P00683 (RNAS1_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 109.
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 |
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| Organism | Mus musculus (Mouse) [Reference proteome] | ||||
| Taxonomic identifier | 10090 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus![]() |
Protein attributes
| Sequence length | 149 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. 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 | |
| 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.3 | |||||||||||||||||||||||||
| Chain | 26 – 149 | 124 | Ribonuclease pancreatic | PRO_0000030929 | ||||||||||||||||||||||||
Regions | ||||||||||||||||||||||||||||
| Region | 66 – 70 | 5 | Substrate binding By similarity | |||||||||||||||||||||||||
Sites | ||||||||||||||||||||||||||||
| Active site | 37 | 1 | Proton acceptor By similarity | |||||||||||||||||||||||||
| Active site | 144 | 1 | Proton donor By similarity | |||||||||||||||||||||||||
| Binding site | 32 | 1 | Substrate By similarity | |||||||||||||||||||||||||
| Binding site | 35 | 1 | Substrate By similarity | |||||||||||||||||||||||||
| Binding site | 91 | 1 | Substrate By similarity | |||||||||||||||||||||||||
Amino acid modifications | ||||||||||||||||||||||||||||
| Disulfide bond | 51 ↔ 109 | By similarity | ||||||||||||||||||||||||||
| Disulfide bond | 65 ↔ 120 | By similarity | ||||||||||||||||||||||||||
| Disulfide bond | 83 ↔ 135 | By similarity | ||||||||||||||||||||||||||
| Disulfide bond | 90 ↔ 97 | By similarity | ||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||
| Helix | 29 – 37 | 9 | ||||||||||||||||||||||||||
| Helix | 50 – 57 | 8 | ||||||||||||||||||||||||||
| Beta strand | 61 – 64 | 4 | ||||||||||||||||||||||||||
| Beta strand | 67 – 72 | 6 | ||||||||||||||||||||||||||
| Helix | 76 – 80 | 5 | ||||||||||||||||||||||||||
| Helix | 81 – 84 | 4 | ||||||||||||||||||||||||||
| Beta strand | 85 – 88 | 4 | ||||||||||||||||||||||||||
| Beta strand | 97 – 99 | 3 | ||||||||||||||||||||||||||
| Beta strand | 104 – 111 | 8 | ||||||||||||||||||||||||||
| Beta strand | 122 – 136 | 15 | ||||||||||||||||||||||||||
| Turn | 137 – 140 | 4 | ||||||||||||||||||||||||||
| Beta strand | 141 – 149 | 9 | ||||||||||||||||||||||||||
Sequences
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References
| [1] | "Evolution of nucleic acids coding for ribonucleases: the mRNA sequence of mouse pancreatic ribonuclease." Schueller C., Nijssen H.M.J., Kok R., Beintema J.J. Mol. Biol. Evol. 7:29-44(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [2] | "Isolation of the murine ribonuclease gene Rib-1: structure and tissue specific expression in pancreas and parotid gland." Samuelson L.C., Wiebauer K., Howard G., Schmid R.M., Koeplin D., Meisler M.H. Nucleic Acids Res. 19:6935-6941(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: C3H/HeJ. Tissue: Spleen. |
| [3] | "The amino acid sequence of mouse pancreatic ribonuclease. Extremely rapid evolutionary rates of the myomorph rodent ribonucleases." Lenstra J.A., Beintema J.J. Eur. J. Biochem. 98:399-408(1979) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 26-149. Tissue: Pancreas. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | M27814 mRNA. Translation: AAA40060.1. X60103 Genomic DNA. Translation: CAA42697.1. | ||||||||||||
| IPI | IPI00133541. | ||||||||||||
| PIR | NRMS. A34090. | ||||||||||||
| UniGene | Mm.235538. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | P00683. | ||||||||||||
| SMR | P00683. Positions 26-149. | ||||||||||||
| ModBase | Search... | ||||||||||||
PTM databases | |||||||||||||
| PhosphoSite | P00683. | ||||||||||||
Proteomic databases | |||||||||||||
| PaxDb | P00683. | ||||||||||||
| PRIDE | P00683. | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Organism-specific databases | |||||||||||||
| MGI | MGI:97919. Rnase1. | ||||||||||||
Phylogenomic databases | |||||||||||||
| eggNOG | NOG40319. | ||||||||||||
| HOGENOM | HOG000276883. | ||||||||||||
| HOVERGEN | HBG008396. | ||||||||||||
| InParanoid | P00683. | ||||||||||||
| OrthoDB | EOG4TMR3F. | ||||||||||||
Gene expression databases | |||||||||||||
| CleanEx | MM_RNASE1. | ||||||||||||
| Genevestigator | P00683. | ||||||||||||
| GermOnline | ENSMUSG00000035896. Mus musculus. | ||||||||||||
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 | |||||||||||||
| ChiTaRS | RNASE1. mouse. | ||||||||||||
| SOURCE | Search... | ||||||||||||
Entry information
| Entry name | RNAS1_MOUSE | ||||||||
| Accession | Primary (citable) accession number: P00683 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
