| IED ID | IndEnz0002002614 |
| Enzyme Type ID | protease002614 |
| Protein Name |
Aminopeptidase P1 AtAPP1 EC 3.4.11.9 |
| Gene Name | APP1 At4g36760 AP22.64 C7A10.600 |
| 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 | MSEILSSLRSLMASHSPPLDALVVPSEDYHQSEYVSARDKRREFVSGFSGSAGLALITKKEARLWTDGRYFLQALQQLSDEWTLMRMGEDPLVEVWMSDNLPEEANIGVDSWCVSVDTANRWGKSFAKKNQKLITTTTDLVDEVWKSRPPSEMSPVVVHPLEFAGRSVSHKFEDLRAKLKQEGARGLVIAALDEVAWLYNIRGTDVAYCPVVHAFAILTTDSAFLYVDKKKVSDEANSYFNGLGVEVREYTDVISDVALLASDRLISSFASKTVQHEAAKDMEIDSDQPDRLWVDPASCCYALYSKLDAEKVLLQPSPISLSKALKNPVELEGIKNAHVRDGAAVVQYLVWLDNQMQELYGASGYFLEAEASKKKPSETSKLTEVTVSDKLESLRASKEHFRGLSFPTISSVGSNAAVIHYSPEPEACAEMDPDKIYLCDSGAQYLDGTTDITRTVHFGKPSAHEKECYTAVFKGHVALGNARFPKGTNGYTLDILARAPLWKYGLDYRHGTGHGVGSYLCVHEGPHQVSFRPSARNVPLQATMTVTDEPGYYEDGNFGIRLENVLVVNDAETEFNFGDKGYLQFEHITWAPYQVKLIDLDELTREEIDWLNTYHSKCKDILAPFMNQTEMEWLKKATEPVSVSA |
| Enzyme Length | 645 |
| Uniprot Accession Number | F4JQH3 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by EGTA and apstatin, and, to some extent, by the flavonoid kaempferol. {ECO:0000269|PubMed:11891249}. |
| Binding Site | BINDING 69; /note=Substrate; /evidence=ECO:0000250|UniProtKB:O44750; BINDING 420; /note=Substrate; via tele nitrogen; /evidence=ECO:0000250|UniProtKB:O44750; BINDING 514; /note=Substrate; via tele nitrogen; /evidence=ECO:0000250|UniProtKB:O44750; BINDING 523; /note=Substrate; via tele nitrogen; /evidence=ECO:0000250|UniProtKB:O44750; BINDING 549; /note=Substrate; /evidence=ECO:0000250|UniProtKB:O44750 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide.; EC=3.4.11.9; Evidence={ECO:0000269|PubMed:11891249}; |
| DNA Binding | |
| EC Number | 3.4.11.9 |
| Enzyme Function | FUNCTION: Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Arg-Pro-Pro (By similarity). Aminopeptidase that binds to the auxin transport inhibitor N-1-naphthylphthalamic acid (NPA). May play a negative role in the regulation of PIN auxin transport proteins (PubMed:11891249). {ECO:0000250|UniProtKB:Q9VJG0, ECO:0000269|PubMed:11891249}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (1); Binding site (5); Chain (1); Initiator methionine (1); Metal binding (7); Modified residue (1); Sequence conflict (2) |
| Keywords | Acetylation;Alternative splicing;Aminopeptidase;Cell membrane;Cytoplasm;Direct protein sequencing;Endoplasmic reticulum;Glycoprotein;Hydrolase;Manganese;Membrane;Metal-binding;Metalloprotease;Microsome;Protease;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11891249}. Cell membrane {ECO:0000269|PubMed:11891249}; Peripheral membrane protein {ECO:0000303|PubMed:11891249}. Microsome membrane {ECO:0000269|PubMed:11891249}; Peripheral membrane protein {ECO:0000303|PubMed:11891249}. |
| Modified Residue | MOD_RES 2; /note=N-acetylserine; /evidence=ECO:0007744|PubMed:22223895 |
| Post Translational Modification | PTM: Glycosylated. Also present in a non-glycosylated form. {ECO:0000269|PubMed:11891249}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 15911562; 16258011; 18775970; 23148892; 27247031; 27583367; 28627464; 33042167; |
| Motif | |
| Gene Encoded By | |
| Mass | 71,993 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Vmax=36 nmol/min/mg enzyme for Tyr-aminofluoromethylcoumarin {ECO:0000269|PubMed:11891249}; Vmax=20 nmol/min/mg enzyme for Trp-aminofluoromethylcoumarin {ECO:0000269|PubMed:11891249}; Vmax=74 nmol/min/mg enzyme for Ala-Pro-aminofluoromethylcoumarin {ECO:0000269|PubMed:11891249}; Vmax=29 nmol/min/mg enzyme for Pro-aminofluoromethylcoumarin {ECO:0000269|PubMed:11891249}; |
| Metal Binding | METAL 440; /note=Manganese 1; /evidence=ECO:0000250|UniProtKB:Q9NQW7; METAL 451; /note=Manganese 1; /evidence=ECO:0000250|UniProtKB:Q9NQW7; METAL 451; /note=Manganese 2; /evidence=ECO:0000250|UniProtKB:Q9NQW7; METAL 514; /note=Manganese 2; via tele nitrogen; /evidence=ECO:0000250|UniProtKB:Q9NQW7; METAL 549; /note=Manganese 2; /evidence=ECO:0000250|UniProtKB:Q9NQW7; METAL 563; /note=Manganese 1; /evidence=ECO:0000250|UniProtKB:Q9NQW7; METAL 563; /note=Manganese 2; /evidence=ECO:0000250|UniProtKB:Q9NQW7 |
| Rhea ID | |
| Cross Reference Brenda |