P00684 (RNS1B_RAT) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 110.
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 beta-type EC=3.1.27.5 Alternative name(s): RL1 RNase 1 gamma RNase A | ||||
| Gene names |
| ||||
| Organism | Rattus norvegicus (Rat) [Reference proteome] | ||||
| Taxonomic identifier | 10116 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus![]() |
Protein attributes
| Sequence length | 152 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 | 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 By similarity. |
| Subcellular location | |
| Tissue specificity | Pancreas. |
| Sequence similarities | Belongs to the pancreatic ribonuclease family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Secreted |
| Domain | Signal |
| Molecular function | Endonuclease Hydrolase Nuclease |
| PTM | Disulfide bond |
| Technical term | 3D-structure Complete proteome Direct protein sequencing Reference proteome |
| 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 – 25 | 25 | Ref.2 | |||||||||||||||||||||||||||
| Chain | 26 – 152 | 127 | Ribonuclease pancreatic beta-type | PRO_0000030940 | ||||||||||||||||||||||||||
Regions | ||||||||||||||||||||||||||||||
| Region | 69 – 73 | 5 | Substrate binding | |||||||||||||||||||||||||||
Sites | ||||||||||||||||||||||||||||||
| Active site | 40 | 1 | Proton acceptor | |||||||||||||||||||||||||||
| Active site | 147 | 1 | Proton donor | |||||||||||||||||||||||||||
| Binding site | 35 | 1 | Substrate | |||||||||||||||||||||||||||
| Binding site | 38 | 1 | Substrate | |||||||||||||||||||||||||||
| Binding site | 94 | 1 | Substrate | |||||||||||||||||||||||||||
| Binding site | 113 | 1 | Substrate | |||||||||||||||||||||||||||
Amino acid modifications | ||||||||||||||||||||||||||||||
| Disulfide bond | 54 ↔ 112 | |||||||||||||||||||||||||||||
| Disulfide bond | 68 ↔ 123 | |||||||||||||||||||||||||||||
| Disulfide bond | 86 ↔ 138 | |||||||||||||||||||||||||||||
| Disulfide bond | 93 ↔ 100 | |||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||
| Helix | 34 – 40 | 7 | ||||||||||||||||||||||||||||
| Helix | 53 – 60 | 8 | ||||||||||||||||||||||||||||
| Turn | 61 – 64 | 4 | ||||||||||||||||||||||||||||
| Beta strand | 65 – 67 | 3 | ||||||||||||||||||||||||||||
| Beta strand | 70 – 75 | 6 | ||||||||||||||||||||||||||||
| Helix | 79 – 83 | 5 | ||||||||||||||||||||||||||||
| Helix | 84 – 87 | 4 | ||||||||||||||||||||||||||||
| Beta strand | 100 – 102 | 3 | ||||||||||||||||||||||||||||
| Beta strand | 107 – 114 | 8 | ||||||||||||||||||||||||||||
| Beta strand | 125 – 132 | 8 | ||||||||||||||||||||||||||||
| Beta strand | 134 – 139 | 6 | ||||||||||||||||||||||||||||
| Turn | 140 – 143 | 4 | ||||||||||||||||||||||||||||
| Beta strand | 144 – 151 | 8 | ||||||||||||||||||||||||||||
Sequences
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References
| [1] | "Rat pancreatic ribonuclease messenger RNA. The nucleotide sequence of the entire mRNA and the derived amino acid sequence of the pre-enzyme." McDonald R.J., Stary S.J., Swift G.H. J. Biol. Chem. 257:14582-14585(1982) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [2] | "Rat pancreatic ribonuclease. II. Amino acid sequence." Beintema J.J., Gruber M. Biochim. Biophys. Acta 310:161-173(1973) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 26-152. Tissue: Pancreas. |
| [3] | "Rat pancreatic ribonuclease: agreement between the corrected amino acid sequence and the sequence derived from its messenger RNA." Beintema J.J. FEBS Lett. 159:191-195(1983) [PubMed] [Europe PMC] [Abstract] Cited for: SEQUENCE REVISION TO 98; 124; 126; 129 AND 131. Tissue: Pancreas. |
| [4] | "The crystal structure of recombinant rat pancreatic RNase A." Gupta V., Muyldermans S., Wyns L., Salunke D.M. Proteins 35:1-12(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 30-152. Tissue: Pancreas. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | J00771 mRNA. No translation available. | ||||||||||||
| IPI | IPI00211902. | ||||||||||||
| PIR | NRRT. A92356. | ||||||||||||
| UniGene | Rn.9397. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | P00684. | ||||||||||||
| SMR | P00684. Positions 30-152. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| STRING | 10116.ENSRNOP00000043700. | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| UCSC | RGD:3574. rat. | ||||||||||||
Organism-specific databases | |||||||||||||
| RGD | 3574. Rnase1. | ||||||||||||
Phylogenomic databases | |||||||||||||
| eggNOG | NOG40319. | ||||||||||||
| HOGENOM | HOG000276883. | ||||||||||||
| HOVERGEN | HBG008396. | ||||||||||||
| InParanoid | P00684. | ||||||||||||
| OrthoDB | EOG4TMR3F. | ||||||||||||
Gene expression databases | |||||||||||||
| ArrayExpress | P00684. | ||||||||||||
| Genevestigator | P00684. | ||||||||||||
| GermOnline | ENSRNOG00000031577. Rattus norvegicus. | ||||||||||||
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... | ||||||||||||
Other | |||||||||||||
| EvolutionaryTrace | P00684. | ||||||||||||
| NextBio | 13948373. | ||||||||||||
Entry information
| Entry name | RNS1B_RAT | ||||||||
| Accession | Primary (citable) accession number: P00684 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
