Non-secretory ribonuclease precursor

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Reviewed, UniProtKB/Swiss-Prot P10153 (RNAS2_HUMAN)

Last modified November 25, 2008. Version 110. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

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Protein attributes

Sequence length	161 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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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. Selectively chemotactic for dendritic cells. 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	LysosomeProbable. Cytoplasmic granule. Note= Matrix of eosinophil's large specific granule.
Tissue specificity	Liver, lung, spleen, leukocytes and body fluids.
Domain	The N-terminal region is necessary for mediating chemotactic activity.
Post-translational modification	A particular signal processing and glycosylation pattern may differentiate the UpI2 RNase, found specifically in pregnant women urine, from other nonsecretory RNases.
Involvement in disease	EDN induces ataxia and paralysis, the neurotoxic effect known as the Gordon phenomenon.
Sequence similarities	Belongs to the pancreatic ribonuclease family.

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Ontologies

Keywords
Biological process	Chemotaxis
Cellular component	Lysosome
Coding sequence diversity	Polymorphism
Domain	Signal
Molecular function	Endonuclease Hydrolase Nuclease
PTM	Glycoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	RNA catabolic process Ref.3 Traceable author statement. Source: ProtInc chemotaxis Ref.17 Inferred from direct assay. Source: UniProtKB
Cellular component	extracellular region Ref.3 Traceable author statement. Source: ProtInc lysosome Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	nucleic acid binding Inferred from electronic annotation. Source: InterPro pancreatic ribonuclease activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 27

Chain

28 – 161

134

Non-secretory ribonuclease

PRO_0000030874

Regions

Region

65 – 69

Substrate binding

Sites

Active site

Proton acceptor

Active site

156

Proton donor

Amino acid modifications

Glycosylation

C-linked (Man)

CAR_000004

Glycosylation

N-linked (GlcNAc...)

Glycosylation

N-linked (GlcNAc...)

Glycosylation

N-linked (GlcNAc...)

Glycosylation

111

N-linked (GlcNAc...)

Glycosylation

119

N-linked (GlcNAc...)

Disulfide bond

Disulfide bond

Disulfide bond

Disulfide bond

Natural variations

Natural variant

156

H → N Probably inactive.

VAR_013150

Experimental info

Sequence conflict

W → R AA sequence Ref.10

Sequence conflict

39 – 40

ET → QE AA sequence Ref.10

Sequence conflict

T → V AA sequence Ref.10

Sequence conflict

S → T AA sequence Ref.11

Secondary structure

161

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P10153-1 [UniParc].

Last modified January 1, 1990. Version 2.
Checksum: 9406C4596CA69038
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FASTA

161

18,354

        10         20         30         40         50         60 
MVPKLFTSQI CLLLLLGLLA VEGSLHVKPP QFTWAQWFET QHINMTSQQC TNAMQVINNY 

        70         80         90        100        110        120 
QRRCKNQNTF LLTTFANVVN VCGNPNMTCP SNKTRKNCHH SGSQVPLIHC NLTTPSPQNI 

