Eri1
entrez
361159
canonical
uniprot
Q5FVR4
canonical
ensembl
ENSRNOG00000011448
resolver
ensembl
ENSRNOG00055012468
resolver
ensembl
ENSRNOG00060007146
resolver
ensembl
ENSRNOG00065002836
resolver
ensp
ENSRNOP00000015239
resolver
ensp
ENSRNOP00055017199
resolver
ensp
ENSRNOP00060008848
resolver
ensp
ENSRNOP00065002779
resolver
enst
ENSRNOT00000015239
resolver
enst
ENSRNOT00055021262
resolver
enst
ENSRNOT00060011749
resolver
enst
ENSRNOT00065003921
resolver
genesymbol
Eri1
resolver
genesymbol_syn
Thex1
resolver
uniprot_entry
ERI1_RAT
resolver
activity_regulation
ACTIVITY REGULATION: Although it can bind simultaneously with SLBP to the 3'-end of histone mRNA, the presence of SLBP prevents the exonuclease activity. {ECO:0000250|UniProtKB:Q8IV48}.
uniprot
proteins
amino_acid_sequence
MEDERGREHGGDAAQQKTPRPECEESRPLSVEKKQRCRLDGKDTDGSKFITSNGGDFSDPVYKEIAMTNGCINRMSKEELRAKLSEFKLETRGVKDVLKKRLKNYYKKQKLMLKESNAVDSYYDYICIIDFEATCEEGNPAEFLHEIIEFPVVLLNTHSLEIEDTFQQYVRPEVNSQLSEFCIGLTGITQDQVDRADAFPQVLKKVIEWMKSKELGTKYKYCILTDGSWDMSKFLNIQCQLSRLKYPSFAKKWINIRKSYGNFYKVPRSQTKLTIMLEKLGMDYDGRPHSGLDDSKNIARIAVRMLQDGCELRINEKLHGGQLMSVSSSLPVEGAPAPQMPHSRK
uniprot
proteins
ec_number
3.1.13.1
uniprot
proteins
function
FUNCTION: RNA exonuclease that binds to the 3'-end of histone mRNAs and degrades them, suggesting that it plays an essential role in histone mRNA decay after replication. A 2' and 3'-hydroxyl groups at the last nucleotide of the histone 3'-end is required for efficient 3'-end histone mRNA exonuclease activity and degradation of RNA substrates. Also able to degrade the 3'-overhangs of short interfering RNAs (siRNAs) in vitro, suggesting a possible role as regulator of RNA interference (RNAi). Required for binding the 5'-ACCCA-3' sequence present in stem-loop structure. Able to bind other mRNAs (By similarity). Required for 5.8S rRNA 3'-end processing. Also binds to 5.8s ribosomal RNA (By similarity). Binds with high affinity to the stem-loop structure of replication-dependent histone pre-mRNAs. In vitro, does not have sequence specificity. In vitro, has weak DNA exonuclease activity. In vitro, shows biphasic kinetics such that there is rapid hydrolysis of the last three unpaired RNA nucleotides in the 39 flanking sequence followed by a much slower cleavage through the stem that occurs over a longer incubation period in the order of hours (By similarity). ERI1-mediated RNA metabolism plays a key role in chondrogenesis (By similarity). {ECO:0000250|UniProtKB:Q7TMF2, ECO:0000250|UniProtKB:Q8IV48}.
uniprot
proteins
mass_dalton
39580
uniprot
proteins
pubmed
15489334
uniprot
proteins
sequence_length
345
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8IV48}. Nucleus {ECO:0000250|UniProtKB:Q8IV48}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q8IV48}.
uniprot
proteins