Detail Information for IndEnz0002019395
IED ID IndEnz0002019395
Enzyme Type ID protease019395
Protein Name Ubiquitin-like-specific protease ESD4
EC 3.4.22.68
Protein EARLY IN SHORT DAYS 4
AtESD4
Gene Name ESD4 At4g15880 dl3980w FCAALL.406
Organism Arabidopsis thaliana (Mouse-ear cress)
Taxonomic Lineage cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids malvids Brassicales Brassicaceae Camelineae Arabidopsis Arabidopsis thaliana (Mouse-ear cress)
Enzyme Sequence MGAVAINRKRSDESFNFINQQSTNPLRNSPYFQASKKRRFSFAMSEDSGKPASSNPTISRISRYPDAKAPLRREIHAPSRGILRYGKAKSNDYCEKDANFFVRKYDDAKRSALEALRFVNKGKDFVDLGDEVEKEEVVSDDSSVQAIEVIDCDDDEEKKNLQPSFSSGVTDVKKGENFRVEDTSMMLDSLSLDRDVDNDASSLEAYRKLMQSAEKRNSKLEALGFEIVLNEKKLSLLRQSRPKTVEKRVEVPREPFIPLTEDEEAEVYRAFSGRNRRKVLATHENSNIDITGEVLQCLTPSAWLNDEVINVYLELLKERETREPKKYLKCHYFNTFFYKKLVSDSGYNFKAVRRWTTQRKLGYALIDCDMIFVPIHRGVHWTLAVINNRESKLLYLDSLNGVDPMILNALAKYMGDEANEKSGKKIDANSWDMEFVEDLPQQKNGYDCGMFMLKYIDFFSRGLGLCFSQEHMPYFRLRTAKEILRLRAD
Enzyme Length 489
Uniprot Accession Number Q94F30
Absorption
Active Site ACT_SITE 380; /evidence=ECO:0000250; ACT_SITE 397; /evidence=ECO:0000250; ACT_SITE 448; /evidence=ECO:0000250
Activity Regulation ACTIVITY REGULATION: Inhibited by thiol reagent and N-ethylmaleimide, but not by ubiquitin aldehyde, pepstatin A or benzamidine HCl.
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Hydrolysis of the alpha-linked peptide bond in the sequence Gly-Gly-|-Ala-Thr-Tyr at the C-terminal end of the small ubiquitin-like modifier (SUMO) propeptide, Smt3, leading to the mature form of the protein. A second reaction involves the cleavage of an epsilon-linked peptide bond between the C-terminal glycine of the mature SUMO and the lysine epsilon-amino group of the target protein.; EC=3.4.22.68;
DNA Binding
EC Number 3.4.22.68
Enzyme Function FUNCTION: Protease that catalyzes two essential functions in the SUMO pathway: processing of full-length SUMOs to their mature forms and deconjugation of SUMO from targeted proteins. Cleaves precursors of SUM1 and SUM2, but not of SUM3 or SUM5. Able to release SUM1 and SUM2 from conjugates, but unable to cleave SUM3. Acts predominantly as an isopeptidase, cleaving SUMO-conjugated proteins better than SUMO peptides. Plays an important role in the control of flowering time. {ECO:0000269|PubMed:14507998, ECO:0000269|PubMed:16740136}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Chain (1); Coiled coil (1); Compositional bias (1); Erroneous gene model prediction (2); Mutagenesis (1); Region (1); Sequence conflict (2)
Keywords Coiled coil;Hydrolase;Membrane;Nucleus;Protease;Reference proteome;Thiol protease;Ubl conjugation pathway
Interact With
Induction INDUCTION: No circadian regulation. {ECO:0000269|PubMed:14507998}.
Subcellular Location SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000269|PubMed:14507998, ECO:0000269|PubMed:17513499}; Peripheral membrane protein {ECO:0000269|PubMed:14507998, ECO:0000269|PubMed:17513499}. Note=The nuclear envelope localization is independent of the presence of the nuclear pore anchor NUA.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 12403707; 18775970; 19151129; 19666737; 20074036; 20922545; 24816345; 26008766; 27247031; 28878488; 28979848; 33087527;
Motif
Gene Encoded By
Mass 56,426
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda 3.4.22.68;