       130        140        150        160 
SNCRYAQTPA NMFYIVACDN RDQRRDPPQY PVVPVHLDRI I

« Hide

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence of human eosinophil-derived neurotoxin cDNA: identity of deduced amino acid sequence with human nonsecretory ribonucleases." Hamann K.J., Barker R.L., Loegering D.A., Pease L.R., Gleich G.J. Gene 83:161-167(1989) [PubMed: 2591744] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Eosinophil cationic protein cDNA. Comparison with other toxic cationic proteins and ribonucleases." Barker R.L., Loegering D.A., Ten R.M., Hamann K.J., Pease L.R., Gleich G.J. J. Immunol. 143:952-955(1989) [PubMed: 2745977] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Molecular cloning of the human eosinophil-derived neurotoxin: a member of the ribonuclease gene family." Rosenberg H.F., Tenen D.G., Ackerman S.J. Proc. Natl. Acad. Sci. U.S.A. 86:4460-4464(1989) [PubMed: 2734298] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"Structure and chromosome localization of the human eosinophil-derived neurotoxin and eosinophil cationic protein genes: evidence for intronless coding sequences in the ribonuclease gene superfamily." Hamann K.J., Ten R.M., Loegering D.A., Jenkins R.B., Heise M.T., Schad C.R., Pease L.R., Gleich G.J., Barker R.L. Genomics 7:535-546(1990) [PubMed: 2387583] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"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 ASN-156.
[6]	Simonsen C.C., Kennedy J., Comstock L., Ashton N., McGrogan M. Submitted (OCT-1990) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. Tissue: Colon and Leukemia.
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[8]	"Amino acid sequence of the nonsecretory ribonuclease of human urine." Beintema J.J., Hofsteenge J., Iwama M., Morita T., Ohgi K., Irie M., Sugiyama R.H., Schieven G.L., Dekker C.A., Glitz D.G. Biochemistry 27:4530-4538(1988) [PubMed: 3166997] [Abstract] Cited for: PROTEIN SEQUENCE OF 28-161.
[9]	"Biochemical and functional similarities between human eosinophil-derived neurotoxin and eosinophil cationic protein: homology with ribonuclease." Gleich G.J., Loegering D.A., Bell M.P., Checkel J.L., Ackerman S.J., McKean D.J. Proc. Natl. Acad. Sci. U.S.A. 83:3146-3150(1986) [PubMed: 3458170] [Abstract] Cited for: PROTEIN SEQUENCE OF 28-82.
[10]	"Purification and properties of bovine kidney ribonucleases." Niwata Y., Ohgi K., Sanda A., Takizawa Y., Irie M. J. Biochem. 97:923-934(1985) [PubMed: 3926759] [Abstract] Cited for: PROTEIN SEQUENCE OF 28-55.
[11]	"Purification and characterization of a ribonuclease from human liver." Sorrentino S., Tucker G.K., Glitz D.G. J. Biol. Chem. 263:16125-16131(1988) [PubMed: 3182786] [Abstract] Cited for: PROTEIN SEQUENCE OF 28-53. Tissue: Liver.
[12]	"Characterization of a unique nonsecretory ribonuclease from urine of pregnant women." Sakakibara R., Hashida K., Kitahara T., Ishiguro M. J. Biochem. 111:325-330(1992) [PubMed: 1587793] [Abstract] Cited for: PROTEIN SEQUENCE OF 24-43. Tissue: Urine.
[13]	"Characterisation of UGP and its relationship with beta-core fragment." Kardana A., Bagshawe K.D., Coles B., Read D., Taylor M. Br. J. Cancer 67:686-692(1993) [PubMed: 8471426] [Abstract] Cited for: PROTEIN SEQUENCE OF 28-45. Tissue: Urine.
[14]	"New type of linkage between a carbohydrate and a protein: C-glycosylation of a specific tryptophan residue in human RNase Us." Hofsteenge J., Mueller D.R., de Beer T., Loeffler A., Richter W.J., Vliegenthart J.F.G. Biochemistry 33:13524-13530(1994) [PubMed: 7947762] [Abstract] Cited for: GLYCOSYLATION AT TRP-34.
[15]	"The hexopyranosyl residue that is C-glycosidically linked to the side chain of tryptophan-7 in human RNase Us is alpha-mannopyranose." de Beer T., Vliegenthart J.F.G., Loeffler A., Hofsteenge J. Biochemistry 34:11785-11789(1995) [PubMed: 7547911] [Abstract] Cited for: STRUCTURE OF C-GLYCOSYLATED GROUP.
[16]	"Recognition signal for C-mannosylation of Trp-7 in RNase 2 consists of sequence Trp-x-x-Trp." Krieg J., Hartmann S., Vicentini A., Glasner W., Hess D., Hofsteenge J. Mol. Biol. Cell 9:301-309(1998) [PubMed: 9450956] [Abstract] Cited for: GLYCOSYLATION AT TRP-34.
[17]	"Eosinophil-derived neurotoxin (EDN), an antimicrobial protein with chemotactic activities for dendritic cells." Yang D., Rosenberg H.F., Chen Q., Dyer K.D., Kurosaka K., Oppenheim J.J. Blood 102:3396-3403(2003) [PubMed: 12855582] [Abstract] Cited for: INVOLVEMENT IN CHEMOTAXIS.
[18]	"X-ray crystallographic structure of recombinant eosinophil-derived neurotoxin at 1.83-A resolution." Mosimann S.C., Newton D.L., Youle R.J., James M.N.G. J. Mol. Biol. 260:540-552(1996) [PubMed: 8759319] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS).
[19]	"Mapping the ribonucleolytic active site of eosinophil-derived neurotoxin (EDN). High resolution crystal structures of EDN complexes with adenylic nucleotide inhibitors." Leonidas D.D., Boix E., Prill R., Suzuki M., Turton R., Minson K., Swaminathan G.J., Youle R.J., Acharya K.R. J. Biol. Chem. 276:15009-15017(2001) [PubMed: 11154698] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
+	Additional computationally mapped references.

