| IED ID | IndEnz0018000082 |
| Enzyme Type ID | peroxidase000082 |
| Protein Name |
Annexin D1 AnnAt1 Annexin A1 |
| Gene Name | ANN1 ANNAT1 ANX23-ATH ATOXY5 OXY5 At1g35720 F14D7.2 |
| 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 | MATLKVSDSVPAPSDDAEQLRTAFEGWGTNEDLIISILAHRSAEQRKVIRQAYHETYGEDLLKTLDKELSNDFERAILLWTLEPGERDALLANEATKRWTSSNQVLMEVACTRTSTQLLHARQAYHARYKKSLEEDVAHHTTGDFRKLLVSLVTSYRYEGDEVNMTLAKQEAKLVHEKIKDKHYNDEDVIRILSTRSKAQINATFNRYQDDHGEEILKSLEEGDDDDKFLALLRSTIQCLTRPELYFVDVLRSAINKTGTDEGALTRIVTTRAEIDLKVIGEEYQRRNSIPLEKAITKDTRGDYEKMLVALLGEDDA |
| Enzyme Length | 317 |
| Uniprot Accession Number | Q9SYT0 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Has a peroxidase activity. May act in counteracting oxidative stress. May also mediate regulated, targeted secretion of Golgi-derived vesicles during seedling development. {ECO:0000269|PubMed:15368128, ECO:0000269|PubMed:16153598}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Active at pH 7.0 and 9.0, but not at pH 5.5. {ECO:0000269|PubMed:16153598}; |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (2); Chain (1); Helix (20); Initiator methionine (1); Metal binding (9); Modified residue (9); Mutagenesis (1); Repeat (4); Sequence conflict (7); Turn (5) |
| Keywords | 3D-structure;Acetylation;Annexin;Calcium;Calcium/phospholipid-binding;Cytoplasm;Membrane;Metal-binding;Phosphoprotein;Reference proteome;Repeat;Stress response |
| Interact With | |
| Induction | INDUCTION: Up-regulated by cold, dehydration, salt, osmotic and oxidative stresses. Up-regulated by abscisic acid (ABA) and salicylic acid (SA). {ECO:0000269|PubMed:15161963, ECO:0000269|PubMed:16531057, ECO:0000269|PubMed:8855345}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm, cytosol. Membrane. Note=translocate from cytosol to membrane upon salt treatment; this translocation is calcium dependent. |
| Modified Residue | MOD_RES 2; /note=N-acetylalanine; /evidence=ECO:0007744|PubMed:22223895; MOD_RES 100; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:Q9XEE2; MOD_RES 102; /note=Phosphoserine; /evidence=ECO:0000269|PubMed:26452715; MOD_RES 112; /note=Phosphothreonine; /evidence=ECO:0000269|PubMed:26452715; MOD_RES 129; /note=Phosphotyrosine; /evidence=ECO:0000250|UniProtKB:Q9XEE2; MOD_RES 155; /note=Phosphoserine; /evidence=ECO:0000269|PubMed:26452715; MOD_RES 156; /note=Phosphotyrosine; /evidence=ECO:0000269|PubMed:26452715; MOD_RES 284; /note=Phosphotyrosine; /evidence=ECO:0000269|PubMed:26452715; MOD_RES 289; /note=Phosphoserine; /evidence=ECO:0000269|PubMed:26452715 |
| Post Translational Modification | PTM: Phosphorylated. |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 1YCN; 2Q4C; |
| Mapped Pubmed ID | 11378440; 11826309; 15028209; 15539469; 16207701; 16242667; 16287169; 16502469; 16526091; 17137349; 17151019; 17317660; 17452342; 17644812; 17850744; 17969875; 18319616; 18431481; 18538804; 18650403; 18775970; 19482919; 19887499; 20018591; 20215861; 20656895; 20706207; 21146842; 21166475; 21333657; 21798377; 22115780; 22442409; 22523205; 23281391; 23334891; 23886625; 24180429; 25587034; 26041321; 26732494; 27135495; 27247031; 27888535; 28627464; 28726305; 30018170; 31365744; 32849711; 33419052; 9069178; 9551087; |
| Motif | |
| Gene Encoded By | |
| Mass | 36,204 |
| Kinetics | |
| Metal Binding | METAL 24; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P93157; METAL 26; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P93157; METAL 28; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P93157; METAL 68; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:P93157; METAL 255; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P93157; METAL 259; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P93157; METAL 299; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:P93157; METAL 300; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P93157; METAL 305; /note=Calcium 3; /evidence=ECO:0000250|UniProtKB:P93157 |
| Rhea ID | |
| Cross Reference Brenda |