NSE2_ARATH
ID NSE2_ARATH Reviewed; 249 AA.
AC Q8GYH7; Q9LIM0;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=E3 SUMO-protein ligase MMS21;
DE EC=2.3.2.-;
DE AltName: Full=E3 SUMO-protein transferase MMS21 {ECO:0000305};
DE AltName: Full=MMS21 homolog;
DE Short=AtMMS21;
DE AltName: Full=Protein HIGH PLOIDY 2;
GN Name=MMS21; Synonyms=HPY2; OrderedLocusNames=At3g15150; ORFNames=F4B12.6;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF Clones.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, SUMOYLATION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF CYS-178 AND HIS-180.
RX PubMed=19666737; DOI=10.1105/tpc.109.068072;
RA Ishida T., Fujiwara S., Miura K., Stacey N., Yoshimura M., Schneider K.,
RA Adachi S., Minamisawa K., Umeda M., Sugimoto K.;
RT "SUMO E3 ligase HIGH PLOIDY2 regulates endocycle onset and meristem
RT maintenance in Arabidopsis.";
RL Plant Cell 21:2284-2297(2009).
RN [6]
RP FUNCTION, SUMOYLATION, INTERACTION WITH SCE1, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=19682286; DOI=10.1111/j.1365-313x.2009.03992.x;
RA Huang L., Yang S., Zhang S., Liu M., Lai J., Qi Y., Shi S., Wang J.,
RA Wang Y., Xie Q., Yang C.;
RT "The Arabidopsis SUMO E3 ligase AtMMS21, a homologue of NSE2/MMS21,
RT regulates cell proliferation in the root.";
RL Plant J. 60:666-678(2009).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: E3 SUMO-protein ligase that modulates cell cycle progression
CC and functions as a repressor of endocycle onset in meristems. May
CC function downstream of the meristem patterning transcription factors
CC PLETHORA 1 and 2 (PLT1 and PLT2) in root meristem development.
CC Modulates the expression of the mitotic cyclins CYCB1-1 and CYCB1-2 and
CC cyclin-dependent kinases CDKB1-1 and CDKB2-1 in root meristem. Involved
CC in cytokinin signaling in root development.
CC {ECO:0000269|PubMed:19666737, ECO:0000269|PubMed:19682286}.
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC -!- SUBUNIT: Interacts with SCE1. {ECO:0000269|PubMed:19682286}.
CC -!- INTERACTION:
CC Q8GYH7; Q9ZR37: DSPTP1; NbExp=3; IntAct=EBI-25512915, EBI-25512239;
CC Q8GYH7; Q9LQF0: TCP23; NbExp=3; IntAct=EBI-25512915, EBI-15192297;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19666737,
CC ECO:0000269|PubMed:19682286}. Cytoplasm {ECO:0000269|PubMed:19682286}.
CC -!- PTM: Sumoylated, possibly via autosumoylation.
CC {ECO:0000269|PubMed:19666737, ECO:0000269|PubMed:19682286}.
CC -!- DISRUPTION PHENOTYPE: Dwarf plants with short roots and defective
CC meristems. {ECO:0000269|PubMed:19666737, ECO:0000269|PubMed:19682286}.
CC -!- SIMILARITY: Belongs to the NSE2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB02569.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP001299; BAB02569.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE75625.1; -; Genomic_DNA.
DR EMBL; BT026417; ABH04524.1; -; mRNA.
DR EMBL; AK117616; BAC42272.1; -; mRNA.
DR RefSeq; NP_188133.2; NM_112378.3.
DR AlphaFoldDB; Q8GYH7; -.
DR SMR; Q8GYH7; -.
DR BioGRID; 6080; 4.
DR IntAct; Q8GYH7; 2.
DR STRING; 3702.AT3G15150.1; -.
DR iPTMnet; Q8GYH7; -.
DR PaxDb; Q8GYH7; -.
DR PRIDE; Q8GYH7; -.
DR ProteomicsDB; 249126; -.
DR EnsemblPlants; AT3G15150.1; AT3G15150.1; AT3G15150.
DR GeneID; 820746; -.
DR Gramene; AT3G15150.1; AT3G15150.1; AT3G15150.
DR KEGG; ath:AT3G15150; -.
DR Araport; AT3G15150; -.
DR TAIR; locus:2083641; AT3G15150.
DR eggNOG; KOG2979; Eukaryota.
DR HOGENOM; CLU_099247_0_0_1; -.
DR InParanoid; Q8GYH7; -.
DR OMA; IWNVHHA; -.
DR OrthoDB; 1434342at2759; -.
DR PhylomeDB; Q8GYH7; -.
DR UniPathway; UPA00886; -.
DR PRO; PR:Q8GYH7; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8GYH7; baseline and differential.
DR Genevisible; Q8GYH7; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0030915; C:Smc5-Smc6 complex; IBA:GO_Central.
DR GO; GO:0061665; F:SUMO ligase activity; IBA:GO_Central.
DR GO; GO:0019789; F:SUMO transferase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:TAIR.
DR GO; GO:0009736; P:cytokinin-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR GO; GO:0060250; P:germ-line stem-cell niche homeostasis; IMP:TAIR.
DR GO; GO:0032876; P:negative regulation of DNA endoreduplication; IMP:TAIR.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0080038; P:positive regulation of cytokinin-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:0045931; P:positive regulation of mitotic cell cycle; IMP:UniProtKB.
DR GO; GO:0016925; P:protein sumoylation; IDA:UniProtKB.
DR GO; GO:0048509; P:regulation of meristem development; IMP:TAIR.
DR GO; GO:0010082; P:regulation of root meristem growth; IMP:UniProtKB.
DR CDD; cd16651; SPL-RING_NSE2; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR026846; Nse2(Mms21).
DR InterPro; IPR004181; Znf_MIZ.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR21330; PTHR21330; 1.
DR Pfam; PF11789; zf-Nse; 1.
DR PROSITE; PS51044; ZF_SP_RING; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell cycle; Cytokinin signaling pathway; Cytoplasm;
KW Metal-binding; Nucleus; Reference proteome; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..249
FT /note="E3 SUMO-protein ligase MMS21"
FT /id="PRO_0000396014"
FT ZN_FING 141..228
FT /note="SP-RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT BINDING 178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT BINDING 180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT BINDING 199
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT BINDING 204
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MUTAGEN 178
FT /note="C->S: Loss of function; when associated with A-180."
FT /evidence="ECO:0000269|PubMed:19666737"
FT MUTAGEN 180
FT /note="H->A: Loss of function; when associated with S-178.
FT Loss of autosumoylation."
FT /evidence="ECO:0000269|PubMed:19666737"
SQ SEQUENCE 249 AA; 27717 MW; 5C48EE9FF9D70D88 CRC64;
MASASSSDGV AGRIQNASLV LVSDNSSTLA DIRKAVAMMK NIAVQLEKEN QTDKVKDLEN
SVAELLDLHS DCNHRSTAIQ SVANRYQPVE QLTDFKKLLD DEFTKLKATP SSVPQNDHLM
RQFREAVWNV HHAGEPMPGD DDEDIVMTST QCPLLNMTCP LSGKPVTELA DPVRSMDCRH
VYEKSVILHY IVNNPNANCP VAGCRGKLQN SKVICDAMLK FEIEEMRSLN KQSNRAEVIE
DFTEDVDED
