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Nuclear factor of activated T-cells, cytoplasmic 1 (NF-ATc1) (NFATc1) (NFAT transcription complex cytosolic component) (NF-ATc) (NFATc)

 NFAC1_MOUSE             Reviewed;         717 AA.
O88942; O70345;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
25-OCT-2017, entry version 160.
RecName: Full=Nuclear factor of activated T-cells, cytoplasmic 1;
Short=NF-ATc1;
Short=NFATc1;
AltName: Full=NFAT transcription complex cytosolic component;
Short=NF-ATc;
Short=NFATc;
Name=Nfatc1; Synonyms=Nfat2, Nfatc;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA), INDUCTION, TISSUE
SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=9388475; DOI=10.1006/bbrc.1997.7381;
Pan S., Koyano-Nakagawa N., Tsuruta L., Amasaki Y., Yokota T.,
Mori S., Arai N., Arai K.;
"Molecular cloning and functional characterization of murine cDNA
encoding transcription factor NFATc.";
Biochem. Biophys. Res. Commun. 240:314-323(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA), INDUCTION, AND TISSUE
SPECIFICITY.
STRAIN=BALB/cJ; TISSUE=Fetal liver, and Mast cell;
PubMed=10072529;
Sherman M.A., Powell D.R., Weiss D.L., Brown M.A.;
"NF-ATc Isoforms are differentially expressed and regulated in murine
T and mast cells.";
J. Immunol. 162:2820-2828(1999).
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235 AND SER-239, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Lung, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[4]
SUBCELLULAR LOCATION.
PubMed=24039232; DOI=10.1242/jcs.127571;
Tiedemann K., Boraschi-Diaz I., Rajakumar I., Kaur J., Roughley P.,
Reinhardt D.P., Komarova S.V.;
"Fibrillin-1 directly regulates osteoclast formation and function by a
dual mechanism.";
J. Cell Sci. 126:4187-4194(2013).
[5]
FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
PubMed=26644563; DOI=10.1073/pnas.1511285112;
Decker C.E., Yang Z., Rimer R., Park-Min K.H., Macaubas C.,
Mellins E.D., Novack D.V., Faccio R.;
"Tmem178 acts in a novel negative feedback loop targeting NFATc1 to
regulate bone mass.";
Proc. Natl. Acad. Sci. U.S.A. 112:15654-15659(2015).
[6]
SUBCELLULAR LOCATION.
PubMed=28341745; DOI=10.1074/jbc.M117.784777;
Murakami A., Matsuda M., Harada Y., Hirata M.;
"Phospholipase C-related, but catalytically inactive protein (PRIP)
upregulates osteoclast differentiation via calcium-calcineurin-NFATc1
signaling.";
J. Biol. Chem. 292:7994-8006(2017).
-!- FUNCTION: Plays a role in the inducible expression of cytokine
genes in T-cells, especially in the induction of the IL-2 or IL-4
gene transcription. Also controls gene expression in embryonic
cardiac cells. Could regulate not only the activation and
proliferation but also the differentiation and programmed death of
T-lymphocytes as well as lymphoid and non-lymphoid cells (By
similarity). Required for osteoclastogenesis and regulates many
genes important for osteoclast differentiation and function
(PubMed:26644563). {ECO:0000250|UniProtKB:O95644,
ECO:0000303|PubMed:26644563}.
-!- SUBUNIT: Member of the multicomponent NFATC transcription complex
that consists of at least two components, a pre-existing
cytoplasmic component NFATC2 and an inducible nuclear component
NFATC1. Other members such as NFATC4, NFATC3 or members of the
activating protein-1 family, MAF, GATA4 and Cbp/p300 can also bind
the complex. NFATC proteins bind to DNA as monomers (By
similarity). {ECO:0000250}.
-!- INTERACTION:
Q913V3:- (xeno); NbExp=2; IntAct=EBI-8073353, EBI-10053030;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:28341745}.
Nucleus {ECO:0000269|PubMed:24039232, ECO:0000269|PubMed:26644563,
ECO:0000269|PubMed:28341745}. Note=Cytoplasmic for the
phosphorylated form and 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 and transient calcium signals.
The subcellular localization of NFATC plays a key role in the
regulation of gene transcription (By similarity). Nuclear
translocation of NFATC1 is enhanced in the presence of TNFSF11
(PubMed:26644563). Nuclear translocation is decreased in the
presence of FBN1 which can bind and sequester TNFSF11
(PubMed:24039232). {ECO:0000250|UniProtKB:O95644,
ECO:0000269|PubMed:24039232, ECO:0000269|PubMed:26644563}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing, Alternative initiation; Named isoforms=3;
Name=Alpha;
IsoId=O88942-1; Sequence=Displayed;
Name=Beta;
IsoId=O88942-2; Sequence=VSP_005594;
Name=Alpha';
IsoId=O88942-3; Sequence=VSP_018867;
Note=Produced by alternative initiation at Met-37 of isoform
Alpha. No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in spleen, lung, skeletal muscle,
thymus and skin (PubMed:9388475). Weakly expressed in heart,
brain, liver and kidney. Not expressed in testis
(PubMed:10072529). {ECO:0000269|PubMed:10072529,
ECO:0000269|PubMed:9388475}.
