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Reviewed, UniProtKB/Swiss-Prot P10153 (RNAS2_HUMAN)

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

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length161 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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. 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.

Ontologies

Keywords

   Biological processChemotaxis
   Cellular componentLysosome
   Coding sequence diversityPolymorphism
   DomainSignal
   Molecular functionEndonuclease
Hydrolase
Nuclease
   PTMGlycoprotein
   Technical term3D-structure
Direct protein sequencing

Gene Ontology (GO)

   Biological processRNA catabolic process Ref.3

Traceable author statement. Source: ProtInc

chemotaxis Ref.17

Inferred from direct assay. Source: UniProtKB

   Cellular componentextracellular region Ref.3

Traceable author statement. Source: ProtInc

lysosome

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionnucleic acid binding

Inferred from electronic annotation. Source: InterPro

pancreatic ribonuclease activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727
Chain28 – 161134Non-secretory ribonuclease
PRO_0000030874

Regions

Region65 – 695Substrate binding

Sites

Active site421Proton acceptor
Active site1561Proton donor

Amino acid modifications

Glycosylation341C-linked (Man)
CAR_000004
Glycosylation441N-linked (GlcNAc...)
Glycosylation861N-linked (GlcNAc...)
Glycosylation921N-linked (GlcNAc...)
Glycosylation1111N-linked (GlcNAc...)
Glycosylation1191N-linked (GlcNAc...)
Disulfide bond50 ↔ 110
Disulfide bond64 ↔ 123
Disulfide bond82 ↔ 138
Disulfide bond89 ↔ 98

Natural variations

Natural variant1561H → N Probably inactive.
VAR_013150

Experimental info

Sequence conflict371W → R AA sequence Ref.10
Sequence conflict39 – 402ET → QE AA sequence Ref.10
Sequence conflict461T → V AA sequence Ref.10
Sequence conflict471S → T AA sequence Ref.11

Secondary structure

..................... 161
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P10153-1 [UniParc].

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

FASTA16118,354
        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

References

« Hide '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.

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.
PIRA33922. A35328.
RefSeqNP_002925.1.
UniGeneHs.728

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1GQVX-ray0.98A28-161[»]
1HI2X-ray1.60A28-161[»]
1HI3X-ray1.80A28-161[»]
1HI4X-ray1.80A28-161[»]
1HI5X-ray1.80A28-161[»]
1K2AX-ray1.00A26-161[»]
2BEXX-ray1.99C/D28-161[»]
2BZZX-ray0.98A28-161[»]
2C01X-ray1.24X28-161[»]
2C02X-ray2.00A28-161[»]
2C05X-ray1.86A28-161[»]
ModBaseSearch...

PTM databases

GlycoSuiteDBP10153.

Proteomic databases

PeptideAtlasP10153.

Genome annotation databases

EnsemblENSG00000169385. Homo sapiens. [Contig view]
GeneID6036.
KEGGhsa:6036.

Organism-specific databases

H-InvDBHIX0037783.
HGNCHGNC:10045. RNASE2.
MIM131410. gene.
PharmGKBPA34413.
GenAtlasSearch...
GeneCardsSearch...

Phylogenomic databases

HOGENOMP10153.
HOVERGENP10153.

Gene expression databases

ArrayExpressP10153.
CleanExHS_RNASE2.
GermOnlineENSG00000169385. Homo sapiens.

Family and domain databases

InterProIPR001427. RNaseA.
[Graphical view]
Gene3DG3DSA:3.10.130.10. RNaseA. 1 hit.
PANTHERPTHR11437. RNaseA. 1 hit.
PfamPF00074. RnaseA. 1 hit.
[Graphical view]
PRINTSPR00794. RIBONUCLEASE.
ProDomPD000535. RNaseA. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00092. RNAse_Pc. 1 hit.
[Graphical view]
PROSITEPS00127. RNASE_PANCREATIC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

LinkHubP10153.
NextBio23525.
SOURCESearch...

Entry information

Entry nameRNAS2_HUMAN
AccessionPrimary (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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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 · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents