NFAT5_RAT
ID NFAT5_RAT Reviewed; 1548 AA.
AC D3ZGB1;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Nuclear factor of activated T-cells 5;
DE Short=NF-AT5;
DE AltName: Full=T-cell transcription factor NFAT5;
GN Name=Nfat5;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, INTERACTION WITH CIDEC, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND INDUCTION BY OSMOTIC STRESS.
RX PubMed=23233732; DOI=10.1194/jlr.m033365;
RA Ueno M., Shen W.J., Patel S., Greenberg A.S., Azhar S., Kraemer F.B.;
RT "Fat-specific protein 27 modulates nuclear factor of activated T cells 5
RT and the cellular response to stress.";
RL J. Lipid Res. 54:734-743(2013).
CC -!- FUNCTION: Transcription factor involved in the transcriptional
CC regulation of osmoprotective and inflammatory genes. Regulates
CC hypertonicity-induced cellular accumulation of osmolytes.
CC {ECO:0000269|PubMed:23233732}.
CC -!- SUBUNIT: Homodimer when bound to DNA, completely encircles its DNA
CC target. Does not bind with Fos and Jun transcription factors (By
CC similarity). Interacts with CIDEC; this interaction is direct and
CC retains NFAT5 in the cytoplasm. {ECO:0000250,
CC ECO:0000269|PubMed:23233732}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23233732}. Cytoplasm
CC {ECO:0000269|PubMed:23233732}. Note=Nuclear distribution increases
CC under hypertonic conditions.
CC -!- INDUCTION: Up-regulated under hypertonic conditions.
CC {ECO:0000269|PubMed:23233732}.
CC -!- PTM: Phosphorylated at Thr-152 by CDK5 in response to osmotic stress;
CC this phosphorylation mediates its rapid nuclear localization.
CC {ECO:0000250}.
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DR EMBL; AABR06098525; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06098526; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06098527; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473972; EDL92476.1; -; Genomic_DNA.
DR RefSeq; NP_001100895.1; NM_001107425.1.
DR AlphaFoldDB; D3ZGB1; -.
DR SMR; D3ZGB1; -.
DR BioGRID; 258819; 1.
DR STRING; 10116.ENSRNOP00000017005; -.
DR iPTMnet; D3ZGB1; -.
DR PhosphoSitePlus; D3ZGB1; -.
DR PaxDb; D3ZGB1; -.
DR Ensembl; ENSRNOT00000017005; ENSRNOP00000017005; ENSRNOG00000011879.
DR GeneID; 307820; -.
DR KEGG; rno:307820; -.
DR CTD; 10725; -.
DR RGD; 1309142; Nfat5.
DR eggNOG; ENOG502QSVE; Eukaryota.
DR GeneTree; ENSGT00940000155213; -.
DR HOGENOM; CLU_004396_0_0_1; -.
DR InParanoid; D3ZGB1; -.
DR OMA; LMETPGN; -.
DR OrthoDB; 95502at2759; -.
DR TreeFam; TF326480; -.
DR PRO; PR:D3ZGB1; -.
DR Proteomes; UP000002494; Chromosome 19.
DR Proteomes; UP000234681; Chromosome 19.
DR Bgee; ENSRNOG00000011879; Expressed in Ammon's horn and 20 other tissues.
DR ExpressionAtlas; D3ZGB1; baseline and differential.
DR Genevisible; D3ZGB1; RN.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; ISO:RGD.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:RGD.
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; ISO:RGD.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
DR GO; GO:0033173; P:calcineurin-NFAT signaling cascade; IBA:GO_Central.
DR GO; GO:0071345; P:cellular response to cytokine stimulus; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:1904996; P:positive regulation of leukocyte adhesion to vascular endothelial cell; ISO:RGD.
DR GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0070884; P:regulation of calcineurin-NFAT signaling cascade; ISO:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006970; P:response to osmotic stress; IEP:RGD.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:InterPro.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 2.60.40.340; -; 1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR002909; IPT_dom.
DR InterPro; IPR008366; NFAT.
DR InterPro; IPR015646; NFAT5.
DR InterPro; IPR008967; p53-like_TF_DNA-bd.
DR InterPro; IPR032397; RHD_dimer.
DR InterPro; IPR011539; RHD_DNA_bind_dom.
DR InterPro; IPR037059; RHD_DNA_bind_dom_sf.
DR PANTHER; PTHR12533; PTHR12533; 1.
DR PANTHER; PTHR12533:SF10; PTHR12533:SF10; 1.
DR Pfam; PF16179; RHD_dimer; 1.
DR Pfam; PF00554; RHD_DNA_bind; 1.
DR PRINTS; PR01789; NUCFACTORATC.
DR SMART; SM00429; IPT; 1.