-!- DEVELOPMENTAL STAGE: Expression begins at E7 day and increases
until E17 day. Strongly expressed in thymus, lung and
submandibular gland and weakly in skeletal muscle and heart.
{ECO:0000269|PubMed:9388475}.
-!- INDUCTION: Inducibly expressed in T-lymphocytes upon activation of
the T-cell receptor (TCR) complex. Induced after addition of
phorbol 12-myristate 13-acetate (PMA) (PubMed:9388475,
PubMed:10072529). Expressed during osteoclastogenesis and its
induction and activation is regulated by TNFSF11
(PubMed:26644563). {ECO:0000269|PubMed:10072529,
ECO:0000269|PubMed:26644563, ECO:0000269|PubMed:9388475}.
-!- DOMAIN: Rel Similarity Domain (RSD) allows DNA-binding and
cooperative interactions with AP1 factors. {ECO:0000250}.
-!- DOMAIN: The N-terminal transactivation domain (TAD-A) binds to and
is activated by Cbp/p300. The dephosphorylated form contains two
unmasked nuclear localization signals (NLS), which allow
translocation of the protein to the nucleus (By similarity).
{ECO:0000250}.
-!- PTM: Phosphorylated by NFATC-kinase and GSK3B; phosphorylation
induces NFATC1 nuclear exit and dephosphorylation by calcineurin
promotes nuclear import. Phosphorylation by PKA and DYRK2
negatively modulates nuclear accumulation, and promotes subsequent
phosphorylation by GSK3B or casein kinase 1 (By similarity).
{ECO:0000250}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AF049606; AAC05505.1; -; mRNA.
EMBL; AF087434; AAC36725.1; -; mRNA.
CCDS; CCDS29369.1; -. [O88942-2]
UniGene; Mm.329560; -.
ProteinModelPortal; O88942; -.
SMR; O88942; -.
IntAct; O88942; 2.
MINT; MINT-6612506; -.
STRING; 10090.ENSMUSP00000129001; -.
ChEMBL; CHEMBL6034; -.
iPTMnet; O88942; -.
PhosphoSitePlus; O88942; -.
MaxQB; O88942; -.
PaxDb; O88942; -.
PRIDE; O88942; -.
MGI; MGI:102469; Nfatc1.
eggNOG; ENOG410IHFR; Eukaryota.
eggNOG; ENOG41105U2; LUCA.
HOGENOM; HOG000231780; -.
HOVERGEN; HBG069754; -.
InParanoid; O88942; -.
PhylomeDB; O88942; -.
PRO; PR:O88942; -.
Proteomes; UP000000589; Unplaced.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0016604; C:nuclear body; ISO:MGI.
GO; GO:0000790; C:nuclear chromatin; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005667; C:transcription factor complex; IPI:MGI.
GO; GO:0003682; F:chromatin binding; IDA:MGI.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0048273; F:mitogen-activated protein kinase p38 binding; IPI:BHF-UCL.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IDA:MGI.
GO; GO:0000980; F:RNA polymerase II distal enhancer sequence-specific DNA binding; IDA:BHF-UCL.
GO; GO:0001085; F:RNA polymerase II transcription factor binding; IPI:BHF-UCL.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
GO; GO:0003705; F:transcription factor activity, RNA polymerase II distal enhancer sequence-specific binding; IDA:BHF-UCL.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:NTNU_SB.
GO; GO:0001205; F:transcriptional activator activity, RNA polymerase II distal enhancer sequence-specific binding; IDA:BHF-UCL.
GO; GO:0001227; F:transcriptional repressor activity, RNA polymerase II transcription regulatory region sequence-specific binding; IDA:MGI.
GO; GO:0003180; P:aortic valve morphogenesis; IMP:MGI.
GO; GO:0002337; P:B-1a B cell differentiation; IMP:MGI.
GO; GO:0060854; P:branching involved in lymph vessel morphogenesis; IMP:MGI.
GO; GO:0033173; P:calcineurin-NFAT signaling cascade; IMP:MGI.
GO; GO:0006816; P:calcium ion transport; IMP:MGI.
GO; GO:0001837; P:epithelial to mesenchymal transition; IMP:MGI.
GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IMP:MGI.
GO; GO:0007507; P:heart development; IMP:MGI.
GO; GO:0061384; P:heart trabecula morphogenesis; IMP:MGI.
GO; GO:0003179; P:heart valve morphogenesis; IMP:MGI.
GO; GO:0035556; P:intracellular signal transduction; ISO:MGI.
GO; GO:0001946; P:lymphangiogenesis; IGI:MGI.
GO; GO:0045668; P:negative regulation of osteoblast differentiation; IDA:MGI.
GO; GO:2000647; P:negative regulation of stem cell proliferation; IMP:MGI.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:MGI.
GO; GO:0030316; P:osteoclast differentiation; IGI:MGI.
