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non-secretory ribonuclease; ribonuclease US; eosinophil-derived neurotoxin; Rnase UpI-2; ribonuclease 2; Rnase 2 (RNASE2, EDN, RNS2)

Function: - non-secretory ribonuclease - pyrimidine specific nuclease with a slight preference for U. cytotoxin & helminthotoxin - selectively chemotactic for dendritic cells - possesses a wide variety of biological activities - a particular signal processing & glycosylation pattern may differentiate the UpI2 Rnase, found specifically in pregnant women urine, from other nonsecretory Rnases - endonucleolytic cleavage to nucleoside 3'-phosphates & 3'-phosphooligonucleotides ending in Cp or Up with 2',3'-cyclic phosphate intermediates Structure: - N-terminal region is necessary for mediating chemotactic activity - belongs to the pancreatic ribonuclease family Compartment: - lysosome (probable) - cytoplasmic granule - matrix of eosinophil's large specific granule Expression: liver, lung, spleen, leukocytes & body fluids Pathology: - EDN induces ataxia & paralysis, the neurotoxic effect known as the Gordon phenomenon

General

endoribonuclease glycoprotein

Properties

SIZE: entity length = 161 aa MW = 18 kD COMPARTMENT: lysosome cytoplasm MOTIF: signal sequence {1-27} histidine residue {H42} N-glycosylation site {N44} cysteine residue {C50} MODIFICATION: cysteine residue {C110} cysteine residue {C64} MODIFICATION: cysteine residue {C123} Substrate binding {65-69} cysteine residue {C82} MODIFICATION: cysteine residue {C138} N-glycosylation site {N86} cysteine residue {C89} MODIFICATION: cysteine residue {C98} N-glycosylation site {N92} cysteine residue {C98} MODIFICATION: cysteine residue {C89} cysteine residue {C110} MODIFICATION: cysteine residue {C50} N-glycosylation site {N111} N-glycosylation site {N119} cysteine residue {C123} MODIFICATION: cysteine residue {C64} cysteine residue {C138} MODIFICATION: cysteine residue {C82} histidine residue {H156}

Database Correlations

OMIM 131410 UniProt P10153 Pfam PF00074 Entrez Gene 6036 Kegg hsa:6036 ENZYME 3.1.27.5

References

UniProt :accession P10153