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O00584 (RNT2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribonuclease T2

EC=3.1.27.-
Alternative name(s):
Ribonuclease 6
Gene names
Name:RNASET2
Synonyms:RNASE6PL
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length256 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Has ribonuclease activity, with higher activity at acidic pH. Probably is involved in lysosomal degradation of ribosomal RNA By similarity. Probably plays a role in cellular RNA catabolism. Ref.8 Ref.9 Ref.12

Enzyme regulation

Inhibited by Zn2+ and Cu2+. Ref.12

Subcellular location

Secreted. Lysosome lumen. Endoplasmic reticulum lumen. Note: Subcellular fractionation of transfected ovarian cancer cells reveals full-length RNASET2 in the endoplasmic reticulum fraction and the 2 smaller RNASET2 proteolytic products in the lysosome fraction. Ref.7 Ref.8 Ref.9 Ref.11

Tissue specificity

Ubiquitous. Higher expression levels observed in the temporal lobe and fetal brain. Ref.9

Involvement in disease

Leukoencephalopathy, cystic, without megalencephaly (LCWM) [MIM:612951]: An infantile-onset syndrome of cerebral leukoencephalopathy. Affected newborns develop microcephaly and neurologic abnormalities including psychomotor impairment, seizures and sensorineural hearing impairment. The brain shows multifocal white matter lesions, anterior temporal lobe subcortical cysts, pericystic abnormal myelination, ventriculomegaly and intracranial calcifications.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9 Ref.11

Sequence similarities

Belongs to the RNase T2 family.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O00584-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: O00584-2)

The sequence of this isoform differs from the canonical sequence as follows:
     88-121: DLLPEMRAYWPDVIHSFPNRSRFWKHEWEKHGTC → KNWMEITDSSLPSPSTLPIINIFYSVLHLLQLMN
     122-256: Missing.
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Chain25 – 256232Ribonuclease T2
PRO_0000030987

Sites

Active site651 By similarity
Active site1141 By similarity
Active site1181 By similarity

Amino acid modifications

Glycosylation761N-linked (GlcNAc...) Ref.12
Glycosylation1061N-linked (GlcNAc...) Ref.12
Glycosylation2121N-linked (GlcNAc...) Ref.12
Disulfide bond48 ↔ 55 Ref.12
Disulfide bond75 ↔ 121 Ref.12
Disulfide bond184 ↔ 241 Ref.12
Disulfide bond202 ↔ 213 Ref.12

Natural variations

Alternative sequence88 – 12134DLLPE…KHGTC → KNWMEITDSSLPSPSTLPII NIFYSVLHLLQLMN in isoform 2.
VSP_008405
Alternative sequence122 – 256135Missing in isoform 2.
VSP_008406
Natural variant1841C → R in LCWM; the loss of a disulfide bond may affect protein folding and stability; the protein is retained in the endoplasmic reticulum. Ref.9 Ref.11
VAR_063596
Natural variant2361R → W.
Corresponds to variant rs11159 [ dbSNP | Ensembl ].
VAR_013004

Secondary structure

................................ 256
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1999. Version 2.
Checksum: 7C8BB08B8ED853EB

FASTA25629,481
        10         20         30         40         50         60 
MRPAALRGAL LGCLCLALLC LGGADKRLRD NHEWKKLIMV QHWPETVCEK IQNDCRDPPD 

        70         80         90        100        110        120 
YWTIHGLWPD KSEGCNRSWP FNLEEIKDLL PEMRAYWPDV IHSFPNRSRF WKHEWEKHGT 

       130        140        150        160        170        180 
CAAQVDALNS QKKYFGRSLE LYRELDLNSV LLKLGIKPSI NYYQVADFKD ALARVYGVIP 

       190        200        210        220        230        240 
KIQCLPPSQD EEVQTIGQIE LCLTKQDQQL QNCTEPGEQP SPKQEVWLAN GAAESRGLRV 

       250 
CEDGPVFYPP PKKTKH 

« Hide

Isoform 2 [UniParc].

Checksum: 984FAD634B7286E8
Show »