GO; GO:0010628; P:positive regulation of gene expression; IDA:MGI.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:0003184; P:pulmonary valve morphogenesis; IMP:MGI.
GO; GO:0042634; P:regulation of hair cycle; IMP:MGI.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
GO; GO:0014883; P:transition between fast and slow fiber; IMP:MGI.
GO; GO:0060412; P:ventricular septum morphogenesis; IMP:MGI.
Gene3D; 2.60.40.10; -; 1.
Gene3D; 2.60.40.340; -; 1.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR014756; Ig_E-set.
InterPro; IPR002909; IPT.
InterPro; IPR008366; NFAT.
InterPro; IPR015647; NFAT1.
InterPro; IPR008967; p53-like_TF_DNA-bd.
InterPro; IPR032397; RHD_dimer.
InterPro; IPR011539; RHD_DNA_bind_dom.
InterPro; IPR037059; RHD_DNA_bind_dom_sf.
PANTHER; PTHR12533; PTHR12533; 1.
PANTHER; PTHR12533:SF5; PTHR12533:SF5; 1.
Pfam; PF16179; RHD_dimer; 1.
Pfam; PF00554; RHD_DNA_bind; 1.
PRINTS; PR01789; NUCFACTORATC.
SMART; SM00429; IPT; 1.
SUPFAM; SSF49417; SSF49417; 1.
SUPFAM; SSF81296; SSF81296; 1.
PROSITE; PS50254; REL_2; 1.
1: Evidence at protein level;
Activator; Alternative initiation; Alternative splicing;
Complete proteome; Cytoplasm; DNA-binding; Nucleus; Phosphoprotein;
Reference proteome; Repeat; Transcription; Transcription regulation.
CHAIN 1 717 Nuclear factor of activated T-cells,
cytoplasmic 1.
/FTId=PRO_0000030331.
REPEAT 205 221 1.
REPEAT 235 251 2.
REPEAT 284 300 3.
DOMAIN 411 593 RHD. {ECO:0000255|PROSITE-
ProRule:PRU00265}.
DNA_BIND 440 447 {ECO:0000250}.
REGION 120 125 Calcineurin-binding.
REGION 128 220 Trans-activation domain A (TAD-A).
REGION 205 300 3 X SP repeats.
MOTIF 267 269 Nuclear localization signal.
MOTIF 312 323 Nuclear export signal.
MOTIF 683 685 Nuclear localization signal.
MOD_RES 235 235 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 239 239 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 247 247 Phosphoserine; by PKA.
{ECO:0000250|UniProtKB:O95644}.
MOD_RES 271 271 Phosphoserine; by PKA.
{ECO:0000250|UniProtKB:O95644}.
MOD_RES 296 296 Phosphoserine; by PKA.
{ECO:0000250|UniProtKB:O95644}.
VAR_SEQ 1 42 MPNTSFPVPSKFPLGPPAAVCGSGETLRPAPPSGGTMKAAE
E -> MTGLEQDPEFDFDFLFEFDQSGGGAAAA (in
isoform Beta).
{ECO:0000303|PubMed:9388475}.
/FTId=VSP_005594.
VAR_SEQ 1 36 Missing (in isoform Alpha').
{ECO:0000305}.
/FTId=VSP_018867.
SEQUENCE 717 AA; 77833 MW; 58837C6CC085268D CRC64;
MPNTSFPVPS KFPLGPPAAV CGSGETLRPA PPSGGTMKAA EEEHYSYVSP SVTSTLPLPT
AHSALPAACH DLQTSTPGIS AVPSANHPPS YGGAVDSGPS GYFLSSGNTR PNGAPTLESP
RIEITSYLGL HHGSGQFFHD VEVEDVLPSC KRSPSTATLH LPSLEAYRDP SCLSPASSLS
SRSCNSEASS YESNYSYPYA SPQTSPWQSP CVSPKTTDPE EGFPRSLGAC HLLGSPRHSP
STSPRASITE ESWLGARGSR PTSPCNKRKY SLNGRQPSCS PHHSPTPSPH GSPRVSVTED
TWLGNTTQYT SSAIVAAINA LTTDSTLDLG DGVPIKSRKT ALEHAPSVAL KVEPAGEDLG
TTPPTSDFPP EEYTFQHLRK GAFCEQYLSV PQASYQWAKP KSLSPTSYMS PSLPALDWQL
PSHSGPYELR IEVQPKSHHR AHYETEGSRG AVKASAGGHP IVQLHGYLEN EPLTLQLFIG
TADDRLLRPH AFYQVHRITG KTVSTTSHEI ILSNTKVLEI PLLPENNMRA IIDCAGILKL
RNSDIELRKG ETDIGRKNTR VRLVFRVHIP QPNGRTLSLQ VASNPIECSQ RSAQELPLVE
KQSTDSYPVI GGKKMVLSGH NFLQDSKVIF VEKAPDGHHV WEMEAKTDRD LCKPNSLVVE
IPPFRNQRIT SPAQVSFYVC NGKRKRSQYQ RFTYLPANGN SVFLTLSSES ELRGGFY


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