RNST2_CAEEL
ID RNST2_CAEEL Reviewed; 279 AA.
AC O61887;
DT 13-NOV-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Ribonuclease T2 protein rnst-2 {ECO:0000305};
DE EC=4.6.1.19 {ECO:0000255|PROSITE-ProRule:PRU10046};
DE AltName: Full=RNase T2 rnst-2 {ECO:0000305};
DE Flags: Precursor;
GN Name=rnst-2 {ECO:0000312|WormBase:K10C9.3};
GN ORFNames=K10C9.3 {ECO:0000312|WormBase:K10C9.3};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND MUTAGENESIS OF 56-GLN--ASN-279; HIS-118 AND GLY-119.
RX PubMed=30102152; DOI=10.7554/elife.36588;
RA Liu Y., Zou W., Yang P., Wang L., Ma Y., Zhang H., Wang X.;
RT "Autophagy-dependent ribosomal RNA degradation is essential for maintaining
RT nucleotide homeostasis during C. elegans development.";
RL Elife 7:0-0(2018).
CC -!- FUNCTION: Probable endoribonuclease involved in the autophagy-mediated
CC degradation of ribosomal RNA and ribosomal proteins in lysosomes.
CC {ECO:0000269|PubMed:30102152}.
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:PRU10046};
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:30102152}.
CC -!- TISSUE SPECIFICITY: Expressed in the pharynx, hypodermis, muscle cells,
CC sheath cells, intestinal cells, the vulva and tail regions.
CC {ECO:0000269|PubMed:30102152}.
CC -!- DEVELOPMENTAL STAGE: Expressed from embryogenesis to adulthood.
CC {ECO:0000269|PubMed:30102152}.
CC -!- SIMILARITY: Belongs to the RNase T2 family.
CC {ECO:0000255|RuleBase:RU004328}.
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DR EMBL; BX284605; CCD62615.1; -; Genomic_DNA.
DR PIR; T33210; T33210.
DR PIR; T33212; T33212.
DR RefSeq; NP_503370.1; NM_070969.4.
DR AlphaFoldDB; O61887; -.
DR SMR; O61887; -.
DR IntAct; O61887; 1.
DR STRING; 6239.K10C9.3; -.
DR EPD; O61887; -.
DR PaxDb; O61887; -.
DR PeptideAtlas; O61887; -.
DR EnsemblMetazoa; K10C9.3.1; K10C9.3.1; WBGene00019624.
DR GeneID; 190096; -.
DR KEGG; cel:CELE_K10C9.3; -.
DR UCSC; K10C9.3; c. elegans.
DR CTD; 190096; -.
DR WormBase; K10C9.3; CE28601; WBGene00019624; rnst-2.
DR eggNOG; KOG1642; Eukaryota.
DR GeneTree; ENSGT00640000091563; -.
DR HOGENOM; CLU_069912_1_1_1; -.
DR InParanoid; O61887; -.
DR OMA; DMRRYWP; -.
DR OrthoDB; 994722at2759; -.
DR PhylomeDB; O61887; -.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR PRO; PR:O61887; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00019624; Expressed in embryo and 3 other tissues.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; 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 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 1: Evidence at protein level;
KW Disulfide bond; Endonuclease; Glycoprotein; Hydrolase; Lyase; Lysosome;
KW Nuclease; Reference proteome; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..279
FT /note="Ribonuclease T2 protein rnst-2"
FT /id="PRO_5004159398"
FT ACT_SITE 60
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10045"
FT ACT_SITE 114
FT /evidence="ECO:0000250|UniProtKB:P08056"
FT ACT_SITE 118
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10046,
FT ECO:0000305|PubMed:30102152"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 37..48
FT /evidence="ECO:0000250|UniProtKB:O00584"
FT DISULFID 200..210
FT /evidence="ECO:0000250|UniProtKB:O00584"
FT MUTAGEN 56..279
FT /note="Missing: In bp555; viable, but growth retarded
FT during embryogenesis and have a shorter lifespan. 20-30% of
FT animals exhibit embryonic lethality and 50% of hatched
FT embryos die during larval development. Lysosomal defects
FT characterized by an accumulation of ribosomal RNA and
FT ribosomal proteins in lysosomes throughout development,
FT which results in enlarged lysosomes."
FT /evidence="ECO:0000269|PubMed:30102152"
FT MUTAGEN 118
FT /note="H->A: Lysosomal defects; when associated with E-
FT 119."
FT /evidence="ECO:0000269|PubMed:30102152"
FT MUTAGEN 119
FT /note="G->E: In qx245; viable, but growth retarded during
FT embryogenesis and have a shorter lifespan. 20-30% of
FT animals exhibit embryonic lethality and 50% of hatched
FT embryos die during larval development. Lysosomal defects
FT characterized by an accumulation of ribosomal RNA and
FT ribosomal proteins in lysosomes throughout development,
FT which results in enlarged lysosomes. This defect is
FT suppressed in either an atg-2 bp576, epg-6 bp242 or lgg-1
FT bp500 mutant background. Lysosomal defects are not rescued;
FT when associated with A-118."
FT /evidence="ECO:0000269|PubMed:30102152"
SQ SEQUENCE 279 AA; 31477 MW; 5AD6F21AEAA67C7F CRC64;
MKLLLLLCIS CIPLAYSHDG EPFDYLMFTT IYPTAVCRAD DDSVPESCEI PSGTPQWSIH
GLWPNFENGS YPQNCRGTPR HFDENLIKSI EDRLVVVWPN LYPKKTIQSF WKHEYDKHGT
CAQSEKLFES ELAYFTEVMK VFDSIDVAGG LKSVGPSEKP ITSSDLKNAL SGVTSGKTFQ
FHCLRDKKTK QFLLGDIRLC LNKDLTIRDC PTDGKHPNRV SRFERSIGRN RRGPPLPSFQ
PCPAEFIYLP EMSSISKSSD STSPSIFGRI WSAIKNIGN