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Cross-references

Sequence databases

M30510 mRNA. Translation: AAC82505.1.
M28129 mRNA. Translation: AAA50284.1.
M24157 mRNA. Translation: AAA52337.1.
X16546 Genomic DNA. Translation: CAA34546.1.
AF294007 Genomic DNA. Translation: AAG31577.1.
AF294008 Genomic DNA. Translation: AAG31578.1.
AF294009 Genomic DNA. Translation: AAG31579.1.
AF294010 Genomic DNA. Translation: AAG31580.1.
AF294011 Genomic DNA. Translation: AAG31581.1.
AF294012 Genomic DNA. Translation: AAG31582.1.
AF294013 Genomic DNA. Translation: AAG31583.1.
AF294014 Genomic DNA. Translation: AAG31584.1.
AF294015 Genomic DNA. Translation: AAG31585.1.
X55987 Genomic DNA. Translation: CAA39459.1.
X55988 mRNA. Translation: CAA39460.1.
BC093678 mRNA. Translation: AAH93678.1.
BC093680 mRNA. Translation: AAH93680.1.
BC096059 mRNA. Translation: AAH96059.1.

PIR

A33922. A35328.

RefSeq

NP_002925.1.

UniGene

Hs.728

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GQV	X-ray	0.98	A	28-161	[»]
1HI2	X-ray	1.60	A	28-161	[»]
1HI3	X-ray	1.80	A	28-161	[»]
1HI4	X-ray	1.80	A	28-161	[»]
1HI5	X-ray	1.80	A	28-161	[»]
1K2A	X-ray	1.00	A	26-161	[»]
2BEX	X-ray	1.99	C/D	28-161	[»]
2BZZ	X-ray	0.98	A	28-161	[»]
2C01	X-ray	1.24	X	28-161	[»]
2C02	X-ray	2.00	A	28-161	[»]
2C05	X-ray	1.86	A	28-161	[»]

ModBase

Search...

PTM databases

GlycoSuiteDB

P10153.

Proteomic databases

PeptideAtlas

P10153.

Genome annotation databases

Ensembl

ENSG00000169385. Homo sapiens. [Contig view]

GeneID

6036.

KEGG

hsa:6036.

Organism-specific databases

H-InvDB

HIX0037783.

HGNC

HGNC:10045. RNASE2.

MIM

131410. gene.

PharmGKB

PA34413.

GenAtlas

Search...

GeneCards

Search...

Phylogenomic databases

HOGENOM

P10153.

HOVERGEN

P10153.

Gene expression databases

ArrayExpress

P10153.

CleanEx

HS_RNASE2.

GermOnline

ENSG00000169385. Homo sapiens.

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...

Other Resources

LinkHub

P10153.

NextBio

23525.

SOURCE

Search...

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Entry information

Entry name

RNAS2_HUMAN

Accession

Primary (citable) accession number: P10153
Secondary accession number(s): Q52M39, Q9H2B7, Q9UCG7

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	January 1, 1990
Last modified:	November 25, 2008
This is version 110 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Keywords

Gene Ontology (GO)

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents