Reviewed,
UniProtKB/Swiss-Prot P00660 (RNAS1_CONTA)
Last modified
June 16, 2009.
Version 59.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Ribonuclease pancreatic EC=3.1.27.5 Alternative name(s): RNase 1 RNase A | ||||
| Gene names |
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| Organism | Connochaetes taurinus (Brindled gnu) | ||||
| Taxonomic identifier | 9927 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Alcelaphinae › Connochaetes |
Protein attributes
| Sequence length | 124 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| 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 |
| Molecular function | Endonuclease Hydrolase Nuclease |
| PTM | Disulfide bond |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| 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 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 124 | 124 | Ribonuclease pancreatic | PRO_0000057193 | |||||||
Regions | |||||||||||
| Region | 41 – 45 | 5 | Substrate binding | ||||||||
Sites | |||||||||||
| Active site | 12 | 1 | Proton acceptor | ||||||||
| Active site | 119 | 1 | Proton donor | ||||||||
| Binding site | 7 | 1 | Substrate | ||||||||
| Binding site | 10 | 1 | Substrate | ||||||||
| Binding site | 66 | 1 | Substrate | ||||||||
| Binding site | 85 | 1 | Substrate | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 26 ↔ 84 | ||||||||||
| Disulfide bond | 40 ↔ 95 | ||||||||||
| Disulfide bond | 58 ↔ 110 | ||||||||||
| Disulfide bond | 65 ↔ 72 | ||||||||||
Sequences
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References
| [1] | "The amino acid sequence of gnu pancreatic ribonuclease." Groen G., Welling G.W., Beintema J.J. FEBS Lett. 60:300-304(1975) [PubMed: 1227969] [Abstract] Cited for: PROTEIN SEQUENCE. Tissue: Pancreas. |
Cross-references
Sequence databases | |
|---|---|
| PIR | NRGN. A00808. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1SRN based on UniProtKB P00656. |
| SMR | P00660. Positions 1-124. |
| ModBase | Search... |
Phylogenomic databases | |
| HOVERGEN | P00660. |
Enzyme and pathway databases | |
| BRENDA | 3.1.27.5. 293933. |
Family and domain databases | |
| InterPro | IPR001427. RNaseA. [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] |
| PROSITE | PS00127. RNASE_PANCREATIC. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | RNAS1_CONTA | ||||||||
| Accession | Primary (citable) accession number: P00660 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||

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