DR SUPFAM; SSF49417; SSF49417; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS50254; REL_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Cytoplasm; DNA-binding; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..1548
FT /note="Nuclear factor of activated T-cells 5"
FT /id="PRO_0000423618"
FT DOMAIN 281..460
FT /note="RHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00265"
FT DNA_BIND 310..317
FT /evidence="ECO:0000250"
FT REGION 54..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 141..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 192..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 659..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 750..777
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 851..892
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 970..1010
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1097..1127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1257..1388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..278
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 873..892
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94916"
FT MOD_RES 139
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9WV30"
FT MOD_RES 151
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94916"
FT MOD_RES 152
FT /note="Phosphothreonine; by CDK5"
FT /evidence="ECO:0000250|UniProtKB:O94916"
FT MOD_RES 172
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94916"
FT MOD_RES 577
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94916"
FT CROSSLNK 572
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:O94916"
FT CROSSLNK 572
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:O94916"
FT CROSSLNK 619
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O94916"
SQ SEQUENCE 1548 AA; 167207 MW; CE3F4A41532770EF CRC64;
MPSDFISLLS ADLDLESPKS LYSRDSLKLH PSQNFHRAGL LEESVYDLLP KELQLPPPRE
TSAASMSQTS GGEAGSPPPA VVAADASSAP SSSMGGACSS FTTSSSPTIY STSVTDSKAM
QVESCSSAVG VSNRGVSEKQ LTGNTVQQHP STPKRHTVLY ISPPPEDLLD NSRMSCQDEG
CGLESEQSCS MWMEDSPSNF SNMSTSSYND NTEVPRKSRK RNPKQRPGVK RRDCEESNMD
IFDADSAKAP HYVLSQLTTD NKGNSKAGNG TLDSQKGTGV KKSPMLCGQY PVKSEGKELK
IVVQPETQHR ARYLTEGSRG SVKDRTQQGF PTVKLEGHNE PVVLQVFVGN DSGRVKPHGF
YQACRVTGRN TTPCKEVDIE GTTVIEVGLD PSSNMTLAVD CVGILKLRNA DVEARIGIAG
SKKKSTRARL VFRVNITRKD GSTLTLQTPS SPILCTQPAG VPEILKKSLH SCSVKGEEEV
FLIGKNFLKG TKVIFQENVS DENSWKSEAE IDMELFHQNH LIVKVPPYHD QHITLPVSVG
IYVVTNAGRS HDVQPFTYTP DPAAGALSVN VKKEISSPAR PCSFEEALKA MKTTGCNVDK
VTILPNALIT PLISSSMIKT EDVTPMEVTS EKRSSPIFQT TKTVGSTQQT LETISNIAGN
ASFSSPSSSH LSPENENQQQ LQPKAYNPET LTTIQTQDIS QPGTFPAVSA SSQLPSSDAL
LQQAAQFQTR DAQSRDTMQS DSVVNLSQLT EAPQQQQSPL QEQAQIPSNI FPSPNSVSQL
QSTIQQLQAG SFTGSTASGS NGSVDLVQQV LEAQQQLSSV LFSTPDGNEN VQEQLNADIF
QVSQIQNSVS PGMFSSTESA VHTRPDNLLP GRADSVHQQT ENTLSSQQQQ QQQQQQQQQQ
QVIESSAAMV MEMQQSICQA AAQIQSELFP SAASANGSLQ QSPVYQQPSH MMSALPTSED
MQMQCELFSS PPAVSGNETS TTTTPQVATP GSTMFQPPNS GDGEETGAQA KQIQSSVFQT
MVQMQHSGDS QPQVNLFSST KNIMSVQSNG TQQQGNSLFQ QGSEMLSLQS GSFLQQSSHS
QAQLFHPQNP IADAQSLSQE TQGPMFHSAN PIVHSQTSTA SSEQLQPSMF HSQSTIAVLQ
GSSVPQDQQS PNIYLSQSSI SNLQTNTVAQ EEQISFFSAQ NSISPLQSTS NTEQQAAFQQ
QPPISHIQTP LLSQEQAQPS QQGLFQPQVA LGSLPANPMP QNQQGPIFQT QRPIVGMQSN
SPSQEQQQQQ QQQQQQQQQQ QQQSILFSNQ NAMATMASQK QPPPNMIFSP NQNPMASQEQ
QNQSIFHQQS NMAPMNQEQQ PMQFQNQPTV SSLQNPGPTP SESPQTSLFH SSPQIQLVQG
SPSSQEQQVT LFLSPASMSA LQTSINQPDM QQSPLYSPQN NIPGIQGSTS SPQPQAALFH
NTTGGTINQL QNSPGSSQQT SGMFLFGIQN NCSQLLTSGP ATLPEQLMAI NQPGQPQNEG
QSSVTTLLSQ QMPESAPLAS SVNNSQNMEK IDLLVSLQSQ GNNLTGSF
