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O35291 (RNAS2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Non-secretory ribonuclease

EC=3.1.27.5
Alternative name(s):
Eosinophil cationic-type ribonuclease 4
MR-4
Ribonuclease 2
Short name=RNase 2
Gene names
Name:Rnase2
Synonyms:Ear4
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length155 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This is a non-secretory ribonuclease. It is a pyrimidine specific nuclease with a slight preference for U. Cytotoxin and helminthotoxin. Possesses a wide variety of biological activities.

Catalytic activity

Endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides ending in Cp or Up with 2',3'-cyclic phosphate intermediates.

Subunit structure

Interacts with and forms a tight 1:1 complex with RNH1. Dimerization of two such complexes may occur By similarity.

Subcellular location

Lysosome Probable. Cytoplasmic granule. Note: Matrix of eosinophil's large specific granule.

Sequence similarities

Belongs to the pancreatic ribonuclease family.

Ontologies

Keywords
   Cellular componentLysosome
   DomainSignal
   Molecular functionEndonuclease
Hydrolase
Nuclease
   PTMDisulfide bond
Glycoprotein
Nitration
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentlysosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionnucleic acid binding

Inferred from electronic annotation. Source: InterPro

pancreatic ribonuclease activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Potential
Chain26 – 155130Non-secretory ribonuclease
PRO_0000030882

Regions

Region62 – 665Substrate binding By similarity

Sites

Active site381Proton acceptor By similarity
Active site1501Proton donor By similarity
Binding site331Substrate By similarity

Amino acid modifications

Modified residue571Nitrated tyrosine By similarity
Glycosylation411N-linked (GlcNAc...) Potential
Glycosylation831N-linked (GlcNAc...) Potential
Glycosylation881N-linked (GlcNAc...) Potential
Glycosylation1071N-linked (GlcNAc...) Potential
Disulfide bond47 ↔ 106 By similarity
Disulfide bond61 ↔ 118 By similarity
Disulfide bond79 ↔ 133 By similarity
Disulfide bond86 ↔ 94 By similarity

Sequences

Sequence LengthMass (Da)Tools
O35291 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 36879AAF1CCFB961

FASTA15517,723
        10         20         30         40         50         60 
MGPKLLESRL CLLLLLGLVL MLASCQAQIL SQKFYTQHIY NSTYPRCDAV MRVVNRYRPR 

        70         80         90        100        110        120 
CKDINTFLHT SFADVVAVCG HPNITCNNLT RKNCHASSFQ VFITFCNLTM PTRICTQCRY 

       130        140        150 
QTTGSVKYYR VACENRTPQD TPMYPVVPVH LDGTF 

« Hide

References

[1]"Molecular cloning of four novel murine ribonuclease genes: unusual expansion within the ribonuclease A gene family."
Batten D., Dyer K.D., Domachowske J.B., Rosenberg H.F.
Nucleic Acids Res. 25:4235-4239(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Fibroblast.
[2]"Post-translational tyrosine nitration of eosinophil granule toxins mediated by eosinophil peroxidase."
Ulrich M., Petre A., Youhnovski N., Proemm F., Schirle M., Schumm M., Pero R.S., Doyle A., Checkel J., Kita H., Thiyagarajan N., Acharya K.R., Schmid-Grendelmeier P., Simon H.-U., Schwarz H., Tsutsui M., Shimokawa H., Bellon G. expand/collapse author list , Lee J.J., Przybylski M., Doering G.
J. Biol. Chem. 283:28629-28640(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NITRATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF017259 Genomic DNA. Translation: AAC53490.1.
RefSeqNP_001017422.1. NM_001017422.1.
UniGeneMm.377124.

3D structure databases

ProteinModelPortalO35291.
SMRO35291. Positions 31-152.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000056293.

PTM databases

PhosphoSiteO35291.

Proteomic databases

PRIDEO35291.

Protocols and materials databases

DNASU53877.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID53877.
KEGGmmu:53877.

Organism-specific databases

CTD53877.
MGIMGI:1858238. Ear4.

Phylogenomic databases

eggNOGNOG39501.
HOGENOMHOG000276882.
HOVERGENHBG008396.
InParanoidO35291.
PhylomeDBO35291.

Gene expression databases

GenevestigatorO35291.

Family and domain databases

Gene3D3.10.130.10. 1 hit.
InterProIPR001427. RNaseA.
IPR023411. RNaseA_AS.
IPR023412. RNaseA_domain.
[Graphical view]
PANTHERPTHR11437. PTHR11437. 1 hit.
PfamPF00074. RnaseA. 1 hit.
[Graphical view]
PRINTSPR00794. RIBONUCLEASE.
ProDomPD000535. RNaseA. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00092. RNAse_Pc. 1 hit.
[Graphical view]
SUPFAMSSF54076. SSF54076. 1 hit.
PROSITEPS00127. RNASE_PANCREATIC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio310745.
PROO35291.
SOURCESearch...

Entry information

Entry nameRNAS2_MOUSE
AccessionPrimary (citable) accession number: O35291
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 1, 1998
Last modified: April 16, 2014
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot