RNT2_HUMAN
ID RNT2_HUMAN Reviewed; 256 AA.
AC O00584; B2RDA7; E1P5C3; Q5T8Q0; Q8TCU2; Q9BZ46; Q9BZ47;
DT 03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Ribonuclease T2;
DE EC=4.6.1.19 {ECO:0000255|PROSITE-ProRule:PRU10046};
DE AltName: Full=Ribonuclease 6;
DE Flags: Precursor;
GN Name=RNASET2; Synonyms=RNASE6PL;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=9192857; DOI=10.1006/geno.1997.4679;
RA Trubia M., Sessa L., Taramelli R.;
RT "Mammalian Rh/T2/S-glycoprotein ribonuclease family genes: cloning of a
RT human member located in a region of chromosome 6 (6q27) frequently deleted
RT in human malignancies.";
RL Genomics 42:342-344(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RX PubMed=11821951; DOI=10.1038/sj.onc.1205067;
RA Liu Y., Emilion G., Mungall A.J., Dunham I., Beck S., LeMeuth-Metzinger V.,
RA Shelling A.N., Charnock F.M., Ganesan T.S.;
RT "Physical and transcript map of the region between D6S264 and D6S149 on
RT chromosome 6q27, the minimal region of allele loss in sporadic epithelial
RT ovarian cancer.";
RL Oncogene 21:387-399(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon, Pancreas, and Spleen;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=15809705;
RA Acquati F., Possati L., Ferrante L., Campomenosi P., Talevi S.,
RA Bardelli S., Margiotta C., Russo A., Bortoletto E., Rocchetti R., Calza R.,
RA Cinquetti R., Monti L., Salis S., Barbanti-Brodano G., Taramelli R.;
RT "Tumor and metastasis suppression by the human RNASET2 gene.";
RL Int. J. Oncol. 26:1159-1168(2005).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16620762; DOI=10.1016/j.abb.2006.02.022;
RA Campomenosi P., Salis S., Lindqvist C., Mariani D., Nordstrom T.,
RA Acquati F., Taramelli R.;
RT "Characterization of RNASET2, the first human member of the Rh/T2/S family
RT of glycoproteins.";
RL Arch. Biochem. Biophys. 449:17-26(2006).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, VARIANT LCWM ARG-184,
RP AND CHARACTERIZATION OF VARIANT LCWM ARG-184.
RX PubMed=19525954; DOI=10.1038/ng.398;
RA Henneke M., Diekmann S., Ohlenbusch A., Kaiser J., Engelbrecht V.,
RA Kohlschutter A., Kratzner R., Madruga-Garrido M., Mayer M., Opitz L.,
RA Rodriguez D., Ruschendorf F., Schumacher J., Thiele H., Thoms S.,
RA Steinfeld R., Nurnberg P., Gartner J.;
RT "RNASET2-deficient cystic leukoencephalopathy resembles congenital
RT cytomegalovirus brain infection.";
RL Nat. Genet. 41:773-775(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP SUBCELLULAR LOCATION, AND CHARACTERIZATION OF VARIANT LCWM ARG-184.
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).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, AND CHARACTERIZATION OF VARIANT ARG-184.
RX PubMed=28730546; DOI=10.1007/s13238-017-0448-9;
RA Liu P., Huang J., Zheng Q., Xie L., Lu X., Jin J., Wang G.;
RT "Mammalian mitochondrial RNAs are degraded in the mitochondrial
RT intermembrane space by RNASET2.";
RL Protein Cell 8:735-749(2017).
RN [14]
RP FUNCTION, MUTAGENESIS OF HIS-65 AND HIS-118, AND SUBCELLULAR LOCATION.
RX PubMed=30385512; DOI=10.1074/jbc.ra118.005433;
RA Huang J., Liu P., Wang G.;
RT "Regulation of mitochondrion-associated cytosolic ribosomes by mammalian
RT mitochondrial ribonuclease T2 (RNASET2).";
RL J. Biol. Chem. 293:19633-19644(2018).
RN [15]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=30184494; DOI=10.1016/j.celrep.2018.08.003;
RA Cheng Y., Liu P., Zheng Q., Gao G., Yuan J., Wang P., Huang J., Xie L.,
RA Lu X., Tong T., Chen J., Lu Z., Guan J., Wang G.;
RT "Mitochondrial Trafficking and Processing of Telomerase RNA TERC.";
RL Cell Rep. 24:2589-2595(2018).
RN [16]
RP FUNCTION.
RX PubMed=31778653; DOI=10.1016/j.cell.2019.11.001;
RA Greulich W., Wagner M., Gaidt M.M., Stafford C., Cheng Y., Linder A.,
RA Carell T., Hornung V.;
RT "TLR8 Is a Sensor of RNase T2 Degradation Products.";
RL Cell 179:1264-1275.E13(2019).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS) OF 25-256, GLYCOSYLATION AT ASN-76;
RP ASN-106 AND ASN-212, FUNCTION, ACTIVITY REGULATION, DISULFIDE BONDS, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=22735700; DOI=10.1093/nar/gks614;
RA Thorn A., Steinfeld R., Ziegenbein M., Grapp M., Hsiao H.H., Urlaub H.,
RA Sheldrick G.M., Gartner J., Kratzner R.;
RT "Structure and activity of the only human RNase T2.";
RL Nucleic Acids Res. 40:8733-8742(2012).
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 (PubMed:31778653). Cleaves
CC preferentially single-stranded RNA molecules between purine and uridine
CC residues, which critically contributes to the supply of catabolic
CC uridine and the generation of purine-2',3'-cyclophosphate-terminated
CC oligoribonucleotides (PubMed:31778653). In turn, RNase T2 degradation
CC products promote the RNA-dependent activation of TLR8
CC (PubMed:31778653). Also plays a key role in degradation of
CC mitochondrial RNA and processing of non-coding RNA imported from the
CC cytosol into mitochondria (PubMed:28730546, PubMed:30184494).
CC Participates as well in degradation of mitochondrion-associated
CC cytosolic rRNAs (PubMed:30385512). {ECO:0000269|PubMed:16620762,
CC ECO:0000269|PubMed:19525954, ECO:0000269|PubMed:22735700,
CC ECO:0000269|PubMed:28730546, ECO:0000269|PubMed:30184494,
CC ECO:0000269|PubMed:30385512, ECO:0000269|PubMed:31778653}.
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 -!- ACTIVITY REGULATION: Inhibited by Zn(2+) and Cu(2+).
CC {ECO:0000269|PubMed:22735700}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15809705,
CC ECO:0000269|PubMed:16620762}. Lysosome lumen
CC {ECO:0000269|PubMed:16620762}. Endoplasmic reticulum lumen
CC {ECO:0000269|PubMed:16620762}. Mitochondrion intermembrane space
CC {ECO:0000269|PubMed:28730546, ECO:0000269|PubMed:30184494,
CC ECO:0000269|PubMed:30385512}. Note=Full-length RNASET2 is found in the
CC endoplasmic reticulum while smaller RNASET2 proteolytic products are
CC found in the lysosome fraction. {ECO:0000269|PubMed:16620762}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O00584-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O00584-2; Sequence=VSP_008405, VSP_008406;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Higher expression levels observed in
CC the temporal lobe and fetal brain. {ECO:0000269|PubMed:19525954}.
CC -!- DISEASE: Leukoencephalopathy, cystic, without megalencephaly (LCWM)
CC [MIM:612951]: An infantile-onset syndrome of cerebral
CC leukoencephalopathy. Affected newborns develop microcephaly and
CC neurologic abnormalities including psychomotor impairment, seizures and
CC sensorineural hearing impairment. The brain shows multifocal white
CC matter lesions, anterior temporal lobe subcortical cysts, pericystic
CC abnormal myelination, ventriculomegaly and intracranial calcifications.
CC {ECO:0000269|PubMed:19525954, ECO:0000269|PubMed:21199949}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the RNase T2 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/RNASET2ID518ch6q27.html";
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DR EMBL; U85625; AAC51363.2; -; mRNA.
DR EMBL; AJ419865; CAD12030.1; -; mRNA.
DR EMBL; AJ419866; CAD12031.1; -; mRNA.
DR EMBL; AK315467; BAG37854.1; -; mRNA.
