Detail Information for IndEnz0002019031
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