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Information on EC 4.6.1.19 - ribonuclease T2 and Organism(s) Danio rerio and UniProt Accession B8XY56
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4.6.1.19 ribonuclease T2IUBMB Comments
A widely distributed family of related enzymes found in protozoans, plants, bacteria, animals and viruses that cleave ssRNA 3'-phosphate group with little base specificity. The enzyme catalyses a two-stage endonucleolytic cleavage. The first reaction produces 5'-hydroxy-phosphooligonucletides and 3'-phosphooligonucleotides ending with a 2',3'-cyclic phosphodiester, which are released from the enzyme. The enzyme then hydrolyses the cyclic products in a second reaction that takes place only when all the susceptible 3',5'-phosphodiester bonds have been cyclised. The second reaction is a reversal of the first reaction using the hydroxyl group of water instead of the 5'-hydroxyl group of ribose. The overall process is that of a phosphorus-oxygen lyase followed by hydrolysis to form the 3'-nucleotides.
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Word Map
- 4.6.1.19
- oligoadenylate
-
endoribonuclease
- 2',5'-oligoadenylate
- viruses
- dsrna
-
single-stranded
-
interferon-induced
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2-5a-dependent
- s-rnases
-
ifn-induced
-
omega-3
- rhizopus
-
lauric
-
5'-phosphorylated
- polynucleotide
- niveus
- colicins
-
s-locus
-
interferon-regulated
- gametophytic
- rig-i
-
encephalomyocarditis
-
solanaceous
- oligoribonucleotides
-
ifn-beta
-
anticodons
-
dsrna-dependent
- pistil
-
self-compatible
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xenotropic
- alata
-
ifn-stimulated
-
omega-hydroxylation
-
dsrna-activated
-
dinucleoside
- polyu
-
interferon-treated
- biotechnology
- medicine
The taxonomic range for the selected organisms is: Danio rerio
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
hide(Overall reactions are displayed. Show all >>)
+
=
an [RNA fragment]-3'-nucleoside-3'-phosphate
+
a 5'-hydroxy-ribonucleotide-3'-[RNA fragment]
Synonyms
rnase l, omega-1, rnase t2, rnaset2, rnase i, acid rnase, ribonuclease l, rnase rh, acid ribonuclease, rnase m, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acid ribonuclease
-
-
-
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acid RNase
-
-
-
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base-non-specific ribonuclease
-
-
-
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Escherichia coli ribonuclease I
-
-
-
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non-base specific ribonuclease
-
-
-
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nonbase-specific RNase
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-
-
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nonspecific RNase
-
-
-
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nuclease, Escherichia coli ribo-, II
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-
-
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nuclease, ribo- (non-base specific)
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-
-
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ribonuclease (non-base specific)
-
-
-
-
ribonuclease II
-
-
-
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ribonuclease M
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-
-
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ribonuclease N2
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-
-
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ribonuclease PP2
-
-
-
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ribonuclease PP3
-
-
-
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ribonuclease U4
-
-
-
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ribonucleate 3'-oligonucleotide hydrolase
-
-
-
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ribonucleate nucleotido-2'-transferase (cyclizing)
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-
-
-
RNAase CL
-
-
-
-
RNase (non-base specific)
-
-
-
-
RNase II
-
-
-
-
RNase LE
-
-
-
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RNase LX
-
-
-
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RNase M
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-
-
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RNase MC
-
-
-
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RNase Ms
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-
-
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RNase T2
S1-RNase
-
-
-
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S2-RNase
-
-
-
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S3-RNase
-
-
-
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S4-RNase
-
-
-
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S5-RNase
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-
-
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S6-RNase
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-
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S7-RNase
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-
-
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RNase T2
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
[RNA] 5'-hydroxy-ribonucleotide-3'-[RNA fragment]-lyase (cyclicizing; [RNA fragment]-3'- nucleoside-2',3'-cyclophosphate-forming and hydrolysing)
A widely distributed family of related enzymes found in protozoans, plants, bacteria, animals and viruses that cleave ssRNA 3'-phosphate group with little base specificity. The enzyme catalyses a two-stage endonucleolytic cleavage. The first reaction produces 5'-hydroxy-phosphooligonucletides and 3'-phosphooligonucleotides ending with a 2',3'-cyclic phosphodiester, which are released from the enzyme. The enzyme then hydrolyses the cyclic products in a second reaction that takes place only when all the susceptible 3',5'-phosphodiester bonds have been cyclised. The second reaction is a reversal of the first reaction using the hydroxyl group of water instead of the 5'-hydroxyl group of ribose. The overall process is that of a phosphorus-oxygen lyase followed by hydrolysis to form the 3'-nucleotides.
