IED ID | IndEnz0002007616 |
Enzyme Type ID | protease007616 |
Protein Name |
Protein RALF-like 1 Rapid alkalinization factor 1 AtRALF1 |
Gene Name | RALF1 RALFL1 At1g02900 F22D16.10 |
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 | MDKSFTLFLTLTILVVFIISSPPVQAGFANDLGGVAWATTGDNGSGCHGSIAECIGAEEEEMDSEINRRILATTKYISYQSLKRNSVPCSRRGASYYNCQNGAQANPYSRGCSKIARCRS |
Enzyme Length | 120 |
Uniprot Accession Number | Q9SRY3 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | |
Enzyme Function | FUNCTION: Cell signaling peptide that may regulate plant stress, growth, and development. Mediates a rapid alkalinization of extracellular space by mediating a transient increase in the cytoplasmic Ca(2+) concentration leading to a calcium-dependent signaling events through a cell surface receptor and a concomitant activation of some intracellular mitogen-activated protein kinases. Mostly active in roots. Prevents plant growth (e.g. root and leaf length). Suppresses cell elongation of the primary root by activating the cell surface receptor FER and triggering phosphorylation of AHA2 and subsequent extracellular alkalinization. {ECO:0000269|PubMed:18494498, ECO:0000269|PubMed:18775699, ECO:0000269|PubMed:24458638}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Chain (1); Disulfide bond (2); Glycosylation (1); Mutagenesis (1); Propeptide (1); Signal peptide (1); Site (1) |
Keywords | Direct protein sequencing;Disulfide bond;Glycoprotein;Hormone;Reference proteome;Secreted;Signal |
Interact With | Q9SCZ4 |
Induction | INDUCTION: More efficient to mediate cytoplasmic Ca(2+) accumulation when oxidized, but inactive when reduced. {ECO:0000269|PubMed:18494498}. |
Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. |
Modified Residue | |
Post Translational Modification | PTM: Proteolytically cleaved, probably by S1P, a subtilisin-like serine protease (subtilase). {ECO:0000269|PubMed:18775699}. |
Signal Peptide | SIGNAL 1..26; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 16173598; 16531500; 16673935; 23858430; 24620000; 25482784; 27155375; 27566404; 27930296; 28174582; 29028796; 29282286; 29301953; 29907954; 30124284; 30207378; 30339663; 31433471; 31904511; 31948398; 32083740; 32541006; 32559234; 32671204; |
Motif | |
Gene Encoded By | |
Mass | 12,967 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |