RNT2_DANRE
ID RNT2_DANRE Reviewed; 240 AA.
AC B8XY56; Q4V9G5;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Ribonuclease T2;
DE EC=4.6.1.19 {ECO:0000255|PROSITE-ProRule:PRU10045};
DE AltName: Full=RNase Dre2;
DE Flags: Precursor;
GN Name=rnaset2; Synonyms=dre2; ORFNames=zgc:113369;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=19619322; DOI=10.1186/1471-2148-9-170;
RA Hillwig M.S., Rizhsky L., Wang Y., Umanskaya A., Essner J.J.,
RA MacIntosh G.C.;
RT "Zebrafish RNase T2 genes and the evolution of secretory ribonucleases in
RT animals.";
RL BMC Evol. Biol. 9:170-170(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21199949; DOI=10.1073/pnas.1009811107;
RA Haud N., Kara F., Diekmann S., Henneke M., Willer J.R., Hillwig M.S.,
RA Gregg R.G., Macintosh G.C., Gartner J., Alia A., Hurlstone A.F.;
RT "rnaset2 mutant zebrafish model familial cystic leukoencephalopathy and
RT reveal a role for RNase T2 in degrading ribosomal RNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:1099-1103(2011).
CC -!- FUNCTION: Has ribonuclease activity, with higher activity at acidic pH.
CC Probably is involved in lysosomal degradation of ribosomal RNA.
CC {ECO:0000269|PubMed:21199949}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleotidyl-ribonucleotide-RNA + H2O = a 3'-end 3'-
CC phospho-ribonucleotide-RNA + a 5'-end dephospho-ribonucleoside-RNA +
CC H(+); Xref=Rhea:RHEA:68052, Rhea:RHEA-COMP:10463, Rhea:RHEA-
CC COMP:13936, Rhea:RHEA-COMP:17355, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:83062, ChEBI:CHEBI:138284,
CC ChEBI:CHEBI:173118; EC=4.6.1.19; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10045};
CC -!- SUBCELLULAR LOCATION: Lysosome lumen {ECO:0000250}. Endoplasmic
CC reticulum lumen {ECO:0000250}. Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:19619322}.
CC -!- DISRUPTION PHENOTYPE: AO127 mutants were identified based on increased
CC acridine orange uptake. AO127 mutants display enlarged lysosomes in
CC brain and lysosomal accumulation of undigested ribosomal RNA in brain
CC neurons, white matter lesions adjacent to brain ventricles, and
CC frequent focal white matter anomalies throughout the brain.
CC Nevertheless, mutants appear basically normal, reach normal adult size
CC and length, are fertile and do not display obvious gross motor
CC deficiencies. {ECO:0000269|PubMed:21199949}.
CC -!- SIMILARITY: Belongs to the RNase T2 family. {ECO:0000305}.
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DR EMBL; FJ460212; ACK38071.1; -; mRNA.
DR EMBL; BX255965; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC096907; AAH96907.1; -; mRNA.
DR RefSeq; NP_001025235.2; NM_001030064.2.
DR RefSeq; NP_001307320.1; NM_001320391.1.
DR AlphaFoldDB; B8XY56; -.
DR SMR; B8XY56; -.
DR STRING; 7955.ENSDARP00000107199; -.
DR PaxDb; B8XY56; -.
DR PeptideAtlas; B8XY56; -.
DR Ensembl; ENSDART00000128675; ENSDARP00000111898; ENSDARG00000036282.
DR Ensembl; ENSDART00000161443; ENSDARP00000132627; ENSDARG00000036282.
DR Ensembl; ENSDART00000164789; ENSDARP00000156176; ENSDARG00000036282.
DR Ensembl; ENSDART00000168608; ENSDARP00000141181; ENSDARG00000036282.
DR Ensembl; ENSDART00000178997; ENSDARP00000144562; ENSDARG00000036282.
DR GeneID; 791890; -.
DR KEGG; dre:791890; -.
DR CTD; 8635; -.
DR ZFIN; ZDB-GENE-030131-2513; rnaset2.
DR eggNOG; KOG1642; Eukaryota.
DR GeneTree; ENSGT00640000091563; -.
DR HOGENOM; CLU_069912_1_0_1; -.
DR InParanoid; B8XY56; -.
DR OMA; DMRRYWP; -.
DR OrthoDB; 994722at2759; -.
DR PhylomeDB; B8XY56; -.
DR TreeFam; TF315063; -.
DR BRENDA; 4.6.1.19; 928.
DR Reactome; R-DRE-6798695; Neutrophil degranulation.
DR PRO; PR:B8XY56; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 13.
DR Bgee; ENSDARG00000036282; Expressed in granulocyte and 24 other tissues.
DR ExpressionAtlas; B8XY56; baseline.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0043202; C:lysosomal lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0004521; F:endoribonuclease activity; IBA:GO_Central.
DR GO; GO:0033897; F:ribonuclease T2 activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0006401; P:RNA catabolic process; IBA:GO_Central.
DR GO; GO:0016075; P:rRNA catabolic process; IMP:ZFIN.
DR CDD; cd01061; RNase_T2_euk; 1.
DR Gene3D; 3.90.730.10; -; 1.
DR InterPro; IPR033697; Ribonuclease_T2_eukaryotic.
DR InterPro; IPR001568; RNase_T2-like.
DR InterPro; IPR036430; RNase_T2-like_sf.
DR InterPro; IPR018188; RNase_T2_His_AS_1.
DR InterPro; IPR033130; RNase_T2_His_AS_2.
DR PANTHER; PTHR11240; PTHR11240; 1.
DR Pfam; PF00445; Ribonuclease_T2; 1.
DR SUPFAM; SSF55895; SSF55895; 1.
DR PROSITE; PS00530; RNASE_T2_1; 1.
DR PROSITE; PS00531; RNASE_T2_2; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Endonuclease; Endoplasmic reticulum; Glycoprotein;
KW Hydrolase; Lyase; Lysosome; Nuclease; Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..240
FT /note="Ribonuclease T2"
FT /id="PRO_0000420169"
FT ACT_SITE 56
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10045"
FT ACT_SITE 103
FT /evidence="ECO:0000250|UniProtKB:P08056"
FT ACT_SITE 107
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10046"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 41..46
FT /evidence="ECO:0000250|UniProtKB:O00584"
FT DISULFID 66..110
FT /evidence="ECO:0000250|UniProtKB:O00584"
FT DISULFID 173..227
FT /evidence="ECO:0000250|UniProtKB:O00584"
FT DISULFID 191..201
FT /evidence="ECO:0000250|UniProtKB:O00584"
FT CONFLICT 45
FT /note="H -> Q (in Ref. 3; AAH96907)"
FT /evidence="ECO:0000305"
FT CONFLICT 153
FT /note="T -> S (in Ref. 3; AAH96907)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 240 AA; 27456 MW; 7FE633A83863D84B CRC64;
MRFIAFAVIF SAVYLCSSAF THPRGEWTKL ILTQHWPQTF CKMEHCKTDF SYWTLHGLWP
NTGVRCNTSW HFNASLIEDI LPEMEKFWPD LLEPSSPKFW NYEWTKHGTC AAKSESLNSE
HKYFGKALEL YHKFDLNSVL LKNQIVPSEK HYTLEDVEEA ITSAYGVKPK IQCVHPGQGG
QVQILGQIEI CVDRDFQLMG CEKSSEDTWS NDLPTVPVSG QSGLSVCDHS MPVYYPPVQA
