Reviewed, UniProtKB/Swiss-Prot P47785 (RNAS2_PANTR)

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

Pan troglodytes (Chimpanzee)

Taxonomic identifier

9598 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pan

Protein attributes

Sequence length	161 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 By similarity.
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 By similarity. Note: Matrix of eosinophil's large specific granule By similarity.
Sequence similarities	Belongs to the pancreatic ribonuclease family.

Ontologies

Keywords
Cellular component	Lysosome
Coding sequence diversity	Polymorphism
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	By similarity
	Chain	28 – 161	134	Non-secretory ribonuclease		PRO_0000030878
Regions
	Region	65 – 69	5	Substrate binding By similarity
Sites
	Active site	42	1	Proton acceptor By similarity
	Active site	156	1	Proton donor By similarity
Amino acid modifications
	Modified residue	60	1	Nitrated tyrosine By similarity
	Glycosylation	34	1	C-linked (Man) By similarity
	Glycosylation	44	1	N-linked (GlcNAc...) Potential
	Glycosylation	86	1	N-linked (GlcNAc...) Potential
	Glycosylation	92	1	N-linked (GlcNAc...) Potential
	Glycosylation	111	1	N-linked (GlcNAc...) Potential
	Glycosylation	119	1	N-linked (GlcNAc...) Potential
	Disulfide bond	50 ↔ 110		By similarity
	Disulfide bond	64 ↔ 123		By similarity
	Disulfide bond	82 ↔ 138		By similarity
	Disulfide bond	89 ↔ 98		By similarity
Natural variations
	Natural variant	95	1	R → C in haplotype 3. Ref.2		VAR_021254

Sequences

	Sequence		Length	Mass (Da)
	P47785-1 [UniParc]. Last modified February 1, 1996. Version 1. Checksum: 8321F4596CBF8938	FASTA	161	18,345
	10 20 30 40 50 60 MVPKLFTSQI CLLLLLGLLA VEGSLHVKPP QFTWAQWFET QHINMTSQQC TNAMQVINNY 70 80 90 100 110 120 QRRCKNQNTF LLTTFANVVN VCGNPNMTCP SNKTRKNCHQ SGSQVPLIHC NLTTPSPQNI 130 140 150 160 SNCRYAQTPA NMFYIVACDN RDQRRDPPQY PVVPVHLDRI I

References

[1]	"Rapid evolution of a unique family of primate ribonuclease genes." Rosenberg H.F., Dyer K.D., Tiffany H.L., Gonzalez M. Nat. Genet. 10:219-223(1995) [PubMed: 7663519] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Sequence variation at two eosinophil-associated ribonuclease loci in humans." Zhang J., Rosenberg H.F. Genetics 156:1949-1958(2000) [PubMed: 11102386] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT CYS-95.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U24102 Genomic DNA. Translation: AAC50149.1. AF294016 Genomic DNA. Translation: AAG31586.1. AF294017 Genomic DNA. Translation: AAG31587.1. AF294018 Genomic DNA. Translation: AAG31588.1.
PIR	I61898.
RefSeq	NP_001009133.1.
3D structure databases
SMR	P47785. Positions 26-161.
ModBase	Search...
Protein-protein interaction databases
STRING	P47785.
Genome annotation databases
Ensembl	ENSPTRT00000059611; ENSPTRP00000052810; ENSPTRG00000006106; Pan troglodytes. [Genome view] ENSPTRT00000066116; ENSPTRP00000057691; ENSPTRG00000006106; Pan troglodytes. [Genome view]
GeneID	473325.
KEGG	ptr:473325.
Organism-specific databases
CTD	473325.
Phylogenomic databases
eggNOG	prNOG20780.
HOVERGEN	P47785.
InParanoid	P47785.
OMA	FTWAQWF.
Enzyme and pathway databases
BRENDA	3.1.27.5. 264977.
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_PANTR

Accession

Primary (citable) accession number: P47785
Secondary accession number(s): P60017, Q9GK98

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	January 19, 2010
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)