Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Non-secretory ribonuclease

Gene

Rnase2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei33SubstrateBy similarity1
Active sitei38Proton acceptorBy similarity1
Active sitei150Proton donorBy similarity1

GO - Molecular functioni

Keywordsi

Molecular functionEndonuclease, Hydrolase, Nuclease

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Rnase2
Synonyms:Ear4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1858238. Ear4.

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Lysosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 25Sequence analysisAdd BLAST25
ChainiPRO_000003088226 – 155Non-secretory ribonucleaseAdd BLAST130

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi41N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi47 ↔ 106By similarity
Modified residuei57Nitrated tyrosineBy similarity1
Disulfide bondi61 ↔ 118By similarity
Disulfide bondi79 ↔ 133By similarity
Glycosylationi83N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi86 ↔ 94By similarity
Glycosylationi88N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi107N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein, Nitration

Proteomic databases

PRIDEiO35291.

PTM databases

PhosphoSitePlusiO35291.

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliO35291.
SMRiO35291.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni62 – 66Substrate bindingBy similarity5

Sequence similaritiesi

Belongs to the pancreatic ribonuclease family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000276882.
HOVERGENiHBG008396.
InParanoidiO35291.
KOiK01168.
PhylomeDBiO35291.

Family and domain databases

Gene3Di3.10.130.10. 1 hit.
InterProiView protein in InterPro
IPR001427. RNaseA.
IPR023411. RNaseA_AS.
IPR023412. RNaseA_domain.
PANTHERiPTHR11437. PTHR11437. 1 hit.
PfamiView protein in Pfam
PF00074. RnaseA. 1 hit.
PRINTSiPR00794. RIBONUCLEASE.
ProDomiView protein in ProDom or Entries sharing at least one domain
PD000535. RNaseA. 1 hit.
SMARTiView protein in SMART
SM00092. RNAse_Pc. 1 hit.
SUPFAMiSSF54076. SSF54076. 1 hit.
PROSITEiView protein in PROSITE
PS00127. RNASE_PANCREATIC. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O35291-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGPKLLESRL CLLLLLGLVL MLASCQAQIL SQKFYTQHIY NSTYPRCDAV
60 70 80 90 100
MRVVNRYRPR CKDINTFLHT SFADVVAVCG HPNITCNNLT RKNCHASSFQ
110 120 130 140 150
VFITFCNLTM PTRICTQCRY QTTGSVKYYR VACENRTPQD TPMYPVVPVH

LDGTF
Length:155
Mass (Da):17,723
Last modified:January 1, 1998 - v1
Checksum:i36879AAF1CCFB961
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF017259 Genomic DNA. Translation: AAC53490.1.
RefSeqiNP_001017422.1. NM_001017422.1.
UniGeneiMm.377124.

Genome annotation databases

GeneIDi53877.
KEGGimmu:53877.

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

Entry informationi

Entry nameiRNAS2_MOUSE
AccessioniPrimary (citable) accession number: O35291
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 1, 1998
Last modified: May 10, 2017
This is version 116 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families