CAS REGISTRY NUMBER
COMMENTARY
37278-25-4
-
9075-06-3
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
at an acidic pH stronger activities in the 20-30 kDa range that may correspond to RNase T2 enzymes
additional information
at an acidic pH stronger activities in the 20-30 kDa range that may correspond to RNase T2 enzymes
additional information
at an acidic pH stronger activities in the 20-30 kDa range that may correspond to RNase T2 enzymes
additional information
-
at an acidic pH stronger activities in the 20-30 kDa range that may correspond to RNase T2 enzymes
additional information
at an acidic pH stronger activities in the 20-30 kDa range that may correspond to RNase T2 enzymes
additional information
at an acidic pH stronger activities in the 20-30 kDa range that may correspond to RNase T2 enzymes
additional information
at an acidic pH stronger activities in the 20-30 kDa range that may correspond to RNase T2 enzymes
additional information
-
at an acidic pH stronger activities in the 20-30 kDa range that may correspond to RNase T2 enzymes
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
-
rnaset2 is expressed ubiquitously in zebrafish embryos and adults from conception
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
the zebrafish genome contains two RNase T2 genes, RNase Dre1 and RNase Dre2. These genes are part of two phylogenetic clades, one conserved in all chordates (the RNase Dre2 clade), and another fish-specific (the RNase Dre1 clade). RNase T2 enzymes carry out a housekeeping function
malfunction
-
loss of rnaset2 in mutant zebrafish results in accumulation of undigested rRNA within lysosomes within neurons of the brain, the mutants show white matter lesions correlating with accumulation of amyloid precursor protein and astrocytes at sites of neurodegeneration
physiological function
the zebrafish genome contains two RNase T2 genes, RNase Dre1 and RNase Dre2. These genes are part of two phylogenetic clades, one conserved in all chordates (the RNase Dre2 clade), and another fish-specific (the RNase Dre1 clade). RNase T2 enzymes carry out a housekeeping function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). RNT2_DANRE
240
0
27456
Swiss-Prot
Secretory Pathway (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
23700
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C184R
-
RNASET2C184R, harboring a missense mutation as identified from a patient with cystic leukoencephalopathy, signal is retained within the endoplasmic reticulum
T304A
-
naturally occuring mutation, inactivce mutant AO127. A mutation within codon 118 of the rnaset2 ORF creates a premature stop codon truncating the protein before its second conserved catalytic site, CAS II, resulting in loss of essential catalytic residues and results in a dramatic down-regulation of the rnaset2 messenger RNA
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
sequencing of a positional candidate zgc:113369, equivalent to rnaset2, expresison of myc-tagged wild-type and mutants in HEK-293 cells, phenotypes, overview
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
RNase Dre2 expressed in all developmental stages and peaking at 72 h, signal is lower at 5 and 12 h
strong expression of RNase Dre1 during all developmental stages analyzed (2, 5, 12, 24, 72 h after fertilization), with a peak of expression at 72 hours
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hillwig, M.; Rizhsky, L.; Wang, Y.; Umanskaya, A.; Essner, J.; MacIntosh, G.
Zebrafish RNase T2 genes and the evolution of secretory ribonucleases in animals
BMC Evol. Biol.
9
170
2009
Danio rerio (B8XY54), Danio rerio (B8XY55), Danio rerio (B8XY56), Danio rerio
Haud, N.; Kara, F.; Diekmann, S.; Henneke, M.; Willer, J.R.; Hillwig, M.S.; Gregg, R.G.; Macintosh, G.C.; Gaertner, J.; Alia, A.; Hurlstone, A.F.
rnaset2 mutant zebrafish model familial cystic leukoencephalopathy and reveal a role for RNase T2 in degrading ribosomal RNA
Proc. Natl. Acad. Sci. USA
108
1099-1103
2011
Danio rerio
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