Full text data of RNASE3
RNASE3
(ECP, RNS3)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Eosinophil cationic protein; ECP; 3.1.27.- (Ribonuclease 3; RNase 3; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Eosinophil cationic protein; ECP; 3.1.27.- (Ribonuclease 3; RNase 3; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P12724
ID ECP_HUMAN Reviewed; 160 AA.
AC P12724; Q4VBC1; Q8WTP7; Q8WZ62; Q9GZN9;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
read moreDT 15-MAY-2007, sequence version 2.
DT 22-JAN-2014, entry version 142.
DE RecName: Full=Eosinophil cationic protein;
DE Short=ECP;
DE EC=3.1.27.-;
DE AltName: Full=Ribonuclease 3;
DE Short=RNase 3;
DE Flags: Precursor;
GN Name=RNASE3; Synonyms=ECP, RNS3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ARG-124.
RC TISSUE=Peripheral blood granulocyte;
RX PubMed=2473157; DOI=10.1084/jem.170.1.163;
RA Rosenberg H.F., Ackerman S.J., Tenen D.G.;
RT "Human eosinophil cationic protein. Molecular cloning of a cytotoxin
RT and helminthotoxin with ribonuclease activity.";
RL J. Exp. Med. 170:163-176(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ARG-124.
RC TISSUE=Fetal liver;
RX PubMed=2387583; DOI=10.1016/0888-7543(90)90197-3;
RA Hamann K.J., Ten R.M., Loegering D.A., Jenkins R.B., Heise M.T.,
RA Schad C.R., Pease L.R., Gleich G.J., Barker R.L.;
RT "Structure and chromosome localization of the human eosinophil-derived
RT neurotoxin and eosinophil cationic protein genes: evidence for
RT intronless coding sequences in the ribonuclease gene superfamily.";
RL Genomics 7:535-546(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ARG-124.
RX PubMed=2745977;
RA Barker R.L., Loegering D.A., Ten R.M., Hamann K.J., Pease L.R.,
RA Gleich G.J.;
RT "Eosinophil cationic protein cDNA. Comparison with other toxic
RT cationic proteins and ribonucleases.";
RL J. Immunol. 143:952-955(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ARG-124.
RC TISSUE=Colon;
RA Simonsen C.C., Kennedy J., Comstock L., Ashton N., McGrogan M.;
RL Submitted (OCT-1990) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ARG-124.
RX PubMed=11102386;
RA Zhang J., Rosenberg H.F.;
RT "Sequence variation at two eosinophil-associated ribonuclease loci in
RT humans.";
RL Genetics 156:1949-1958(2000).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
RA Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
RA Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
RA Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
RA Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
RA Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
RA Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
RA Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
RA Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
RA Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
RA Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
RA Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
RA Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
RA Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
RA Quetier F., Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-124.
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 20-160, AND VARIANTS CYS-72 AND
RP ARG-124.
RA Bystrom J., Molin D., Jonsson U.B., Enblad G., Sundstrom C.,
RA Hogbom E., Venge P.;
RT "Identification of polymorphisms in the ECP gene. Relation to disease
RT activity in Hodgkins lymphoma.";
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP PROTEIN SEQUENCE OF 28-87.
RX PubMed=3458170; DOI=10.1073/pnas.83.10.3146;
RA Gleich G.J., Loegering D.A., Bell M.P., Checkel J.L., Ackerman S.J.,
RA McKean D.J.;
RT "Biochemical and functional similarities between human eosinophil-
RT derived neurotoxin and eosinophil cationic protein: homology with
RT ribonuclease.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:3146-3150(1986).
RN [10]
RP PROTEIN SEQUENCE OF 28-47, AND FUNCTION AS AN ANTIMICROBIAL PROTEIN.
RX PubMed=2501794; DOI=10.1073/pnas.86.14.5610;
RA Gabay J.E., Scott R.W., Campanelli D., Griffith J., Wilde C.,
RA Marra M.N., Seeger M., Nathan C.F.;
RT "Antibiotic proteins of human polymorphonuclear leukocytes.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:5610-5614(1989).