DR EMBL; AL133458; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL159163; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW47512.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW47513.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW47514.1; -; Genomic_DNA.
DR EMBL; BC001660; AAH01660.1; -; mRNA.
DR EMBL; BC001819; AAH01819.1; -; mRNA.
DR EMBL; BC039713; AAH39713.1; -; mRNA.
DR EMBL; BC051912; AAH51912.1; -; mRNA.
DR CCDS; CCDS5295.1; -. [O00584-1]
DR PIR; S78046; S78046.
DR RefSeq; NP_003721.2; NM_003730.4. [O00584-1]
DR PDB; 3T0O; X-ray; 1.59 A; A=25-256.
DR PDBsum; 3T0O; -.
DR AlphaFoldDB; O00584; -.
DR SMR; O00584; -.
DR BioGRID; 114188; 20.
DR IntAct; O00584; 7.
DR STRING; 9606.ENSP00000426455; -.
DR GlyConnect; 1719; 7 N-Linked glycans (2 sites).
DR GlyGen; O00584; 4 sites, 7 N-linked glycans (2 sites), 2 O-linked glycans (1 site).
DR iPTMnet; O00584; -.
DR PhosphoSitePlus; O00584; -.
DR SwissPalm; O00584; -.
DR BioMuta; RNASET2; -.
DR EPD; O00584; -.
DR jPOST; O00584; -.
DR MassIVE; O00584; -.
DR MaxQB; O00584; -.
DR PaxDb; O00584; -.
DR PeptideAtlas; O00584; -.
DR PRIDE; O00584; -.
DR ProteomicsDB; 47985; -. [O00584-1]
DR ProteomicsDB; 47986; -. [O00584-2]
DR Antibodypedia; 33528; 196 antibodies from 29 providers.
DR DNASU; 8635; -.
DR Ensembl; ENST00000421787.5; ENSP00000390833.1; ENSG00000026297.17. [O00584-2]
DR Ensembl; ENST00000476238.6; ENSP00000422846.1; ENSG00000026297.17. [O00584-1]
DR Ensembl; ENST00000508775.6; ENSP00000426455.2; ENSG00000026297.17. [O00584-1]
DR GeneID; 8635; -.
DR KEGG; hsa:8635; -.
DR MANE-Select; ENST00000508775.6; ENSP00000426455.2; NM_003730.6; NP_003721.2.
DR UCSC; uc003qve.4; human. [O00584-1]
DR CTD; 8635; -.
DR DisGeNET; 8635; -.
DR GeneCards; RNASET2; -.
DR HGNC; HGNC:21686; RNASET2.
DR HPA; ENSG00000026297; Low tissue specificity.
DR MalaCards; RNASET2; -.
DR MIM; 612944; gene.
DR MIM; 612951; phenotype.
DR neXtProt; NX_O00584; -.
DR OpenTargets; ENSG00000026297; -.
DR Orphanet; 85136; Cystic leukoencephalopathy without megalencephaly.
DR PharmGKB; PA128394541; -.
DR VEuPathDB; HostDB:ENSG00000026297; -.
DR eggNOG; KOG1642; Eukaryota.
DR GeneTree; ENSGT00640000091563; -.
DR HOGENOM; CLU_2037289_0_0_1; -.
DR InParanoid; O00584; -.
DR OrthoDB; 994722at2759; -.
DR PhylomeDB; O00584; -.
DR TreeFam; TF315063; -.
DR BRENDA; 4.6.1.19; 2681.
DR PathwayCommons; O00584; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; O00584; -.
DR BioGRID-ORCS; 8635; 15 hits in 1070 CRISPR screens.
DR ChiTaRS; RNASET2; human.
DR GeneWiki; RNASET2; -.
DR GenomeRNAi; 8635; -.
DR Pharos; O00584; Tbio.
DR PRO; PR:O00584; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; O00584; protein.
DR Bgee; ENSG00000026297; Expressed in right uterine tube and 200 other tissues.
DR ExpressionAtlas; O00584; baseline and differential.
DR Genevisible; O00584; HS.
