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Non-secretory ribonuclease (EC 3.1.27.5) (Eosinophil-derived neurotoxin) (RNase UpI-2) (Ribonuclease 2) (RNase 2) (Ribonuclease US)

 RNAS2_HUMAN             Reviewed;         161 AA.
P10153; Q52M39; Q9H2B7; Q9UCG7;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-JAN-1990, sequence version 2.
12-SEP-2018, entry version 196.
RecName: Full=Non-secretory ribonuclease;
EC=3.1.27.5;
AltName: Full=Eosinophil-derived neurotoxin;
AltName: Full=RNase UpI-2;
AltName: Full=Ribonuclease 2;
Short=RNase 2;
AltName: Full=Ribonuclease US;
Flags: Precursor;
Name=RNASE2; Synonyms=EDN, RNS2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2591744; DOI=10.1016/0378-1119(89)90414-9;
Hamann K.J., Barker R.L., Loegering D.A., Pease L.R., Gleich G.J.;
"Sequence of human eosinophil-derived neurotoxin cDNA: identity of
deduced amino acid sequence with human nonsecretory ribonucleases.";
Gene 83:161-167(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2745977;
Barker R.L., Loegering D.A., Ten R.M., Hamann K.J., Pease L.R.,
Gleich G.J.;
"Eosinophil cationic protein cDNA. Comparison with other toxic
cationic proteins and ribonucleases.";
J. Immunol. 143:952-955(1989).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2734298; DOI=10.1073/pnas.86.12.4460;
Rosenberg H.F., Tenen D.G., Ackerman S.J.;
"Molecular cloning of the human eosinophil-derived neurotoxin: a
member of the ribonuclease gene family.";
Proc. Natl. Acad. Sci. U.S.A. 86:4460-4464(1989).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2387583; DOI=10.1016/0888-7543(90)90197-3;
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.;
"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.";
Genomics 7:535-546(1990).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ASN-156.
PubMed=11102386;
Zhang J., Rosenberg H.F.;
"Sequence variation at two eosinophil-associated ribonuclease loci in
humans.";
Genetics 156:1949-1958(2000).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
TISSUE=Colon, and Leukemia;
Simonsen C.C., Kennedy J., Comstock L., Ashton N., McGrogan M.;
Submitted (OCT-1990) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
PROTEIN SEQUENCE OF 28-161.
PubMed=3166997; DOI=10.1021/bi00412a046;
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.;
"Amino acid sequence of the nonsecretory ribonuclease of human
urine.";
Biochemistry 27:4530-4538(1988).
[9]
PROTEIN SEQUENCE OF 28-82, AND FUNCTION.
PubMed=3458170; DOI=10.1073/pnas.83.10.3146;
Gleich G.J., Loegering D.A., Bell M.P., Checkel J.L., Ackerman S.J.,
McKean D.J.;
"Biochemical and functional similarities between human eosinophil-
derived neurotoxin and eosinophil cationic protein: homology with
ribonuclease.";
Proc. Natl. Acad. Sci. U.S.A. 83:3146-3150(1986).
[10]
PROTEIN SEQUENCE OF 28-55.
PubMed=3926759;
Niwata Y., Ohgi K., Sanda A., Takizawa Y., Irie M.;
"Purification and properties of bovine kidney ribonucleases.";
J. Biochem. 97:923-934(1985).
[11]
PROTEIN SEQUENCE OF 28-53.
TISSUE=Liver;
PubMed=3182786;
Sorrentino S., Tucker G.K., Glitz D.G.;
"Purification and characterization of a ribonuclease from human
liver.";
J. Biol. Chem. 263:16125-16131(1988).
[12]
PARTIAL PROTEIN SEQUENCE.
TISSUE=Urine;
PubMed=1587793;
Sakakibara R., Hashida K., Kitahara T., Ishiguro M.;
"Characterization of a unique nonsecretory ribonuclease from urine of
pregnant women.";
J. Biochem. 111:325-330(1992).
[13]
PROTEIN SEQUENCE OF 28-45.
TISSUE=Urine;
PubMed=8471426; DOI=10.1038/bjc.1993.127;
Kardana A., Bagshawe K.D., Coles B., Read D., Taylor M.;
"Characterisation of UGP and its relationship with beta-core
fragment.";
Br. J. Cancer 67:686-692(1993).
[14]
GLYCOSYLATION AT TRP-34.
PubMed=7947762; DOI=10.1021/bi00250a003;
Hofsteenge J., Mueller D.R., de Beer T., Loeffler A., Richter W.J.,
Vliegenthart J.F.G.;
"New type of linkage between a carbohydrate and a protein: C-
glycosylation of a specific tryptophan residue in human RNase Us.";
Biochemistry 33:13524-13530(1994).
[15]
STRUCTURE OF C-GLYCOSYLATED GROUP.
PubMed=7547911; DOI=10.1021/bi00037a016;
de Beer T., Vliegenthart J.F.G., Loeffler A., Hofsteenge J.;
"The hexopyranosyl residue that is C-glycosidically linked to the side
chain of tryptophan-7 in human RNase Us is alpha-mannopyranose.";
Biochemistry 34:11785-11789(1995).
[16]
GLYCOSYLATION AT TRP-34.
PubMed=9450956; DOI=10.1091/mbc.9.2.301;
Krieg J., Hartmann S., Vicentini A., Glasner W., Hess D.,
Hofsteenge J.;
"Recognition signal for C-mannosylation of Trp-7 in RNase 2 consists
of sequence Trp-x-x-Trp.";
Mol. Biol. Cell 9:301-309(1998).
[17]
FUNCTION, AND INTERACTION WITH RNH1.
PubMed=12578357; DOI=10.1021/bi026852o;
Teufel D.P., Kao R.Y., Acharya K.R., Shapiro R.;
"Mutational analysis of the complex of human RNase inhibitor and human
eosinophil-derived neurotoxin (RNase 2).";
Biochemistry 42:1451-1459(2003).
[18]
INVOLVEMENT IN CHEMOTAXIS.
PubMed=12855582; DOI=10.1182/blood-2003-01-0151;
Yang D., Rosenberg H.F., Chen Q., Dyer K.D., Kurosaka K.,
Oppenheim J.J.;
"Eosinophil-derived neurotoxin (EDN), an antimicrobial protein with
chemotactic activities for dendritic cells.";
Blood 102:3396-3403(2003).
[19]
NITRATION AT TYR-60.
PubMed=18694936; DOI=10.1074/jbc.M801196200;
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., Lee J.J., Przybylski M.,
Doering G.;
"Post-translational tyrosine nitration of eosinophil granule toxins
mediated by eosinophil peroxidase.";
J. Biol. Chem. 283:28629-28640(2008).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[22]
X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS).
PubMed=8759319; DOI=10.1006/jmbi.1996.0420;
Mosimann S.C., Newton D.L., Youle R.J., James M.N.G.;
"X-ray crystallographic structure of recombinant eosinophil-derived
neurotoxin at 1.83-A resolution.";
J. Mol. Biol. 260:540-552(1996).
[23]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
PubMed=11154698; DOI=10.1074/jbc.M010585200;
Leonidas D.D., Boix E., Prill R., Suzuki M., Turton R., Minson K.,
Swaminathan G.J., Youle R.J., Acharya K.R.;
"Mapping the ribonucleolytic active site of eosinophil-derived
neurotoxin (EDN). High resolution crystal structures of EDN complexes
with adenylic nucleotide inhibitors.";
J. Biol. Chem. 276:15009-15017(2001).
[24]
X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) OF 28-161 IN COMPLEX WITH RNH1,
AND SUBUNIT.
PubMed=15755456; DOI=10.1016/j.jmb.2005.01.035;
Iyer S., Holloway D.E., Kumar K., Shapiro R., Acharya K.R.;
"Molecular recognition of human eosinophil-derived neurotoxin (RNase
2) by placental ribonuclease inhibitor.";
J. Mol. Biol. 347:637-655(2005).
[25]
X-RAY CRYSTALLOGRAPHY (0.98 ANGSTROMS) OF 28-161 IN COMPLEX WITH ADP
AND ATP.
