SAE2_ARATH
ID SAE2_ARATH Reviewed; 700 AA.
AC Q9SJT1; Q84YI5; Q8GYC2; Q8LKN2;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=SUMO-activating enzyme subunit 2;
DE EC=2.3.2.-;
DE AltName: Full=Protein EMBRYO DEFECTIVE 2764;
DE AltName: Full=Ubiquitin-like 1-activating enzyme E1B;
GN Name=SAE2; Synonyms=EMB2764; OrderedLocusNames=At2g21470;
GN ORFNames=F3K23.23;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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] (ISOFORM 2).
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] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA De Los Reyes C., Quan R., Chen H., Bautista V.R., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 17-700 (ISOFORM 2).
RC STRAIN=cv. Columbia; TISSUE=Root;
RX PubMed=12482876; DOI=10.1074/jbc.m209694200;
RA Kurepa J., Walker J.M., Smalle J., Gosink M.M., Davis S.J., Durham T.L.,
RA Sung D.Y., Vierstra R.D.;
RT "The small ubiquitin-like modifier (SUMO) protein modification system in
RT Arabidopsis. Accumulation of SUMO1 and -2 conjugates is increased by
RT stress.";
RL J. Biol. Chem. 278:6862-6872(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 44-700 (ISOFORM 1).
RC STRAIN=cv. Columbia; TISSUE=Root;
RA Eldainasory M., Hager M., Abu Mager H., Elhashash E., Zaezae E.,
RA Elshami M.;
RT "Study on ubiquitin in Arabidopsis thaliana.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17644626; DOI=10.1104/pp.107.102285;
RA Saracco S.A., Miller M.J., Kurepa J., Vierstra R.D.;
RT "Genetic analysis of SUMOylation in Arabidopsis: conjugation of SUMO1 and
RT SUMO2 to nuclear proteins is essential.";
RL Plant Physiol. 145:119-134(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-678, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-678, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [10]
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: The dimeric enzyme acts as an E1 ligase for SUMO1 and SUMO2.
CC It mediates ATP-dependent activation of SUMO proteins and formation of
CC a thioester with a conserved cysteine residue on SAE2.
CC {ECO:0000269|PubMed:17644626}.
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC -!- SUBUNIT: Heterodimer of SAE1A or SAE1B and SAE2. The complex binds SUMO
CC proteins via SAE2 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9SJT1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9SJT1-2; Sequence=VSP_039565;
CC -!- DISRUPTION PHENOTYPE: Embryonic lethal. {ECO:0000269|PubMed:17644626}.
CC -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN03851.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR EMBL; AC006841; AAD23691.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07181.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07182.1; -; Genomic_DNA.
DR EMBL; AK117731; BAC42380.1; -; mRNA.
DR EMBL; BT044606; ACI31306.1; -; mRNA.
DR EMBL; AF510525; AAN03851.1; ALT_SEQ; mRNA.
DR EMBL; AJ520102; CAD67688.1; -; mRNA.
DR PIR; F84601; F84601.
DR RefSeq; NP_179742.2; NM_127719.4. [Q9SJT1-2]
DR RefSeq; NP_973506.1; NM_201777.1. [Q9SJT1-1]
DR PDB; 6GUM; X-ray; 1.79 A; B=437-700.
DR PDBsum; 6GUM; -.
DR AlphaFoldDB; Q9SJT1; -.
DR SMR; Q9SJT1; -.
DR BioGRID; 2039; 10.
DR STRING; 3702.AT2G21470.2; -.
DR iPTMnet; Q9SJT1; -.
DR PaxDb; Q9SJT1; -.
DR PRIDE; Q9SJT1; -.
DR ProteomicsDB; 232866; -. [Q9SJT1-1]
DR EnsemblPlants; AT2G21470.1; AT2G21470.1; AT2G21470. [Q9SJT1-2]
DR EnsemblPlants; AT2G21470.2; AT2G21470.2; AT2G21470. [Q9SJT1-1]
DR GeneID; 816686; -.
DR Gramene; AT2G21470.1; AT2G21470.1; AT2G21470. [Q9SJT1-2]
DR Gramene; AT2G21470.2; AT2G21470.2; AT2G21470. [Q9SJT1-1]
DR KEGG; ath:AT2G21470; -.
DR Araport; AT2G21470; -.
DR TAIR; locus:2050069; AT2G21470.
DR eggNOG; KOG2013; Eukaryota.
DR InParanoid; Q9SJT1; -.
DR OrthoDB; 686413at2759; -.
DR PhylomeDB; Q9SJT1; -.
DR UniPathway; UPA00886; -.
