Reviewed, UniProtKB/Swiss-Prot O18937 (RNAS2_AOTTR)

Names and origin

Protein names

Recommended name:
    Non-secretory ribonuclease
    EC=3.1.27.5
Alternative name(s):
    Ribonuclease US
    Eosinophil-derived neurotoxin
    RNase UpI-2
    Ribonuclease 2
      Short name=RNase 2

Gene names

Name:	RNASE2
Synonyms:	EDN, RNS2

Organism

Aotus trivirgatus (Night monkey) (Douroucouli)

Taxonomic identifier

9505 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Platyrrhini › Aotidae › Aotus

Protein attributes

Sequence length	158 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology.

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.
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
Gene Ontology (GO)
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 – 27	27	Potential
	Chain	28 – 158	131	Non-secretory ribonuclease		PRO_0000030871
Regions
	Region	65 – 69	5	Substrate binding By similarity
Sites
	Active site	42	1	Proton acceptor By similarity
	Active site	153	1	Proton donor By similarity
Amino acid modifications
	Modified residue	60	1	Nitrated tyrosine By similarity
	Glycosylation	86	1	N-linked (GlcNAc...) Potential
	Glycosylation	92	1	N-linked (GlcNAc...) Potential
	Glycosylation	111	1	N-linked (GlcNAc...) Potential
	Disulfide bond	50 ↔ 110		By similarity
	Disulfide bond	64 ↔ 121		By similarity
	Disulfide bond	82 ↔ 136		By similarity
	Disulfide bond	89 ↔ 98		By similarity

Sequences

	Sequence		Length	Mass (Da)
	O18937-1 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 1E236B62069FE2F9	FASTA	158	17,714
	10 20 30 40 50 60 MVPKLFTSQI CLLLLLGLLG VEGSLHAAPQ KFTRAQWFSI QHIQTTPLRC TNAMRAINKY 70 80 90 100 110 120 QHRCKNQNTF LHTTFAAVVN VCGNTNITCP RNASLNNCHH SRVQVPLTYC NLTGPPTITN 130 140 150 CVYSSTQANM FYVVACDNRD QRDPPQYPVV PVHLDTTI

References

[1]	"Diversity among the primate eosinophil-derived neurotoxin genes: a specific C-terminal sequence is necessary for enhanced ribonuclease activity." Rosenberg H.F., Dyer K.D. Nucleic Acids Res. 25:3532-3536(1997) [PubMed: 9254715] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	U88827 Genomic DNA. Translation: AAB71338.1.
3D structure databases
HSSP	HSSP built from PDB template 1GQV based on UniProtKB P10153.
ModBase	Search...
Phylogenomic databases
HOVERGEN	O18937.
Enzyme and pathway databases
BRENDA	3.1.27.5. 270323.
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

RNAS2_AOTTR

Accession

Primary (citable) accession number: O18937

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	January 1, 1998
Last modified:	October 13, 2009
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)