RNT2B_MOUSE
ID RNT2B_MOUSE Reviewed; 259 AA.
AC C0HKG6; Q9CQ01;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2017, sequence version 1.
DT 03-AUG-2022, entry version 24.
DE RecName: Full=Ribonuclease T2-B {ECO:0000312|MGI:MGI:3702087};
DE EC=4.6.1.19 {ECO:0000255|PROSITE-ProRule:PRU10045};
DE AltName: Full=Ribonuclease 6-B {ECO:0000305};
DE Flags: Precursor;
GN Name=Rnaset2b {ECO:0000312|MGI:MGI:3702087};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC26326.1};
RC TISSUE=Skin {ECO:0000312|EMBL:BAC26326.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK029149; BAC26326.1; -; mRNA.
DR CCDS; CCDS37429.1; -.
DR RefSeq; NP_001077407.1; NM_001083938.2.
DR RefSeq; NP_080887.1; NM_026611.2.
DR AlphaFoldDB; C0HKG6; -.
DR SMR; C0HKG6; -.
DR GlyGen; C0HKG6; 3 sites.
DR jPOST; C0HKG6; -.
DR DNASU; 68195; -.
DR Ensembl; ENSMUST00000089119; ENSMUSP00000086519; ENSMUSG00000094724.
DR Ensembl; ENSMUST00000097420; ENSMUSP00000095031; ENSMUSG00000095687.
DR Ensembl; ENSMUST00000179728; ENSMUSP00000137303; ENSMUSG00000094724.
DR Ensembl; ENSMUST00000231550; ENSMUSP00000156290; ENSMUSG00000116876.
DR Ensembl; ENSMUST00000231927; ENSMUSP00000156083; ENSMUSG00000095687.
DR Ensembl; ENSMUST00000232307; ENSMUSP00000156372; ENSMUSG00000116988.
DR GeneID; 100037283; -.
DR GeneID; 68195; -.
DR KEGG; mmu:100037283; -.
DR KEGG; mmu:68195; -.
DR CTD; 100037283; -.
DR CTD; 68195; -.
DR MGI; MGI:3702087; Rnaset2b.
DR VEuPathDB; HostDB:ENSMUSG00000094724; -.
DR VEuPathDB; HostDB:ENSMUSG00000095687; -.
DR VEuPathDB; HostDB:ENSMUSG00000116876; -.
DR VEuPathDB; HostDB:ENSMUSG00000116988; -.
DR GeneTree; ENSGT00640000091563; -.
DR OMA; DMRRYWP; -.
DR OrthoDB; 994722at2759; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR ChiTaRS; Rnaset2b; mouse.
DR PRO; PR:C0HKG6; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; C0HKG6; protein.
DR Bgee; ENSMUSG00000094724; Expressed in right kidney and 109 other tissues.
DR ExpressionAtlas; C0HKG6; baseline and differential.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0043202; C:lysosomal lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; ISO:MGI.
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; ISO:MGI.
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; ISO:MGI.
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; Endoplasmic reticulum; Glycoprotein;
KW Hydrolase; Immunity; Innate immunity; Lyase; Lysosome; Mitochondrion;
KW Nuclease; Reference proteome; Secreted; Signal.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..259
FT /note="Ribonuclease T2-B"
FT /id="PRO_0000440153"
FT ACT_SITE 69
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10045"
FT ACT_SITE 118
FT /evidence="ECO:0000250|UniProtKB:P08056"
FT ACT_SITE 122
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10046"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 216
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 53..59
FT /evidence="ECO:0000250|UniProtKB:O00584"
FT DISULFID 79..125
FT /evidence="ECO:0000250|UniProtKB:O00584"
FT DISULFID 188..244
FT /evidence="ECO:0000250|UniProtKB:O00584"
FT DISULFID 206..217
FT /evidence="ECO:0000250|UniProtKB:O00584"
SQ SEQUENCE 259 AA; 29609 MW; E0A1C1BBBEAA5033 CRC64;
MAPAEARGAL PGWISVLGWG LALCSLCGAG PLWSGSHEWK KLILTQHWPP TVCKEVNSCQ
DSLDYWTIHG LWPDRAEDCN QSWHFNLDEI KDLLRDMKIY WPDVIHRSSN RSQFWKHEWV
KHGTCAAQVD ALNSEKKYFG KSLDLYKQID LNSVLQKFGI KPSINYYQLA DFKDALTRIY
GVVPKIQCLM PEQGESVQTV GQIELCFTKE DLHLRNCTEP GEQLSSRQEA WLAMEASTHG
MMVCEDGPIF YPPPTKTQH