DR PRO; PR:Q9SJT1; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SJT1; baseline and differential.
DR Genevisible; Q9SJT1; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0031510; C:SUMO activating enzyme complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019948; F:SUMO activating enzyme activity; IDA:TAIR.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR GO; GO:0032446; P:protein modification by small protein conjugation; IBA:GO_Central.
DR GO; GO:0016925; P:protein sumoylation; IDA:TAIR.
DR Gene3D; 1.10.10.520; -; 1.
DR Gene3D; 3.50.50.80; -; 1.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR028077; UAE_UbL_dom.
DR InterPro; IPR042449; Ub-E1_IAD_1.
DR InterPro; IPR023318; Ub_act_enz_dom_a_sf.
DR InterPro; IPR019572; UBA_E1_SCCH.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR PANTHER; PTHR10953; PTHR10953; 1.
DR Pfam; PF00899; ThiF; 1.
DR Pfam; PF14732; UAE_UbL; 1.
DR Pfam; PF10585; UBA_e1_thiolCys; 1.
DR SUPFAM; SSF69572; SSF69572; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; ATP-binding;
KW Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transferase; Ubl conjugation pathway; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..700
FT /note="SUMO-activating enzyme subunit 2"
FT /id="PRO_0000396012"
FT REGION 200..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 614..700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..652
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..677
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 168
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000250"
FT BINDING 19..24
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 51..54
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 67
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 112..117
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 153
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 156
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 432
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 435
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 678
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157,
FT ECO:0007744|PubMed:19376835"
FT VAR_SEQ 532..606
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11910074,
FT ECO:0000303|PubMed:12482876, ECO:0000303|Ref.4"
FT /id="VSP_039565"
FT STRAND 440..444
FT /evidence="ECO:0007829|PDB:6GUM"
FT TURN 446..448
FT /evidence="ECO:0007829|PDB:6GUM"
FT HELIX 451..457
FT /evidence="ECO:0007829|PDB:6GUM"
FT TURN 458..462
FT /evidence="ECO:0007829|PDB:6GUM"
FT STRAND 466..472
FT /evidence="ECO:0007829|PDB:6GUM"
FT STRAND 475..479
FT /evidence="ECO:0007829|PDB:6GUM"
FT HELIX 486..496
FT /evidence="ECO:0007829|PDB:6GUM"
FT HELIX 500..502
FT /evidence="ECO:0007829|PDB:6GUM"
FT STRAND 503..505
FT /evidence="ECO:0007829|PDB:6GUM"
FT STRAND 512..520
FT /evidence="ECO:0007829|PDB:6GUM"
FT STRAND 523..530
FT /evidence="ECO:0007829|PDB:6GUM"
FT TURN 611..613
FT /evidence="ECO:0007829|PDB:6GUM"
FT STRAND 617..622
FT /evidence="ECO:0007829|PDB:6GUM"
SQ SEQUENCE 700 AA; 78526 MW; B96A697287F1CC1B CRC64;
MATQQQQSAI KGAKVLMVGA GGIGCELLKT LALSGFEDIH IIDMDTIEVS NLNRQFLFRR
SHVGQSKAKV ARDAVLRFRP NINIRSYHAN VKNPEFDVDF FKQFDVVLNG LDNLDARRHV
NRLCLAADVP LVESGTTGFL GQVTVHIKGK TECYECQTKP APKTYPVCTI TSTPTKFVHC
IVWAKDLLFA KLFGDKNQDN DLNVRSNNSA SSSKETEDVF ERSEDEDIEQ YGRKIYDHVF
GSNIEAALSN EETWKNRRRP RPIYSKDVLP ESLTQQNGST QNCSVTDGDL MVSAMPSLGL
KNPQELWGLT QNSLVFIEAL KLFFAKRKKE IGHLTFDKDD QLAVEFVTAA ANIRAESFGI
PLHSLFEAKG IAGNIVHAVA TTNAIIAGLI VIEAIKVLKK DVDKFRMTYC LEHPSKKLLL
MPIEPYEPNP ACYVCSETPL VLEINTRKSK LRDLVDKIVK TKLGMNLPLI MHGNSLLYEV
GDDLDDIMVA NYNANLEKYL SELPSPILNG SILTVEDLQQ ELSCKINVKH RFFSEILNPV
LNSVWFLIIL PSTFPKLFHF TESRNQDGLS LDIILGFSNV TIRRVLTMFE TGRRLTHPLL
ILFCHREEFD EEKEPEGMVL SGWTPSPATN GESASTSNNE NPVDVTESSS GSEPASKKRR
LSETEASNHK KETENVESED DDIMEVENPM MVSKKKIRVE