DR GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0043202; C:lysosomal lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; IDA: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; IDA: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; IDA: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 3D-structure; Alternative splicing; Disease variant; Disulfide bond;
KW Endonuclease; Endoplasmic reticulum; Glycoprotein; Hydrolase; Immunity;
KW Innate immunity; Lyase; Lysosome; Mitochondrion; Nuclease;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..256
FT /note="Ribonuclease T2"
FT /id="PRO_0000030987"
FT ACT_SITE 65
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 CARBOHYD 76
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:22735700"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:22735700"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:22735700"
FT DISULFID 48..55
FT /evidence="ECO:0000269|PubMed:22735700"
FT DISULFID 75..121
FT /evidence="ECO:0000269|PubMed:22735700"
FT DISULFID 184..241
FT /evidence="ECO:0000269|PubMed:22735700"
FT DISULFID 202..213
FT /evidence="ECO:0000269|PubMed:22735700"
FT VAR_SEQ 88..121
FT /note="DLLPEMRAYWPDVIHSFPNRSRFWKHEWEKHGTC -> KNWMEITDSSLPSP
FT STLPIINIFYSVLHLLQLMN (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11821951"
FT /id="VSP_008405"
FT VAR_SEQ 122..256
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11821951"
FT /id="VSP_008406"
FT VARIANT 184
FT /note="C -> R (in LCWM; the loss of a disulfide bond may
FT affect protein folding and stability; the protein is
FT retained in the endoplasmic reticulum and the mitochondria
FT while lysosomal localization is disrupted;
FT dbSNP:rs121918137)"
FT /evidence="ECO:0000269|PubMed:19525954,
FT ECO:0000269|PubMed:21199949, ECO:0000269|PubMed:28730546"
FT /id="VAR_063596"
FT VARIANT 236
FT /note="R -> W (in dbSNP:rs11159)"
FT /id="VAR_013004"
FT MUTAGEN 65
FT /note="H->Y: Abolishes the effect on degradation of
FT mitochondrion-associated cytosolic rRNAs."
FT /evidence="ECO:0000269|PubMed:30385512"
FT MUTAGEN 118
FT /note="H->Y: Abolishes the effect on degradation of
FT mitochondrion-associated cytosolic rRNAs."
FT /evidence="ECO:0000269|PubMed:30385512"
FT STRAND 36..42
FT /evidence="ECO:0007829|PDB:3T0O"
FT HELIX 44..47
FT /evidence="ECO:0007829|PDB:3T0O"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:3T0O"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:3T0O"
FT STRAND 63..71
FT /evidence="ECO:0007829|PDB:3T0O"
FT HELIX 83..89
FT /evidence="ECO:0007829|PDB:3T0O"
FT HELIX 90..96
FT /evidence="ECO:0007829|PDB:3T0O"
FT HELIX 108..117
FT /evidence="ECO:0007829|PDB:3T0O"
FT HELIX 119..122
FT /evidence="ECO:0007829|PDB:3T0O"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:3T0O"
FT HELIX 131..145
FT /evidence="ECO:0007829|PDB:3T0O"
FT HELIX 147..153
FT /evidence="ECO:0007829|PDB:3T0O"
FT HELIX 165..176
FT /evidence="ECO:0007829|PDB:3T0O"
FT STRAND 181..185
FT /evidence="ECO:0007829|PDB:3T0O"
FT STRAND 195..204
FT /evidence="ECO:0007829|PDB:3T0O"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:3T0O"
FT STRAND 243..247
FT /evidence="ECO:0007829|PDB:3T0O"
SQ SEQUENCE 256 AA; 29481 MW; 7C8BB08B8ED853EB CRC64;
MRPAALRGAL LGCLCLALLC LGGADKRLRD NHEWKKLIMV QHWPETVCEK IQNDCRDPPD
YWTIHGLWPD KSEGCNRSWP FNLEEIKDLL PEMRAYWPDV IHSFPNRSRF WKHEWEKHGT
CAAQVDALNS QKKYFGRSLE LYRELDLNSV LLKLGIKPSI NYYQVADFKD ALARVYGVIP
KIQCLPPSQD EEVQTIGQIE LCLTKQDQQL QNCTEPGEQP SPKQEVWLAN GAAESRGLRV
CEDGPVFYPP PKKTKH