PubMed=16401072; DOI=10.1021/bi0518592;
Baker M.D., Holloway D.E., Swaminathan G.J., Acharya K.R.;
"Crystal structures of eosinophil-derived neurotoxin (EDN) in complex
with the inhibitors 5'-ATP, Ap3A, Ap4A, and Ap5A.";
Biochemistry 45:416-426(2006).
-!- 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.
{ECO:0000269|PubMed:12578357, ECO:0000269|PubMed:3458170}.
-!- CATALYTIC ACTIVITY: Endonucleolytic cleavage to nucleoside 3'-
phosphates and 3'-phosphooligonucleotides ending in Cp or Up with
2',3'-cyclic phosphate intermediates.
-!- SUBUNIT: Interacts with and forms a tight 1:1 complex with RNH1.
Dimerization of two such complexes may occur.
{ECO:0000269|PubMed:12578357, ECO:0000269|PubMed:15755456,
ECO:0000269|PubMed:16401072}.
-!- SUBCELLULAR LOCATION: Lysosome {ECO:0000305}. 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.
-!- PTM: A particular signal processing and glycosylation pattern may
differentiate the UpI2 RNase, found specifically in pregnant women
urine, from other nonsecretory RNases.
{ECO:0000269|PubMed:7947762, ECO:0000269|PubMed:9450956}.
-!- SIMILARITY: Belongs to the pancreatic ribonuclease family.
{ECO:0000305}.
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EMBL; M30510; AAC82505.1; -; mRNA.
EMBL; M28129; AAA50284.1; -; mRNA.
EMBL; M24157; AAA52337.1; -; mRNA.
EMBL; X16546; CAA34546.1; -; Genomic_DNA.
EMBL; AF294007; AAG31577.1; -; Genomic_DNA.
EMBL; AF294008; AAG31578.1; -; Genomic_DNA.
EMBL; AF294009; AAG31579.1; -; Genomic_DNA.
EMBL; AF294010; AAG31580.1; -; Genomic_DNA.
EMBL; AF294011; AAG31581.1; -; Genomic_DNA.
EMBL; AF294012; AAG31582.1; -; Genomic_DNA.
EMBL; AF294013; AAG31583.1; -; Genomic_DNA.
EMBL; AF294014; AAG31584.1; -; Genomic_DNA.
EMBL; AF294015; AAG31585.1; -; Genomic_DNA.
EMBL; X55987; CAA39459.1; -; Genomic_DNA.
EMBL; X55988; CAA39460.1; -; mRNA.
EMBL; BC093678; AAH93678.1; -; mRNA.
EMBL; BC093680; AAH93680.1; -; mRNA.
EMBL; BC096059; AAH96059.1; -; mRNA.
CCDS; CCDS9561.1; -.
PIR; A35328; A33922.
RefSeq; NP_002925.1; NM_002934.2.
UniGene; Hs.728; -.
PDB; 1GQV; X-ray; 0.98 A; A=28-161.
PDB; 1HI2; X-ray; 1.60 A; A=28-161.
PDB; 1HI3; X-ray; 1.80 A; A=28-161.
PDB; 1HI4; X-ray; 1.80 A; A=28-161.
PDB; 1HI5; X-ray; 1.80 A; A=28-161.
PDB; 1K2A; X-ray; 1.00 A; A=26-160.
PDB; 2BEX; X-ray; 1.99 A; C/D=28-161.
PDB; 2BZZ; X-ray; 0.98 A; A=28-161.
PDB; 2C01; X-ray; 1.24 A; X=28-161.
PDB; 2C02; X-ray; 2.00 A; A=28-161.
PDB; 2C05; X-ray; 1.86 A; A=28-161.
PDB; 5E13; X-ray; 1.34 A; A=1-161.
PDBsum; 1GQV; -.
PDBsum; 1HI2; -.
PDBsum; 1HI3; -.
PDBsum; 1HI4; -.
PDBsum; 1HI5; -.
PDBsum; 1K2A; -.
PDBsum; 2BEX; -.
PDBsum; 2BZZ; -.
PDBsum; 2C01; -.
PDBsum; 2C02; -.
PDBsum; 2C05; -.
PDBsum; 5E13; -.
ProteinModelPortal; P10153; -.
SMR; P10153; -.
BioGrid; 111965; 2.
ELM; P10153; -.
IntAct; P10153; 1.
STRING; 9606.ENSP00000303276; -.
BindingDB; P10153; -.
ChEMBL; CHEMBL5120; -.
DrugBank; DB02098; Adenosine-2'-5'-Diphosphate.
DrugBank; DB01812; Adenosine-3'-5'-Diphosphate.
GlyConnect; 436; -.
GlyConnect; 437; -.
GlyConnect; 539; -.
iPTMnet; P10153; -.
PhosphoSitePlus; P10153; -.
UniCarbKB; P10153; -.
BioMuta; RNASE2; -.
DMDM; 133168; -.
EPD; P10153; -.
PaxDb; P10153; -.
PeptideAtlas; P10153; -.
PRIDE; P10153; -.
ProteomicsDB; 52573; -.
Ensembl; ENST00000304625; ENSP00000303276; ENSG00000169385.
GeneID; 6036; -.
KEGG; hsa:6036; -.
CTD; 6036; -.
DisGeNET; 6036; -.
EuPathDB; HostDB:ENSG00000169385.2; -.
GeneCards; RNASE2; -.
HGNC; HGNC:10045; RNASE2.
HPA; HPA044983; -.
MIM; 131410; gene.
neXtProt; NX_P10153; -.
OpenTargets; ENSG00000169385; -.
PharmGKB; PA34413; -.
eggNOG; ENOG410JDT3; Eukaryota.
eggNOG; ENOG411136R; LUCA.
GeneTree; ENSGT00900000140993; -.
HOGENOM; HOG000276882; -.
HOVERGEN; HBG008396; -.
InParanoid; P10153; -.
KO; K01168; -.
OMA; MFYIVAC; -.
OrthoDB; EOG091G0SFK; -.
PhylomeDB; P10153; -.
TreeFam; TF333393; -.
Reactome; R-HSA-6798695; Neutrophil degranulation.
ChiTaRS; RNASE2; human.
EvolutionaryTrace; P10153; -.
GeneWiki; Eosinophil-derived_neurotoxin; -.
GenomeRNAi; 6036; -.
PRO; PR:P10153; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000169385; Expressed in 137 organ(s), highest expression level in bone marrow.
CleanEx; HS_RNASE2; -.
ExpressionAtlas; P10153; baseline and differential.
Genevisible; P10153; HS.
GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0004519; F:endonuclease activity; IBA:GO_Central.
GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
GO; GO:0004522; F:ribonuclease A activity; IEA:UniProtKB-EC.
GO; GO:0004540; F:ribonuclease activity; IDA:UniProtKB.
GO; GO:0006935; P:chemotaxis; IDA:UniProtKB.
GO; GO:0051607; P:defense response to virus; IDA:UniProtKB.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0006401; P:RNA catabolic process; TAS:ProtInc.
GO; GO:0090501; P:RNA phosphodiester bond hydrolysis; IDA:UniProtKB.
Gene3D; 3.10.130.10; -; 1.
InterPro; IPR001427; RNaseA.
InterPro; IPR036816; RNaseA-like_dom_sf.
InterPro; IPR023411; RNaseA_AS.
InterPro; IPR023412; RNaseA_domain.
PANTHER; PTHR11437; PTHR11437; 1.
Pfam; PF00074; RnaseA; 1.
PRINTS; PR00794; RIBONUCLEASE.
ProDom; PD000535; RNaseA; 1.
SMART; SM00092; RNAse_Pc; 1.
SUPFAM; SSF54076; SSF54076; 1.
PROSITE; PS00127; RNASE_PANCREATIC; 1.
1: Evidence at protein level;
3D-structure; Chemotaxis; Complete proteome;
Direct protein sequencing; Disulfide bond; Endonuclease; Glycoprotein;
Hydrolase; Lysosome; Nitration; Nuclease; Polymorphism;
Reference proteome; Signal.
SIGNAL 1 27 {ECO:0000269|PubMed:3166997,
ECO:0000269|PubMed:3182786,
ECO:0000269|PubMed:3458170,
ECO:0000269|PubMed:3926759,
ECO:0000269|PubMed:8471426}.
CHAIN 28 161 Non-secretory ribonuclease.
/FTId=PRO_0000030874.
REGION 65 69 Substrate binding.
ACT_SITE 42 42 Proton acceptor.
ACT_SITE 156 156 Proton donor.
MOD_RES 60 60 Nitrated tyrosine.
{ECO:0000269|PubMed:18694936}.
CARBOHYD 34 34 C-linked (Man) tryptophan.
{ECO:0000269|PubMed:7947762,
ECO:0000269|PubMed:9450956}.
/FTId=CAR_000004.
CARBOHYD 44 44 N-linked (GlcNAc...) asparagine.
CARBOHYD 86 86 N-linked (GlcNAc...) asparagine.
CARBOHYD 92 92 N-linked (GlcNAc...) asparagine.
CARBOHYD 111 111 N-linked (GlcNAc...) asparagine.
CARBOHYD 119 119 N-linked (GlcNAc...) asparagine.
DISULFID 50 110
DISULFID 64 123
DISULFID 82 138
DISULFID 89 98
VARIANT 100 100 H -> Q (in dbSNP:rs8012891).
/FTId=VAR_059820.
VARIANT 156 156 H -> N (in dbSNP:rs146887874).
{ECO:0000269|PubMed:11102386}.
/FTId=VAR_013150.
CONFLICT 37 37 W -> R (in Ref. 10; AA sequence).
{ECO:0000305}.
CONFLICT 39 40 ET -> QE (in Ref. 10; AA sequence).
{ECO:0000305}.
CONFLICT 46 46 T -> V (in Ref. 10; AA sequence).
{ECO:0000305}.
CONFLICT 47 47 S -> T (in Ref. 11; AA sequence).
{ECO:0000305}.
HELIX 34 42 {ECO:0000244|PDB:1GQV}.
STRAND 46 49 {ECO:0000244|PDB:1GQV}.
HELIX 50 61 {ECO:0000244|PDB:1GQV}.
STRAND 66 73 {ECO:0000244|PDB:1GQV}.
HELIX 75 82 {ECO:0000244|PDB:1GQV}.
STRAND 98 100 {ECO:0000244|PDB:1GQV}.
STRAND 105 114 {ECO:0000244|PDB:1GQV}.
HELIX 120 122 {ECO:0000244|PDB:1GQV}.
STRAND 124 140 {ECO:0000244|PDB:1GQV}.
TURN 143 145 {ECO:0000244|PDB:1GQV}.
STRAND 151 161 {ECO:0000244|PDB:1GQV}.
SEQUENCE 161 AA; 18354 MW; 9406C4596CA69038 CRC64;
MVPKLFTSQI CLLLLLGLLA VEGSLHVKPP QFTWAQWFET QHINMTSQQC TNAMQVINNY
QRRCKNQNTF LLTTFANVVN VCGNPNMTCP SNKTRKNCHH SGSQVPLIHC NLTTPSPQNI
SNCRYAQTPA NMFYIVACDN RDQRRDPPQY PVVPVHLDRI I


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E1758r ELISA kit Ear11,EAR-11,ECP,Eosinophil cationic protein,Eosinophil secondary granule ribonuclease 11,Rat,Rattus norvegicus,Ribonuclease 3,RNase 3,Rnase3,Rns3 96T
CSB-EL019794PI Pig ribonuclease, RNase A family, 2 (liver, eosinophil-derived neurotoxin) (RNASE2) ELISA kit, Species Pig, Sample Type serum, plasma 96T
EIAAB35510 2-5A-dependent ribonuclease,2-5A-dependent RNase,Homo sapiens,Human,Ribonuclease 4,Ribonuclease L,RNase L,RNASEL,RNS4
EIAAB35609 AGS4,Aicardi-Goutieres syndrome 4 protein,Homo sapiens,Human,Ribonuclease H2 subunit A,Ribonuclease HI large subunit,Ribonuclease HI subunit A,RNase H(35),RNase H2 subunit A,RNase HI large subunit,RNA
RNASE2 RNASE2 Gene ribonuclease, RNase A family, 2 (liver, eosinophil-derived neurotoxin)
EIAAB35511 2-5A-dependent ribonuclease,2-5A-dependent RNase,Mouse,Mus musculus,Ribonuclease 4,Ribonuclease L,RNase L,Rnasel,Rns4


 

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