Detail Information for IndEnz0002010397
IED ID IndEnz0002010397
Enzyme Type ID protease010397
Protein Name Proteasome subunit alpha type-3
20S proteasome alpha subunit G-1
DiDi 17A-2a
Proteasome component 8
Proteasome subunit alpha type-7
Gene Name PAG1 PRC8 At2g27020 T20P8.7
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 MSSIGTGYDLSVTTFSPDGRVFQIEYAAKAVDNSGTVVGIKCKDGIVMGVEKLIASKMMLPGSNRRIHSVHRHAGMAVAGLAADGRQIVARAKSEARSYESVYGDAVPVKELSERVASYVHLCTLYWWLRPFGCGVILGGYDRDGPQLYMIEPSGISYRYFGAAIGKGKQAAKTEIEKLNLSEMTCKEGVIEVAKIIYKLHDEAKDKAFELEMSWICEESKREHQKVPDDLLEEAKTAAKTALEEMDAD
Enzyme Length 249
Uniprot Accession Number O23715
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (1); Cross-link (1); Initiator methionine (1); Modified residue (3); Sequence conflict (1)
Keywords Acetylation;Cytoplasm;Isopeptide bond;Nucleus;Proteasome;Reference proteome;Ubl conjugation
Interact With O23160
Induction INDUCTION: Induced by the endoparasitic nematode M.incognita. Levels increase after infection in both giants cells and endodermal cells of galls. Later confined to giant cells at high levels. {ECO:0000269|PubMed:11277426}.
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Modified Residue MOD_RES 2; /note=N-acetylserine; /evidence=ECO:0007744|PubMed:22223895; MOD_RES 214; /note=O-acetylserine; /evidence=ECO:0000269|PubMed:20516081; MOD_RES 220; /note=O-acetylserine; /evidence=ECO:0000269|PubMed:20516081
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 12952558; 14500793; 14617066; 15215502; 16055689; 16502469; 17151019; 17675552; 17825468; 18538804; 18805951; 20118269; 20405473; 28627464;
Motif
Gene Encoded By
Mass 27,377
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda