O35291 (RNAS2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Non-secretory ribonuclease
EC=3.1.27.5

Alternative name(s):
Eosinophil cationic-type ribonuclease 4
MR-4
Ribonuclease 2
Short name=RNase 2

Gene names

Name:	Rnase2
Synonyms:	Ear4

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	155 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	This is a non-secretory ribonuclease. It is a pyrimidine specific nuclease with a slight preference for U. Cytotoxin and helminthotoxin. Possesses a wide variety of biological activities.
Catalytic activity	Endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides ending in Cp or Up with 2',3'-cyclic phosphate intermediates.
Subunit structure	Interacts with and forms a tight 1:1 complex with RNH1. Dimerization of two such complexes may occur By similarity.
Subcellular location	Lysosome Probable. Cytoplasmic granule. Note: Matrix of eosinophil's large specific granule.
Sequence similarities	Belongs to the pancreatic ribonuclease family.

Ontologies

Keywords
Cellular component	Lysosome
Domain	Signal
Molecular function	Endonuclease Hydrolase Nuclease
PTM	Disulfide bond Glycoprotein Nitration
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	nucleic acid phosphodiester bond hydrolysis Inferred from electronic annotation. Source: GOC
Cellular_component	lysosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	nucleic acid binding Inferred from electronic annotation. Source: InterPro pancreatic ribonuclease activity Inferred 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 – 155	130	Non-secretory ribonuclease		PRO_0000030882
Regions
	Region	62 – 66	5	Substrate binding By similarity
Sites
	Active site	38	1	Proton acceptor By similarity
	Active site	150	1	Proton donor By similarity
	Binding site	33	1	Substrate By similarity
Amino acid modifications
	Modified residue	57	1	Nitrated tyrosine By similarity
	Glycosylation	41	1	N-linked (GlcNAc...) Potential
	Glycosylation	83	1	N-linked (GlcNAc...) Potential
	Glycosylation	88	1	N-linked (GlcNAc...) Potential
	Glycosylation	107	1	N-linked (GlcNAc...) Potential
	Disulfide bond	47 ↔ 106		By similarity
	Disulfide bond	61 ↔ 118		By similarity
	Disulfide bond	79 ↔ 133		By similarity
	Disulfide bond	86 ↔ 94		By similarity

Sequences

	Sequence		Length	Mass (Da)
	O35291 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 36879AAF1CCFB961	FASTA	155	17,723
	10 20 30 40 50 60 MGPKLLESRL CLLLLLGLVL MLASCQAQIL SQKFYTQHIY NSTYPRCDAV MRVVNRYRPR 70 80 90 100 110 120 CKDINTFLHT SFADVVAVCG HPNITCNNLT RKNCHASSFQ VFITFCNLTM PTRICTQCRY 130 140 150 QTTGSVKYYR VACENRTPQD TPMYPVVPVH LDGTF

References

[1]

"Molecular cloning of four novel murine ribonuclease genes: unusual expansion within the ribonuclease A gene family." Batten D., Dyer K.D., Domachowske J.B., Rosenberg H.F. Nucleic Acids Res. 25:4235-4239(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Fibroblast.

[2]

"Post-translational tyrosine nitration of eosinophil granule toxins mediated by eosinophil peroxidase." Ulrich M., Petre A., Youhnovski N., Proemm F., Schirle M., Schumm M., Pero R.S., Doyle A., Checkel J., Kita H., Thiyagarajan N., Acharya K.R., Schmid-Grendelmeier P., Simon H.-U., Schwarz H., Tsutsui M., Shimokawa H., Bellon G. , Lee J.J., Przybylski M., Doering G. J. Biol. Chem. 283:28629-28640(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NITRATION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF017259 Genomic DNA. Translation: AAC53490.1.
IPI	IPI00128864.
RefSeq	NP_001017422.1. NM_001017422.1.
UniGene	Mm.377124.
3D structure databases
ProteinModelPortal	O35291.
SMR	O35291. Positions 31-152.
ModBase	Search...
Protein-protein interaction databases
STRING	10090.ENSMUSP00000056293.
PTM databases
PhosphoSite	O35291.
Proteomic databases
PRIDE	O35291.
Protocols and materials databases
DNASU	53877.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	53877.
KEGG	mmu:503847. mmu:53877.
Organism-specific databases
CTD	503847. 53877.
MGI	MGI:1858238. Ear4.
Phylogenomic databases
eggNOG	NOG39501.
HOGENOM	HOG000276882.
HOVERGEN	HBG008396.
InParanoid	O35291.
OrthoDB	EOG4GXFP0.
Gene expression databases
Genevestigator	O35291.
GermOnline	ENSMUSG00000050766. 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
NextBio	310745.
SOURCE	Search...

Entry information

Entry name

RNAS2_MOUSE

Accession

Primary (citable) accession number: O35291

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	January 1, 1998
Last modified:	May 1, 2013
This is version 93 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program