RNT2_PIG
ID RNT2_PIG Reviewed; 200 AA.
AC Q7M329;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Ribonuclease T2;
DE EC=4.6.1.19 {ECO:0000255|PROSITE-ProRule:PRU10045};
GN Name=RNASET2;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP PROTEIN SEQUENCE.
RC TISSUE=Spleen;
RX PubMed=9657053; DOI=10.1248/bpb.21.634;
RA Iwama M., Kusano A., Ogawa Y., Ohgi K., Irie M.;
RT "A protease sensitive region of plant and aminal ribonucleases belonging to
RT the RNase T2 family.";
RL Biol. Pharm. Bull. 21:634-637(1998).
CC -!- FUNCTION: Ribonuclease that plays an essential role in innate immune
CC response by recognizing and degrading RNAs from microbial pathogens
CC that are subsequently sensed by TLR8. Cleaves preferentially single-
CC stranded RNA molecules between purine and uridine residues, which
CC critically contributes to the supply of catabolic uridine and the
CC generation of purine-2',3'-cyclophosphate-terminated
CC oligoribonucleotides. In turn, RNase T2 degradation products promote
CC the RNA-dependent activation of TLR8. Also plays a key role in
CC degradation of mitochondrial RNA and processing of non-coding RNA
CC imported from the cytosol into mitochondria. Participates as well in
CC degradation of mitochondrion-associated cytosolic rRNAs.
CC {ECO:0000250|UniProtKB:O00584}.
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 -!- ACTIVITY REGULATION: Inhibited by Zn(2+) and Cu(2+).
CC {ECO:0000250|UniProtKB:O00584}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:O00584}. Lysosome
CC lumen {ECO:0000250|UniProtKB:O00584}. Endoplasmic reticulum lumen
CC {ECO:0000250|UniProtKB:O00584}. Mitochondrion intermembrane space
CC {ECO:0000250|UniProtKB:O00584}.
CC -!- SIMILARITY: Belongs to the RNase T2 family. {ECO:0000305}.
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DR PIR; JE0172; JE0172.
DR AlphaFoldDB; Q7M329; -.
DR SMR; Q7M329; -.
DR STRING; 9823.ENSSSCP00000004349; -.
DR PaxDb; Q7M329; -.
DR PeptideAtlas; Q7M329; -.
DR PRIDE; Q7M329; -.
DR eggNOG; KOG1642; Eukaryota.
DR InParanoid; Q7M329; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0043202; C:lysosomal lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR GO; GO:0004521; F:endoribonuclease activity; IBA:GO_Central.
DR GO; GO:0004540; F:ribonuclease activity; ISS:UniProtKB.
DR GO; GO:0033897; F:ribonuclease T2 activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0006401; P:RNA catabolic process; ISS:UniProtKB.
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 Direct protein sequencing; Disulfide bond; Endonuclease;
KW Endoplasmic reticulum; Glycoprotein; Hydrolase; Immunity; Innate immunity;
KW Lyase; Lysosome; Mitochondrion; Nuclease; Reference proteome; Secreted.
FT CHAIN 1..200
FT /note="Ribonuclease T2"
FT /id="PRO_0000206509"
FT ACT_SITE 32
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10045"
FT ACT_SITE 82
FT /evidence="ECO:0000250|UniProtKB:P08056"
FT ACT_SITE 86
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10046"
FT CARBOHYD 43
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 17..22
FT /evidence="ECO:0000250|UniProtKB:O00584"
FT DISULFID 42..89
FT /evidence="ECO:0000250|UniProtKB:O00584"
FT DISULFID 152..188
FT /evidence="ECO:0000250|UniProtKB:O00584"
FT DISULFID 170..180
FT /evidence="ECO:0000250|UniProtKB:O00584"
SQ SEQUENCE 200 AA; 23136 MW; B7C37EE3AB79B673 CRC64;
HEWKKLIMVH HWPMTVCNEK NCEHPPDYWT IHGLWPDKSG ECNRSWPFNP DEIKGLLPDM
RLYWPDVLHS SPNHSVHFWR HEWEKHGTCA AQLDALNSQR KYFGKTLDLY KELALNSTLQ
KLGIKPSISY YQISDIKHAL VGVYGVVPKV QCLPPKSGEK VQTLGQIELC LTRDLQLQDC
PEPGLEICED GPVFYPPPKE
