20371.

KEGG

mmu:20371.

Organism-specific databases

CTD

50943.

MGI

MGI:1891436. Foxp3.

Phylogenomic databases

eggNOG

COG5025.

GeneTree

ENSGT00690000101938.

HOGENOM

HOG000082490.

HOVERGEN

HBG051656.

InParanoid

Q99JB6.

K10163.

OrthoDB

EOG4F7NK4.

Gene expression databases

ArrayExpress

Q99JB6.

Bgee

Q99JB6.

CleanEx

MM_FOXP3.

Genevestigator

Q99JB6.

GermOnline

ENSMUSG00000039521. Mus musculus.

Family and domain databases

Gene3D

1.10.10.10. 1 hit.
3.30.160.60. 1 hit.

InterPro

IPR001766. TF_fork_head.
IPR018122. TF_fork_head_CS.
IPR011991. WHTH_DNA-bd_dom.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]

Pfam

PF00250. Fork_head. 1 hit.
[Graphical view]

PRINTS

PR00053. FORKHEAD.

SMART

SM00339. FH. 1 hit.
SM00355. ZnF_C2H2. 1 hit.
[Graphical view]

PROSITE

PS00657. FORK_HEAD_1. False negative.
PS00658. FORK_HEAD_2. 1 hit.
PS50039. FORK_HEAD_3. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 1 hit.
PS50157. ZINC_FINGER_C2H2_2. False negative.
[Graphical view]

ProtoNet

Search...

Other

NextBio

298278.

SOURCE

Search...

Entry information

Entry name

FOXP3_MOUSE

Accession

Primary (citable) accession number: Q99JB6

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 20, 2001
Last sequence update:	June 1, 2001
Last modified:	May 1, 2013
This is version 109 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents