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P10153 (RNAS2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 162. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Non-secretory ribonuclease

EC=3.1.27.5
Alternative name(s):
Eosinophil-derived neurotoxin
RNase UpI-2
Ribonuclease 2
Short name=RNase 2
Ribonuclease US
Gene names
Name:RNASE2
Synonyms:EDN, RNS2
OrganismHomo sapiens (Human) [Reference proteome]
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. Ref.9 Ref.17

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. Ref.17 Ref.22

Subcellular location

Lysosome Probable. 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.

Sequence similarities

Belongs to the pancreatic ribonuclease family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Ref.8 Ref.9 Ref.10 Ref.11 Ref.13
Chain28 – 161134Non-secretory ribonuclease
PRO_0000030874

Regions

Region65 – 695Substrate binding

Sites

Active site421Proton acceptor
Active site1561Proton donor

Amino acid modifications

Modified residue601Nitrated tyrosine Ref.19
Glycosylation341C-linked (Man) Ref.14 Ref.16
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 variant1001H → Q.
Corresponds to variant rs8012891 [ dbSNP | Ensembl ].
VAR_059820
Natural variant1561H → N Probably inactive. Ref.5
Corresponds to variant rs146887874 [ dbSNP | Ensembl ].
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 [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 28-82, FUNCTION.
[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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT TRP-34.
[17]"Mutational analysis of the complex of human RNase inhibitor and human eosinophil-derived neurotoxin (RNase 2)."
Teufel D.P., Kao R.Y., Acharya K.R., Shapiro R.
Biochemistry 42:1451-1459(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH RNH1.
[18]"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] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN CHEMOTAXIS.
[19]"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. expand/collapse author list , Lee J.J., Przybylski M., Doering G.
J. Biol. Chem. 283:28629-28640(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NITRATION AT TYR-60.
[20]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS).
[21]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
[22]"Molecular recognition of human eosinophil-derived neurotoxin (RNase 2) by placental ribonuclease inhibitor."
Iyer S., Holloway D.E., Kumar K., Shapiro R., Acharya K.R.
J. Mol. Biol. 347:637-655(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) OF 28-161 IN COMPLEX WITH RNH1, SUBUNIT.
[23]"Crystal structures of eosinophil-derived neurotoxin (EDN) in complex with the inhibitors 5'-ATP, Ap3A, Ap4A, and Ap5A."
Baker M.D., Holloway D.E., Swaminathan G.J., Acharya K.R.
Biochemistry 45:416-426(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (0.98 ANGSTROMS) OF 28-161 IN COMPLEX WITH ADP AND ATP.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS9561.1.
PIRA33922. A35328.
RefSeqNP_002925.1. NM_002934.2.
UniGeneHs.728.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GQVX-ray0.98A28-161[»]
1HI2X-ray1.60A28-161[»]
1HI3X-ray1.80A28-161[»]
1HI4X-ray1.80A28-161[»]
1HI5X-ray1.80A28-161[»]
1K2AX-ray1.00A26-160[»]
2BEXX-ray1.99C/D28-161[»]
2BZZX-ray0.98A28-161[»]
2C01X-ray1.24X28-161[»]
2C02X-ray2.00A28-161[»]
2C05X-ray1.86A28-161[»]
ProteinModelPortalP10153.
SMRP10153. Positions 26-161.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111965. 1 interaction.
STRING9606.ENSP00000303276.

Chemistry

BindingDBP10153.
ChEMBLCHEMBL5120.

PTM databases

PhosphoSiteP10153.
UniCarbKBP10153.

Polymorphism databases

DMDM133168.

Proteomic databases

PaxDbP10153.
PeptideAtlasP10153.
PRIDEP10153.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000304625; ENSP00000303276; ENSG00000169385.
GeneID6036.
KEGGhsa:6036.
UCSCuc001vyl.1. human.

Organism-specific databases

CTD6036.
GeneCardsGC14P021423.
HGNCHGNC:10045. RNASE2.
HPAHPA044983.
MIM131410. gene.
neXtProtNX_P10153.
PharmGKBPA34413.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG39501.
HOGENOMHOG000276882.
HOVERGENHBG008396.
InParanoidP10153.
KOK01168.
OMARDPPQYP.
OrthoDBEOG7KDFCP.
PhylomeDBP10153.
TreeFamTF333393.

Gene expression databases

BgeeP10153.
CleanExHS_RNASE2.
GenevestigatorP10153.

Family and domain databases

Gene3D3.10.130.10. 1 hit.
InterProIPR001427. RNaseA.
IPR023411. RNaseA_AS.
IPR023412. RNaseA_domain.
[Graphical view]
PANTHERPTHR11437. PTHR11437. 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]
SUPFAMSSF54076. SSF54076. 1 hit.
PROSITEPS00127. RNASE_PANCREATIC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP10153.
GeneWikiEosinophil-derived_neurotoxin.
GenomeRNAi6036.
NextBio23525.
PROP10153.
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: July 9, 2014
This is version 162 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 14

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