| IED ID | IndEnz0002019031 |
| Enzyme Type ID | protease019031 |
| Protein Name |
Uridylate-specific endoribonuclease EC 4.6.1.- Placental protein 11 PP11 Protein endoU |
| Gene Name | ENDOU |
| Organism | Homo sapiens (Human) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MRACISLVLAVLCGLAWAGKIESCASRCNEKFNRDAACQCDRRCLWHGNCCEDYEHLCTEDHKESEPLPQLEEETEEALASNLYSAPTSCQGRCYEAFDKHHQCHCNARCQEFGNCCKDFESLCSDHEVSHSSDAITKEEIQSISEKIYRADTNKAQKEDIVLNSQNCISPSETRNQVDRCPKPLFTYVNEKLFSKPTYAAFINLLNNYQRATGHGEHFSAQELAEQDAFLREIMKTAVMKELYSFLHHQNRYGSEQEFVDDLKNMWFGLYSRGNEEGDSSGFEHVFSGEVKKGKVTGFHNWIRFYLEEKEGLVDYYSHIYDGPWDSYPDVLAMQFNWDGYYKEVGSAFIGSSPEFEFALYSLCFIARPGKVCQLSLGGYPLAVRTYTWDKSTYGNGKKYIATAYIVSST |
| Enzyme Length | 410 |
| Uniprot Accession Number | P21128 |
| Absorption | |
| Active Site | ACT_SITE 285; /evidence=ECO:0000255|PROSITE-ProRule:PRU01304; ACT_SITE 300; /evidence=ECO:0000255|PROSITE-ProRule:PRU01304; ACT_SITE 343; /evidence=ECO:0000255|PROSITE-ProRule:PRU01304 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=ribonucleotidyl-uridine-RNA = a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + a 5'-end dephospho-uridine-RNA; Xref=Rhea:RHEA:67792, Rhea:RHEA-COMP:10464, Rhea:RHEA-COMP:17354, Rhea:RHEA-COMP:17356, ChEBI:CHEBI:83064, ChEBI:CHEBI:173117, ChEBI:CHEBI:173224; Evidence={ECO:0000269|PubMed:18936097};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67793; Evidence={ECO:0000305|PubMed:18936097}; |
| DNA Binding | |
| EC Number | 4.6.1.- |
| Enzyme Function | FUNCTION: Endoribonuclease that cleaves single-stranded RNAs at 5' of uridylates and releases a product with a 2',3'-cyclic phosphate at the 3'-end. The UU and GU sites are more efficiently cleaved than CU and AU sites. {ECO:0000269|PubMed:18936097}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Alternative sequence (2); Chain (1); Disulfide bond (14); Domain (3); Mutagenesis (5); Sequence conflict (2); Signal peptide (1) |
| Keywords | Alternative splicing;Direct protein sequencing;Disulfide bond;Endonuclease;Hydrolase;Lyase;Manganese;Metal-binding;Nuclease;RNA-binding;Reference proteome;Repeat;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | PTM: It has been suggested that the active SMB domain may be permitted considerable disulfide bond heterogeneity or variability, thus two alternate disulfide patterns based on 3D structures are described with 1 disulfide bond conserved in both. |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000269|PubMed:2350438 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 18617639; 20379614; 33197855; 33511665; |
| Motif | |
| Gene Encoded By | |
| Mass | 46,872 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:67792; RHEA:67793 |
| Cross Reference Brenda |