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 07-APR-2021, entry version 85. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 SMR; D3ZGB1; -. DR BioGRID; 258819; 1. DR STRING; 10116.ENSRNOP00000017005; -. DR iPTMnet; D3ZGB1; -. DR PhosphoSitePlus; D3ZGB1; -. DR PaxDb; D3ZGB1; -. DR PRIDE; 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; AQFQTRD; -. DR OrthoDB; 95502at2759; -. DR TreeFam; TF326480; -. DR PRO; PR:D3ZGB1; -. DR Proteomes; UP000002494; Chromosome 19. DR Proteomes; UP000234681; Chromosome 19. DR Proteomes; UP000234681; Unassembled WGS sequence. DR Bgee; ENSRNOG00000011879; Expressed in Ammon's horn and 21 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:0008134; F:transcription factor binding; IBA:GO_Central. 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 COMPBIAS 678..1511 FT /note="Gln-rich" 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 //