ENDOU
entrez
8909
canonical
uniprot
P21128
canonical
ensembl
ENSG00000111405
resolver
ensp
ENSP00000229003
resolver
ensp
ENSP00000397679
resolver
ensp
ENSP00000445004
resolver
genesymbol
ENDOU
resolver
hgnc
HGNC:14369
resolver
uniprot
B2RBJ3
resolver
uniprot
B3KQS7
resolver
uniprot
B7Z6E1
resolver
uniprot
Q2NKJ4
resolver
uniprot_entry
ENDOU_HUMAN
resolver
uniprot_sec
B2RBJ3
resolver
uniprot_sec
B3KQS7
resolver
uniprot_sec
B7Z6E1
resolver
uniprot_sec
Q2NKJ4
resolver
amino_acid_sequence
MRACISLVLAVLCGLAWAGKIESCASRCNEKFNRDAACQCDRRCLWHGNCCEDYEHLCTEDHKESEPLPQLEEETEEALASNLYSAPTSCQGRCYEAFDKHHQCHCNARCQEFGNCCKDFESLCSDHEVSHSSDAITKEEIQSISEKIYRADTNKAQKEDIVLNSQNCISPSETRNQVDRCPKPLFTYVNEKLFSKPTYAAFINLLNNYQRATGHGEHFSAQELAEQDAFLREIMKTAVMKELYSFLHHQNRYGSEQEFVDDLKNMWFGLYSRGNEEGDSSGFEHVFSGEVKKGKVTGFHNWIRFYLEEKEGLVDYYSHIYDGPWDSYPDVLAMQFNWDGYYKEVGSAFIGSSPEFEFALYSLCFIARPGKVCQLSLGGYPLAVRTYTWDKSTYGNGKKYIATAYIVSST
uniprot
proteins
ec_number
3.1.-.-
uniprot
proteins
ec_number
4.6.1.-
uniprot
proteins
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 (PubMed:18936097). Targets mRNAs to regulate their expression (PubMed:37803019). {ECO:0000269|PubMed:18936097, ECO:0000269|PubMed:37803019}.
uniprot
proteins
mass_dalton
46872
uniprot
proteins
mutagenesis
MUTAGEN 284; /note="E->Q: Abolishes endoribonuclease activity and increases RNA-binding activity."; /evidence="ECO:0000269|PubMed:18936097"; MUTAGEN 285; /note="H->A: Abolishes endoribonuclease activity without affecting RNA-binding activity."; /evidence="ECO:0000269|PubMed:18936097"; MUTAGEN 290; /note="E->Q: Abolishes endoribonuclease activity without affecting RNA-binding activity."; /evidence="ECO:0000269|PubMed:18936097"; MUTAGEN 300; /note="H->A: Abolishes endoribonuclease activity without affecting RNA-binding activity."; /evidence="ECO:0000269|PubMed:18936097"; MUTAGEN 343; /note="K->A: Strongly impairs endoribonuclease activity without affecting RNA-binding activity."; /evidence="ECO:0000269|PubMed:18936097
uniprot
proteins
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.
uniprot
proteins
protein_family
ENDOU family
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16541075
uniprot
proteins
pubmed
1710108
uniprot
proteins
pubmed
18936097
uniprot
proteins
pubmed
2350438
uniprot
proteins
pubmed
37803019
uniprot
proteins
sequence_length
410
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
uniprot
proteins