Q9QYX2 (RNAS1_MUSSA) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 31, 2011.
Version 59.
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 | Mus saxicola (Brown spiny mouse) (Rock-loving mouse) | ||
| Taxonomic identifier | 10094 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Pyromys |
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 transcript 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 Glycoprotein |
| 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 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 25 | 25 | Potential | ||||||||
| Chain | 26 – 149 | 124 | Ribonuclease pancreatic | PRO_0000030931 | |||||||
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 | |||||||||||
| Glycosylation | 87 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 51 ↔ 109 | By similarity | |||||||||
| Disulfide bond | 65 ↔ 120 | By similarity | |||||||||
| Disulfide bond | 83 ↔ 135 | By similarity | |||||||||
| Disulfide bond | 90 ↔ 97 | By similarity | |||||||||
Sequences
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References
| [1] | "The phylogenetic position of 'Acomyinae' (Rodentia, Mammalia) as sister group of a Murinae + Gerbillinae clade: evidence from the nuclear ribonuclease gene." Dubois J.-Y.F., Catzeflis F.M., Beintema J.J. Mol. Phylogenet. Evol. 13:181-192(1999) [PubMed: 10508551] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AJ238700 Genomic DNA. Translation: CAB60003.1. |
3D structure databases | |
| ProteinModelPortal | Q9QYX2. |
| SMR | Q9QYX2. Positions 27-149. |
| 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 | RNAS1_MUSSA | ||||||||
| Accession | Primary (citable) accession number: Q9QYX2 | ||||||||
| 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 |

Clusters with