FASTA12114,000

References

« Hide 'large scale' references
[1]"Mammalian Rh/T2/S-glycoprotein ribonuclease family genes: cloning of a human member located in a region of chromosome 6 (6q27) frequently deleted in human malignancies."
Trubia M., Sessa L., Taramelli R.
Genomics 42:342-344(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Physical and transcript map of the region between D6S264 and D6S149 on chromosome 6q27, the minimal region of allele loss in sporadic epithelial ovarian cancer."
Liu Y., Emilion G., Mungall A.J., Dunham I., Beck S., LeMeuth-Metzinger V., Shelling A.N., Charnock F.M., Ganesan T.S.
Oncogene 21:387-399(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[4]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Colon, Pancreas and Spleen.
[7]"Tumor and metastasis suppression by the human RNASET2 gene."
Acquati F., Possati L., Ferrante L., Campomenosi P., Talevi S., Bardelli S., Margiotta C., Russo A., Bortoletto E., Rocchetti R., Calza R., Cinquetti R., Monti L., Salis S., Barbanti-Brodano G., Taramelli R.
Int. J. Oncol. 26:1159-1168(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[8]"Characterization of RNASET2, the first human member of the Rh/T2/S family of glycoproteins."
Campomenosi P., Salis S., Lindqvist C., Mariani D., Nordstrom T., Acquati F., Taramelli R.
Arch. Biochem. Biophys. 449:17-26(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[9]"RNASET2-deficient cystic leukoencephalopathy resembles congenital cytomegalovirus brain infection."
Henneke M., Diekmann S., Ohlenbusch A., Kaiser J., Engelbrecht V., Kohlschutter A., Kratzner R., Madruga-Garrido M., Mayer M., Opitz L., Rodriguez D., Ruschendorf F., Schumacher J., Thiele H., Thoms S., Steinfeld R., Nurnberg P., Gartner J.
Nat. Genet. 41:773-775(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, VARIANT LCWM ARG-184, CHARACTERIZATION OF VARIANT LCWM ARG-184.
[10]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"rnaset2 mutant zebrafish model familial cystic leukoencephalopathy and reveal a role for RNase T2 in degrading ribosomal RNA."
Haud N., Kara F., Diekmann S., Henneke M., Willer J.R., Hillwig M.S., Gregg R.G., Macintosh G.C., Gartner J., Alia A., Hurlstone A.F.
Proc. Natl. Acad. Sci. U.S.A. 108:1099-1103(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT LCWM ARG-184.
[12]"Structure and activity of the only human RNase T2."
Thorn A., Steinfeld R., Ziegenbein M., Grapp M., Hsiao H.H., Urlaub H., Sheldrick G.M., Gartner J., Kratzner R.
Nucleic Acids Res. 40:8733-8742(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS) OF 25-256, GLYCOSYLATION AT ASN-76; ASN-106 AND ASN-212, FUNCTION, ENZYME REGULATION, DISULFIDE BONDS, IDENTIFICATION BY MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U85625 mRNA. Translation: AAC51363.2.
AJ419865 mRNA. Translation: CAD12030.1.
AJ419866 mRNA. Translation: CAD12031.1.
AK315467 mRNA. Translation: BAG37854.1.
AL133458, AL159163 Genomic DNA. Translation: CAI21600.1.
AL159163, AL133458 Genomic DNA. Translation: CAI15001.1.
CH471051 Genomic DNA. Translation: EAW47512.1.
CH471051 Genomic DNA. Translation: EAW47513.1.
CH471051 Genomic DNA. Translation: EAW47514.1.
BC001660 mRNA. Translation: AAH01660.1.
BC001819 mRNA. Translation: AAH01819.1.
BC039713 mRNA. Translation: AAH39713.1.
BC051912 mRNA. Translation: AAH51912.1.
PIRS78046.
RefSeqNP_003721.2. NM_003730.4.
UniGeneHs.529989.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3T0OX-ray1.59A25-256[»]
ProteinModelPortalO00584.
SMRO00584. Positions 34-252.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114188. 8 interactions.
IntActO00584. 5 interactions.
STRING9606.ENSP00000028008.

PTM databases

PhosphoSiteO00584.

Proteomic databases

PaxDbO00584.
PeptideAtlasO00584.
PRIDEO00584.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000421787; ENSP00000390833; ENSG00000026297. [O00584-2]
ENST00000476238; ENSP00000422846; ENSG00000026297. [O00584-1]
ENST00000508775; ENSP00000426455; ENSG00000026297. [O00584-1]
GeneID8635.
KEGGhsa:8635.
UCSCuc003qve.3. human. [O00584-1]

Organism-specific databases

CTD8635.
GeneCardsGC06M167342.
HGNCHGNC:21686. RNASET2.
HPAHPA029013.
MIM612944. gene.
612951. phenotype.
neXtProtNX_O00584.
Orphanet85136. Cystic leukoencephalopathy without megalencephaly.
PharmGKBPA128394541.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG285082.
HOVERGENHBG050037.
InParanoidO00584.
KOK01166.
OMAILTHHWP.
PhylomeDBO00584.
TreeFamTF315063.

Gene expression databases

ArrayExpressO00584.
BgeeO00584.
CleanExHS_RNASET2.
GenevestigatorO00584.

Family and domain databases

Gene3D3.90.730.10. 1 hit.
InterProIPR001568. RNase_T2-like.
IPR018188. RNase_T2_AS.
[Graphical view]
PANTHERPTHR11240. PTHR11240. 1 hit.
PfamPF00445. Ribonuclease_T2. 1 hit.
[Graphical view]
SUPFAMSSF55895. SSF55895. 1 hit.
PROSITEPS00530. RNASE_T2_1. 1 hit.
PS00531. RNASE_T2_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRNASET2. human.
GeneWikiRNASET2.
GenomeRNAi8635.
NextBio32371.
PROO00584.
SOURCESearch...

Entry information

Entry nameRNT2_HUMAN
AccessionPrimary (citable) accession number: O00584
Secondary accession number(s): B2RDA7 expand/collapse secondary AC list , E1P5C3, Q5T8Q0, Q8TCU2, Q9BZ46, Q9BZ47
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2002
Last sequence update: November 1, 1999
Last modified: April 16, 2014
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM