P61822 (RNAS1_MIOTA) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 49.
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: Ribonuclease pancreatic EC=3.1.27.5 Alternative name(s): RNase 1 RNase A | ||||
| Gene names |
| ||||
| Organism | Miopithecus talapoin (Angolan talapoin) (Cercopithecus talapoin) | ||||
| Taxonomic identifier | 36231 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Cercopithecidae › Cercopithecinae › Miopithecus![]() |
Protein attributes
| Sequence length | 152 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Endonuclease that catalyzes the cleavage of RNA on the 3' side of pyrimidine nucleotides. Acts on single stranded and double stranded RNA By similarity. |
| Catalytic activity | Endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides ending in Cp or Up with 2',3'-cyclic phosphate intermediates. |
| Subunit structure | Monomer. Interacts with and forms tight 1:1 complexes with RNH1. Dimerization of two such complexes may occur. Interaction with RNH1 inhibits this protein By similarity. |
| Subcellular location | Secreted By similarity. |
| Sequence similarities | Belongs to the pancreatic ribonuclease family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Secreted |
| Domain | Signal |
| Molecular function | Endonuclease Hydrolase Nuclease |
| PTM | Disulfide bond Glycoprotein |
| Gene Ontology (GO) | |
| Biological_process | nucleic acid phosphodiester bond hydrolysis Inferred from electronic annotation. Source: GOC |
| Cellular_component | extracellular region 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 – 24 | 24 | By similarity | ||||||||
| Chain | 25 – 152 | 128 | Ribonuclease pancreatic | PRO_0000030928 | |||||||
Regions | |||||||||||
| Region | 65 – 69 | 5 | Substrate binding By similarity | ||||||||
Sites | |||||||||||
| Active site | 36 | 1 | Proton acceptor By similarity | ||||||||
| Active site | 143 | 1 | Proton donor By similarity | ||||||||
| Binding site | 31 | 1 | Substrate By similarity | ||||||||
| Binding site | 34 | 1 | Substrate By similarity | ||||||||
| Binding site | 90 | 1 | Substrate By similarity | ||||||||
| Binding site | 109 | 1 | Substrate By similarity | ||||||||
Amino acid modifications | |||||||||||
| Glycosylation | 46 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 112 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 50 ↔ 108 | By similarity | |||||||||
| Disulfide bond | 64 ↔ 119 | By similarity | |||||||||
| Disulfide bond | 82 ↔ 134 | By similarity | |||||||||
| Disulfide bond | 89 ↔ 96 | By similarity | |||||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Adaptive evolution of a duplicated pancreatic ribonuclease gene in a leaf-eating monkey." Zhang J., Zhang Y.-P., Rosenberg H.F. Nat. Genet. 30:411-415(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF449636 Genomic DNA. Translation: AAL87057.1. |
3D structure databases | |
| ProteinModelPortal | P61822. |
| SMR | P61822. Positions 25-151. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Phylogenomic databases | |
| HOVERGEN | HBG008396. |
Family and domain databases | |
| Gene3D | 3.10.130.10. 1 hit. |
| InterPro | IPR001427. RNaseA. IPR023411. RNaseA_AS. IPR023412. RNaseA_domain. [Graphical view] |
| PANTHER | PTHR11437. PTHR11437. 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 | RNAS1_MIOTA | ||||||||
| Accession | Primary (citable) accession number: P61822 Secondary accession number(s): Q8SPF2 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
