P47783 (RNAS2_MACFA) Reviewed, UniProtKB/Swiss-Prot
Last modified
July 27, 2011.
Version 69.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended 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 |
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| Organism | Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey) | ||||
| Taxonomic identifier | 9541 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Cercopithecidae › Cercopithecinae › Macaca |
Protein attributes
| Sequence length | 160 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence 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 component | Lysosome |
| Domain | Signal |
| Molecular function | Endonuclease Hydrolase Nuclease |
| PTM | Disulfide bond Glycoprotein Nitration |
| Gene Ontology (GO) | |
| Cellular component | lysosome Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | nucleic acid binding Inferred from electronic annotation. Source: InterPro pancreatic ribonuclease activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 27 | 27 | By similarity | ||||||||
| Chain | 28 – 160 | 133 | Non-secretory ribonuclease | PRO_0000030876 | |||||||
Regions | |||||||||||
| Region | 65 – 69 | 5 | Substrate binding By similarity | ||||||||
Sites | |||||||||||
| Active site | 42 | 1 | Proton acceptor By similarity | ||||||||
| Active site | 155 | 1 | Proton donor By similarity | ||||||||
Amino acid modifications | |||||||||||
| Modified residue | 60 | 1 | Nitrated tyrosine By similarity | ||||||||
| Glycosylation | 34 | 1 | C-linked (Man) By similarity | ||||||||
| Glycosylation | 44 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 92 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 111 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 138 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 50 ↔ 110 | By similarity | |||||||||
| Disulfide bond | 64 ↔ 122 | By similarity | |||||||||
| Disulfide bond | 82 ↔ 137 | By similarity | |||||||||
| Disulfide bond | 89 ↔ 98 | By similarity | |||||||||
Sequences
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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. |
| PIR | I84444. |
3D structure databases | |
| ProteinModelPortal | P47783. |
| SMR | P47783. Positions 26-160. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Phylogenomic databases | |
| HOVERGEN | HBG008396. |
Family and domain databases | |
| InterPro | IPR001427. RNaseA. IPR023411. RNaseA_AS. IPR023412. RNaseA_domain. [Graphical view] |
| Gene3D | G3DSA:3.10.130.10. RNaseA. 1 hit. |
| PANTHER | PTHR11437. RNaseA. 1 hit. |
| Pfam | PF00074. RnaseA. 1 hit. [Graphical view] |
| PRINTS | PR00794. RIBONUCLEASE. |
| ProDom | PD000535. RNaseA. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| SMART | SM00092. RNAse_Pc. 1 hit. [Graphical view] |
| SUPFAM | SSF54076. RNaseA. 1 hit. |
| PROSITE | PS00127. RNASE_PANCREATIC. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | RNAS2_MACFA | ||||||||
| Accession | Primary (citable) accession number: P47783 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

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