nuclear factor of activated T-cells, cytoplasmic 3; NF-ATc3; NFATc3; T-cell transcription factor NFAT4; NF-AT4; NFATx (NFATC3, NFAT4)

Function: - role in the inducible expression of cytokine genes in T-cells, especially in the induction of the IL-2 - phosphorylated by NFATC-kinase - dephosphorylated by calcineurin (putative) - member of the multicomponent NFATC transcription complex - binds to DNA as monomer Structure: - Rel similarity domain (RSD) allows DNA-binding & cooperative interactions with AP1 factors - contains 1 RHD (Rel-like) domain Compartment: - cytoplasm, nucleus - cytoplasmic for the phosphorylated form - nuclear after activation that is controlled by calcineurin-mediated dephosphorylation - rapid nuclear exit of NFATC is thought to be one mechanism by which cells distinguish between sustained & transient Ca⁺² signals - the subcellular localization of NFATC plays a key role in the regulation of gene transcription Alternative splicing: named isoforms=6 Expression: - isoform 1: - predominantly expressed in thymus - also found in peripheral blood leukocytes & kidney - isoform 2: - predominantly expressed in skeletal muscle - also found in thymus, kidney, testis, spleen, prostate, ovary, small intestine, heart, placenta & pancreas - isoform 3 is expressed in thymus & kidney - isoform 4 is expressed in thymus & skeletal muscle

General

DNA-binding protein phosphoprotein

Properties

SIZE: entity length = 1075 aa MW = 116 kD MOTIF: acetylation site SITE: N-TERMINUS EFFECTOR-BOUND: acetyl proline-rich region SITE: 24-29 MOTIF: proline residue (SEVERAL) binding site SITE: 109-114 FOR-BINDING-OF: calcineurin 3 X SP repeats {207-308} MOTIF: consensus repeat {207-223} consensus repeat {236-252} nuclear translocation signal {273-275} consensus repeat {292-308} RHD {415-596} MOTIF: DNA-binding motif SITE: 444-451 phosphorylation site nuclear translocation signal {686-688} nuclear export signal {1032-1041}

Database Correlations

OMIM 602698 UniProt Q12968 PFAM correlations Entrez Gene 4775 Kegg hsa:4775

References

UniProt :accession Q12968