Skip Header

Contribute Send feedback
Read comments (?) or add your own

P47783 (RNAS2_MACFA) Reviewed, UniProtKB/Swiss-Prot

Last modified July 27, 2011. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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-derived neurotoxin
RNase UpI-2
Ribonuclease 2
Short name=RNase 2
Ribonuclease US
Gene names
Name:RNASE2
Synonyms:EDN, RNS2
OrganismMacaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
Taxonomic identifier9541 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniCercopithecidaeCercopithecinaeMacaca

Protein attributes

Sequence length160 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. Ref.1

Catalytic activity

Endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides ending in Cp or Up with 2',3'-cyclic phosphate intermediates. Ref.1

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.

Biophysicochemical properties

Kinetic parameters:

KM=1.8 µM for yeast tRNA (in the presence of 40 mM sodium phosphate at pH 7.0) Ref.1

Ontologies

Keywords
   Cellular componentLysosome
   DomainSignal
   Molecular functionEndonuclease
Hydrolase
Nuclease
   PTMDisulfide bond
Glycoprotein
Nitration
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: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 By similarity
Chain28 – 160133Non-secretory ribonuclease
PRO_0000030876

Regions

Region65 – 695Substrate binding By similarity

Sites

Active site421Proton acceptor By similarity
Active site1551Proton donor By similarity

Amino acid modifications

Modified residue601Nitrated tyrosine By similarity
Glycosylation341C-linked (Man) By similarity
Glycosylation441N-linked (GlcNAc...) Potential
Glycosylation921N-linked (GlcNAc...) Potential
Glycosylation1111N-linked (GlcNAc...) Potential
Glycosylation1381N-linked (GlcNAc...) Potential
Disulfide bond50 ↔ 110 By similarity
Disulfide bond64 ↔ 122 By similarity
Disulfide bond82 ↔ 137 By similarity
Disulfide bond89 ↔ 98 By similarity

Sequences

Sequence LengthMass (Da)Tools
P47783 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 918F7840BC40C6F3

FASTA16018,000
        10         20         30         40         50         60 
MVPKLFTSQI CLLLLLGLMG VEGSLHAKPG QFTWAQWFEI QHINMTSGQC TNAMQVINNY 

        70         80         90        100        110        120 
QRRCKNQNTF LLTTFADVVH VCGNPSMPCP SNTSLNNCHH SGVQVPLIHC NLTTPSRRIS 

       130        140        150        160 
NCRYTQTTAN KYYIVACNNS DPVRDPPQYP VVPVHLDRII 

« Hide

References

[1]"Rapid evolution of a unique family of primate ribonuclease genes."
Rosenberg H.F., Dyer K.D., Tiffany H.L., Gonzalez M.
Nat. Genet. 10:219-223(1995) [PubMed: 7663519] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U24096 Genomic DNA. Translation: AAC50145.1.
PIRI84444.

3D structure databases

ProteinModelPortalP47783.
SMRP47783. Positions 26-160.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG008396.

Family and domain databases

InterProIPR001427. RNaseA.
IPR023411. RNaseA_AS.
IPR023412. RNaseA_domain.
[Graphical view]
Gene3DG3DSA:3.10.130.10. RNaseA. 1 hit.
PANTHERPTHR11437. RNaseA. 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. RNaseA. 1 hit.
PROSITEPS00127. RNASE_PANCREATIC. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRNAS2_MACFA
AccessionPrimary (citable) accession number: P47783
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: July 27, 2011
This is version 69 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