ID MTA2_MOUSE Reviewed; 668 AA. AC Q9R190; Q3TVT8; DT 28-FEB-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 24-JAN-2024, entry version 198. DE RecName: Full=Metastasis-associated protein MTA2; DE AltName: Full=Metastasis-associated 1-like 1; GN Name=Mta2; Synonyms=Mta1l1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBUNIT. RX PubMed=10444591; DOI=10.1101/gad.13.15.1924; RA Zhang Y., Ng H.-H., Erdjument-Bromage H., Tempst P., Bird A., Reinberg D.; RT "Analysis of the NuRD subunits reveals a histone deacetylase core complex RT and a connection with DNA methylation."; RL Genes Dev. 13:1924-1935(1999). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=129/SvJ; RX PubMed=11368903; DOI=10.1016/s0378-1119(01)00429-2; RA Xia L., Zhang Y.; RT "Sp1 and ETS family transcription factors regulate the mouse Mta2 gene RT expression."; RL Gene 268:77-85(2001). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION, AND SUBCELLULAR RP LOCATION. RC STRAIN=129/SvJ; TISSUE=Liver; RX PubMed=11749719; DOI=10.1089/104454901753340596; RA Matsusue K., Takiguchi S., Toh Y., Kono A.; RT "Characterization of mouse metastasis-associated gene 2: genomic structure, RT nuclear localization signal, and alternative potentials as transcriptional RT activator and repressor."; RL DNA Cell Biol. 20:603-611(2001). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J, and NOD; TISSUE=Amnion, and Thymus; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP INTERACTION WITH HDAC7. RX PubMed=10984530; DOI=10.1073/pnas.97.19.10330; RA Downes M., Ordentlich P., Kao H.-Y., Alvarez J.G.A., Evans R.M.; RT "Identification of a nuclear domain with deacetylase activity."; RL Proc. Natl. Acad. Sci. U.S.A. 97:10330-10335(2000). RN [7] RP INTERACTION WITH MBD3. RX PubMed=12124384; DOI=10.1074/jbc.m203455200; RA Saito M., Ishikawa F.; RT "The mCpG-binding domain of human MBD3 does not bind to mCpG but interacts RT with NuRD/Mi2 components HDAC1 and MTA2."; RL J. Biol. Chem. 277:35434-35439(2002). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54 AND SER-435, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Kidney, Lung, Pancreas, Spleen, RC and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [9] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-460; LYS-522 AND LYS-531, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [10] RP IDENTIFICATION IN THE NURD COMPLEX, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RX PubMed=27806305; DOI=10.1016/j.celrep.2016.10.022; RA Nitarska J., Smith J.G., Sherlock W.T., Hillege M.M., Nott A., RA Barshop W.D., Vashisht A.A., Wohlschlegel J.A., Mitter R., Riccio A.; RT "A Functional Switch of NuRD Chromatin Remodeling Complex Subunits RT Regulates Mouse Cortical Development."; RL Cell Rep. 17:1683-1698(2016). RN [11] RP INTERACTION WITH PWWP2B. RX PubMed=34180153; DOI=10.1002/advs.202102060; RA Yan L., Jin W., Zhao Q., Cui X., Shi T., Xu Y., Li F., Jin W., Zhang Z., RA Zhang Z., Tang Q.Q., Pan D.; RT "PWWP2B Fine-Tunes Adipose Thermogenesis by Stabilizing HDACs in a NuRD RT Subcomplex."; RL Adv. Sci. 8:e2102060-e2102060(2021). CC -!- FUNCTION: May function as a transcriptional coregulator (By CC similarity). Acts as a component of the histone deacetylase NuRD CC complex which participates in the remodeling of chromatin (By CC similarity). {ECO:0000250|UniProtKB:O94776}. CC -!- SUBUNIT: Component of the nucleosome remodeling and deacetylase (NuRD) CC repressor complex, composed of core proteins MTA1, MTA2, MTA3, RBBP4, CC RBBP7, HDAC1, HDAC2, MBD2, MBD3, and peripherally associated proteins CC CDK2AP1, CDK2AP2, GATAD2A, GATAD2B, CHD3, CHD4 and CHD5 CC (PubMed:10444591, PubMed:27806305). The exact stoichiometry of the NuRD CC complex is unknown, and some subunits such as MBD2 and MBD3, GATAD2A CC and GATAD2B, and CHD3, CHD4 and CHD5 define mutually exclusive NuRD CC complexes (PubMed:27806305). Interacts with CHD3 (By similarity). CC Interacts with CHD4 (By similarity). Interacts with GATAD2A (By CC similarity). Interacts with HDAC7 (PubMed:10984530). Interacts with CC MBD3 (PubMed:12124384). Interacts with p53/TP53 (By similarity). CC Interacts with MINT (By similarity). Interacts with PIMREG (By CC similarity). Interacts with NACC2 (By similarity). Interacts with ERCC6 CC (By similarity). Interacts with PWWP2B (PubMed:34180153). CC {ECO:0000250|UniProtKB:O94776, ECO:0000269|PubMed:10444591, CC ECO:0000269|PubMed:10984530, ECO:0000269|PubMed:12124384, CC ECO:0000269|PubMed:27806305, ECO:0000269|PubMed:34180153}. CC -!- INTERACTION: CC Q9R190; Q61539: Esrrb; NbExp=3; IntAct=EBI-904134, EBI-2312731; CC Q9R190; O09106: Hdac1; NbExp=7; IntAct=EBI-904134, EBI-301912; CC Q9R190; P70288: Hdac2; NbExp=7; IntAct=EBI-904134, EBI-302251; CC Q9R190; P12813: Nr4a1; NbExp=2; IntAct=EBI-904134, EBI-10896863; CC Q9R190; P20263: Pou5f1; NbExp=6; IntAct=EBI-904134, EBI-1606219; CC Q9R190; Q8BX22: Sall4; NbExp=3; IntAct=EBI-904134, EBI-2312582; CC Q9R190; Q8VI24: Satb2; NbExp=2; IntAct=EBI-904134, EBI-5737999; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00512, CC ECO:0000255|PROSITE-ProRule:PRU00624, ECO:0000269|PubMed:11749719}. 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; AF159259; AAD51281.1; -; mRNA. DR EMBL; AF348083; AAL30174.1; -; Genomic_DNA. DR EMBL; AB047977; BAB79231.1; -; Genomic_DNA. DR EMBL; AK088158; BAC40180.1; -; mRNA. DR EMBL; AK147099; BAE27675.1; -; mRNA. DR EMBL; AK159979; BAE35530.1; -; mRNA. DR EMBL; BC079847; AAH79847.1; -; mRNA. DR CCDS; CCDS29561.1; -. DR RefSeq; NP_035972.3; NM_011842.3. DR AlphaFoldDB; Q9R190; -. DR EMDB; EMD-21382; -. DR SMR; Q9R190; -. DR BioGRID; 204807; 56. DR ComplexPortal; CPX-953; MBD2/NuRD nucleosome remodeling and deacetylase complex. DR ComplexPortal; CPX-954; MBD3/NuRD nucleosome remodeling and deacetylase complex. DR CORUM; Q9R190; -. DR DIP; DIP-36630N; -. DR IntAct; Q9R190; 47. DR MINT; Q9R190; -. DR STRING; 10090.ENSMUSP00000093959; -. DR GlyGen; Q9R190; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9R190; -. DR MetOSite; Q9R190; -. DR PhosphoSitePlus; Q9R190; -. DR SwissPalm; Q9R190; -. DR REPRODUCTION-2DPAGE; IPI00128230; -. DR EPD; Q9R190; -. DR jPOST; Q9R190; -. DR MaxQB; Q9R190; -. DR PaxDb; 10090-ENSMUSP00000093959; -. DR PeptideAtlas; Q9R190; -. DR ProteomicsDB; 290211; -. DR Pumba; Q9R190; -. DR Antibodypedia; 1799; 473 antibodies from 41 providers. DR DNASU; 23942; -. DR Ensembl; ENSMUST00000096240.3; ENSMUSP00000093959.3; ENSMUSG00000071646.10. DR GeneID; 23942; -. DR KEGG; mmu:23942; -. DR UCSC; uc008gof.1; mouse. DR AGR; MGI:1346340; -. DR CTD; 9219; -. DR MGI; MGI:1346340; Mta2. DR VEuPathDB; HostDB:ENSMUSG00000071646; -. DR eggNOG; KOG3554; Eukaryota. DR GeneTree; ENSGT01030000234573; -. DR HOGENOM; CLU_006585_2_0_1; -. DR InParanoid; Q9R190; -. DR OMA; IRVGCKF; -. DR OrthoDB; 12566at2759; -. DR PhylomeDB; Q9R190; -. DR TreeFam; TF106444; -. DR Reactome; R-MMU-3214815; HDACs deacetylate histones. DR Reactome; R-MMU-6804758; Regulation of TP53 Activity through Acetylation. DR Reactome; R-MMU-73762; RNA Polymerase I Transcription Initiation. DR Reactome; R-MMU-8943724; Regulation of PTEN gene transcription. DR BioGRID-ORCS; 23942; 12 hits in 85 CRISPR screens. DR ChiTaRS; Mta2; mouse. DR PRO; PR:Q9R190; -. DR Proteomes; UP000000589; Chromosome 19. DR RNAct; Q9R190; Protein. DR Bgee; ENSMUSG00000071646; Expressed in retinal neural layer and 228 other cell types or tissues. DR GO; GO:0000781; C:chromosome, telomeric region; ISO:MGI. DR GO; GO:0000118; C:histone deacetylase complex; IDA:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0016581; C:NuRD complex; IDA:MGI. DR GO; GO:0005667; C:transcription regulator complex; ISO:MGI. DR GO; GO:0003682; F:chromatin binding; IEA:InterPro. DR GO; GO:0004407; F:histone deacetylase activity; IDA:MGI. DR GO; GO:0042826; F:histone deacetylase binding; ISO:MGI. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI. DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central. DR GO; GO:0003712; F:transcription coregulator activity; IDA:UniProtKB. DR GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central. DR GO; GO:0006338; P:chromatin remodeling; ISO:MGI. DR GO; GO:0051276; P:chromosome organization; TAS:MGI. DR GO; GO:0006306; P:DNA methylation; IMP:MGI. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; NAS:ComplexPortal. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI. DR GO; GO:0042659; P:regulation of cell fate specification; NAS:ComplexPortal. DR GO; GO:0010762; P:regulation of fibroblast migration; ISO:MGI. DR GO; GO:2000736; P:regulation of stem cell differentiation; NAS:ComplexPortal. DR CDD; cd04709; BAH_MTA; 1. DR CDD; cd11661; SANT_MTA3_like; 1. DR CDD; cd00202; ZnF_GATA; 1. DR Gene3D; 2.30.30.490; -; 1. DR Gene3D; 4.10.1240.50; -; 1. DR Gene3D; 1.10.10.60; Homeodomain-like; 1. DR InterPro; IPR001025; BAH_dom. DR InterPro; IPR043151; BAH_sf. DR InterPro; IPR000949; ELM2_dom. DR InterPro; IPR009057; Homeobox-like_sf. DR InterPro; IPR040138; MIER/MTA. DR InterPro; IPR035170; MTA1_R1. DR InterPro; IPR001005; SANT/Myb. DR InterPro; IPR017884; SANT_dom. DR InterPro; IPR000679; Znf_GATA. DR PANTHER; PTHR10865; METASTASIS-ASSOCIATED PROTEIN AND MESODERM INDUCTION EARLY RESPONSE PROTEIN; 1. DR PANTHER; PTHR10865:SF4; METASTASIS-ASSOCIATED PROTEIN MTA2; 1. DR Pfam; PF01426; BAH; 1. DR Pfam; PF01448; ELM2; 1. DR Pfam; PF00320; GATA; 1. DR Pfam; PF17226; MTA_R1; 1. DR Pfam; PF00249; Myb_DNA-binding; 1. DR SMART; SM00439; BAH; 1. DR SMART; SM01189; ELM2; 1. DR SMART; SM00717; SANT; 1. DR SMART; SM00401; ZnF_GATA; 1. DR SUPFAM; SSF46689; Homeodomain-like; 1. DR PROSITE; PS51038; BAH; 1. DR PROSITE; PS51156; ELM2; 1. DR PROSITE; PS51293; SANT; 1. DR Genevisible; Q9R190; MM. PE 1: Evidence at protein level; KW Acetylation; DNA-binding; Isopeptide bond; Metal-binding; Nucleus; KW Phosphoprotein; Reference proteome; Ubl conjugation; Zinc; Zinc-finger. FT CHAIN 1..668 FT /note="Metastasis-associated protein MTA2" FT /id="PRO_0000083497" FT DOMAIN 1..144 FT /note="BAH" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00370" FT DOMAIN 145..256 FT /note="ELM2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00512" FT DOMAIN 263..315 FT /note="SANT" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624" FT ZN_FING 367..394 FT /note="GATA-type; atypical" FT REGION 412..437 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 580..599 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 647..668 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 52 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O94776" FT MOD_RES 54 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 152 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:O94776" FT MOD_RES 433 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O94776" FT MOD_RES 435 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 460 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 522 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 531 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 534 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:O94776" FT CROSSLNK 492 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2 and SUMO3); alternate" FT /evidence="ECO:0000250" FT CROSSLNK 492 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:O94776" FT CROSSLNK 508 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:O94776" FT CROSSLNK 559 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:O94776" FT CROSSLNK 595 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:O94776" FT CONFLICT 489 FT /note="N -> I (in Ref. 4; BAC40180)" FT /evidence="ECO:0000305" SQ SEQUENCE 668 AA; 75030 MW; 88996F779BA6F4D1 CRC64; MAANMYRVGD YVYFENSSSN PYLVRRIEEL NKTANGNVEA KVVCLFRRRD ISSSLNSLAD SNAREFEEES KQPGVSEQQR HQLKHRELFL SRQFESLPAT HIRGKCSVTL LNETDILNQY LDKEDCFFYS LVFDPVQKTL LADQGEIRVG CKFQAEIPDR LAEGESDNRN QQKMEMKVWD PDNPLTDRQI DQFLVVARAV GTFARALDCS SSIRQPSLHM SAAAASRDIT LFHAMDTLQR NGYDLAKAMS TLVPQGGPVL CRDEMEEWSA SEAMLFEEAL EKYGKDFNDI RQDFLPWKSL ASIVQFYYMW KTTDRYIQQK RLKAAEADSK LKQVYIPTYT KPNPNQIISV GSKPGMNGAG FQKGLTCESC HTTQSAQWYA WGPPNMQCRL CASCWIYWKK YGGLKTPTQL EGAARGTTEP HSRGHLSRPE AQSLSPYTTS ANRAKLLAKN RQTFLLQTTK LTRLARRMCR DLLQPRRAAR RPYAPINANA IKAECSIRLP KAAKTPLKIH PLVRLPLATI VKDLVAQAPL KPKTPRGTKT PINRNQLTQN RGLGGIMVKR SYETMAGAGV PFSANGRPLA SGIRSSSQPA AKRQKLNPAD APNPVVFVAT KDTRALRKAL THLEMRRAAR RPNLPLKVKP TLMTVRPPVP LPASSHPAST NEPIVLED //