RN [11]
RP NITRATION AT TYR-60.
RX PubMed=18694936; DOI=10.1074/jbc.M801196200;
RA Ulrich M., Petre A., Youhnovski N., Proemm F., Schirle M., Schumm M.,
RA Pero R.S., Doyle A., Checkel J., Kita H., Thiyagarajan N.,
RA Acharya K.R., Schmid-Grendelmeier P., Simon H.-U., Schwarz H.,
RA Tsutsui M., Shimokawa H., Bellon G., Lee J.J., Przybylski M.,
RA Doering G.;
RT "Post-translational tyrosine nitration of eosinophil granule toxins
RT mediated by eosinophil peroxidase.";
RL J. Biol. Chem. 283:28629-28640(2008).
RN [12]
RP FUNCTION, AND INTERACTION WITH LPS; LTA AND LIPID BILAYERS.
RX PubMed=19450231; DOI=10.1042/BJ20082330;
RA Torrent M., de la Torre B.G., Nogues V.M., Andreu D., Boix E.;
RT "Bactericidal and membrane disruption activities of the eosinophil
RT cationic protein are largely retained in an N-terminal fragment.";
RL Biochem. J. 421:425-434(2009).
RN [13]
RP IN VITRO FORMATION OF AMYLOID-LIKE AGGREGATES, AND MUTAGENESIS OF
RP ILE-40.
RX PubMed=20690710; DOI=10.1021/bm100334u;
RA Torrent M., Odorizzi F., Nogues M.V., Boix E.;
RT "Eosinophil cationic protein aggregation: identification of an N-
RT terminus amyloid prone region.";
RL Biomacromolecules 11:1983-1990(2010).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 28-160.
RX PubMed=10606511; DOI=10.1021/bi9919145;
RA Boix E., Leonidas D.D., Nikolovski Z., Nogues M.V., Cuchillo C.M.,
RA Acharya K.R.;
RT "Crystal structure of eosinophil cationic protein at 2.4 A
RT resolution.";
RL Biochemistry 38:16794-16801(1999).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 28-160.
RX PubMed=10903870; DOI=10.1006/jmbi.2000.3939;
RA Mallorqui-Fernandez G., Pous J., Peracaula R., Aymami J., Maeda T.,
RA Tada H., Yamada H., Seno M., de Llorens R., Gomis-Rueth F.-X.,
RA Coll M.;
RT "Three-dimensional crystal structure of human eosinophil cationic
RT protein (RNase 3) at 1.75 A resolution.";
RL J. Mol. Biol. 300:1297-1307(2000).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 28-160.
RX PubMed=12356310; DOI=10.1021/bi0264521;
RA Mohan C.G., Boix E., Evans H.R., Nikolovski Z., Nogues M.V.,
RA Cuchillo C.M., Acharya K.R.;
RT "The crystal structure of eosinophil cationic protein in complex with
RT 2',5'-ADP at 2.0 A resolution reveals the details of the
RT ribonucleolytic active site.";
RL Biochemistry 41:12100-12106(2002).
CC -!- FUNCTION: Cytotoxin and helminthotoxin with low-efficiency
CC ribonuclease activity. Possesses a wide variety of biological
CC activities. Exhibits antibacterial activity, including cytoplasmic
CC membrane depolarization of preferentially Gram-negative, but also
CC Gram-positive strains. Promotes E.coli outer membrane detachment,
CC alteration of the overall cell shape and partial loss of cell
CC content.
CC -!- SUBUNIT: Interacts with bacterial lipopolysaccharide (LPS) and
CC lipoteichoic acid (LTA). In vitro interacts with and insert into
CC lipid bilayers composed of dioleoyl phosphatidylcholine and
CC dioleoyl phosphatidylglycerol. In vitro, tends to form amyloid-
CC like aggregates at pH 3, but not at pH 5, nor 7.
CC -!- SUBCELLULAR LOCATION: Secreted. Note=Located in the matrix of
CC eosinophil large specific granule, which are released following
CC activation by an immune stimulus.
CC -!- SIMILARITY: Belongs to the pancreatic ribonuclease family.
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DR EMBL; X15161; CAA33251.1; -; mRNA.
DR EMBL; M28128; AAA50283.1; -; mRNA.
DR EMBL; X16545; CAA34545.1; -; Genomic_DNA.
DR EMBL; X55990; CAA39462.1; -; Genomic_DNA.
DR EMBL; AF294019; AAG31589.1; -; Genomic_DNA.
DR EMBL; AF294020; AAG31590.1; -; Genomic_DNA.
DR EMBL; AF294021; AAG31591.1; -; Genomic_DNA.
DR EMBL; AF294022; AAG31592.1; -; Genomic_DNA.
DR EMBL; AF294023; AAG31593.1; -; Genomic_DNA.
DR EMBL; AF294024; AAG31594.1; -; Genomic_DNA.
DR EMBL; AF294025; AAG31595.1; -; Genomic_DNA.
DR EMBL; AF294026; AAG31596.1; -; Genomic_DNA.
DR EMBL; AL133371; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC096060; AAH96060.1; -; mRNA.
DR EMBL; BC096061; AAH96061.1; -; mRNA.
DR EMBL; BC096062; AAH96062.1; -; mRNA.
DR EMBL; AF441204; AAL35279.1; -; Genomic_DNA.
DR EMBL; AF441205; AAL35280.1; -; Genomic_DNA.
DR EMBL; AF441206; AAL35281.1; -; Genomic_DNA.
DR PIR; B35328; JL0106.
DR RefSeq; NP_002926.2; NM_002935.2.
DR UniGene; Hs.73839; -.
DR PDB; 1DYT; X-ray; 1.75 A; A/B=28-160.
DR PDB; 1H1H; X-ray; 2.00 A; A=28-160.
DR PDB; 1QMT; X-ray; 2.40 A; A=27-160.
DR PDB; 2KB5; NMR; -; A=28-160.
DR PDB; 2LVZ; NMR; -; A=28-160.
DR PDB; 4A2O; X-ray; 1.69 A; A/B=28-160.
DR PDB; 4A2Y; X-ray; 1.70 A; A/B=28-160.
DR PDBsum; 1DYT; -.
DR PDBsum; 1H1H; -.
DR PDBsum; 1QMT; -.
DR PDBsum; 2KB5; -.
DR PDBsum; 2LVZ; -.
DR PDBsum; 4A2O; -.
DR PDBsum; 4A2Y; -.
DR ProteinModelPortal; P12724; -.
DR SMR; P12724; 28-160.
DR STRING; 9606.ENSP00000302324; -.
DR DrugBank; DB01411; Pranlukast.
DR PhosphoSite; P12724; -.
DR DMDM; 147744558; -.
DR PaxDb; P12724; -.
DR PRIDE; P12724; -.
DR Ensembl; ENST00000304639; ENSP00000302324; ENSG00000169397.
DR GeneID; 6037; -.
DR KEGG; hsa:6037; -.
DR UCSC; uc001vyj.3; human.
DR CTD; 6037; -.
DR GeneCards; GC14P021359; -.
DR H-InvDB; HIX0037784; -.
DR HGNC; HGNC:10046; RNASE3.
DR MIM; 131398; gene.
DR neXtProt; NX_P12724; -.
DR PharmGKB; PA34414; -.
DR eggNOG; NOG118739; -.
DR HOGENOM; HOG000276882; -.
DR HOVERGEN; HBG008396; -.
DR InParanoid; P12724; -.
DR KO; K10787; -.
DR OMA; NISRNCH; -.
DR OrthoDB; EOG7KDFCP; -.
DR PhylomeDB; P12724; -.
DR EvolutionaryTrace; P12724; -.
DR GeneWiki; Eosinophil_cationic_protein; -.
DR GenomeRNAi; 6037; -.
DR NextBio; 23529; -.
DR PRO; PR:P12724; -.
DR Bgee; P12724; -.
DR CleanEx; HS_RNASE3; -.
DR Genevestigator; P12724; -.
DR GO; GO:0005576; C:extracellular region; TAS:ProtInc.
DR GO; GO:0016892; F:endoribonuclease activity, producing 3'-phosphomonoesters; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0004540; F:ribonuclease activity; TAS:ProtInc.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0006401; P:RNA catabolic process; TAS:ProtInc.
DR Gene3D; 3.10.130.10; -; 1.
DR InterPro; IPR001427; RNaseA.
DR InterPro; IPR023411; RNaseA_AS.
DR InterPro; IPR023412; RNaseA_domain.
DR PANTHER; PTHR11437; PTHR11437; 1.
DR Pfam; PF00074; RnaseA; 1.
DR PRINTS; PR00794; RIBONUCLEASE.
DR ProDom; PD000535; RNaseA; 1.
DR SMART; SM00092; RNAse_Pc; 1.
DR SUPFAM; SSF54076; SSF54076; 1.
DR PROSITE; PS00127; RNASE_PANCREATIC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic; Antimicrobial; Complete proteome;
KW Direct protein sequencing; Disulfide bond; Endonuclease; Glycoprotein;
KW Hydrolase; Nitration; Nuclease; Polymorphism; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1 27
FT CHAIN 28 160 Eosinophil cationic protein.
FT /FTId=PRO_0000030862.
FT REGION 28 72 Required for nearly all of the
FT bactericidal activity; partially involved
FT in LPS-binding and bacterial membrane
FT depolarization.
FT REGION 65 69 Substrate binding.
FT ACT_SITE 42 42 Proton acceptor.
FT ACT_SITE 155 155 Proton donor.
FT SITE 60 60 May be involved in LPS-binding.
FT SITE 62 62 May be involved in LPS- and LTA-binding.
FT MOD_RES 60 60 Nitrated tyrosine.
FT CARBOHYD 84 84 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 92 92 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 119 119 N-linked (GlcNAc...) (Potential).
FT DISULFID 50 110
FT DISULFID 64 123
FT DISULFID 82 138
FT DISULFID 89 98
FT VARIANT 72 72 R -> C (in dbSNP:rs151169198).
FT /FTId=VAR_014109.
FT VARIANT 124 124 T -> R (in dbSNP:rs2073342).
FT /FTId=VAR_013149.
FT VARIANT 130 130 G -> R (in dbSNP:rs12147890).
FT /FTId=VAR_029017.
FT MUTAGEN 40 40 I->A: Loss of in vitro formation of
FT amyloid-like aggregates.
FT STRAND 30 32
FT HELIX 34 42
FT HELIX 50 53
FT HELIX 55 58
FT STRAND 61 63
FT STRAND 66 73
FT HELIX 75 81
FT TURN 93 95
FT STRAND 98 100
FT STRAND 105 113
FT HELIX 120 122
FT STRAND 125 132
FT STRAND 134 140
FT TURN 143 145
FT STRAND 150 159
SQ SEQUENCE 160 AA; 18385 MW; D7BED24F67B23FA9 CRC64;
MVPKLFTSQI CLLLLLGLMG VEGSLHARPP QFTRAQWFAI QHISLNPPRC TIAMRAINNY
RWRCKNQNTF LRTTFANVVN VCGNQSIRCP HNRTLNNCHR SRFRVPLLHC DLINPGAQNI
SNCTYADRPG RRFYVVACDN RDPRDSPRYP VVPVHLDTTI
//
ID ECP_HUMAN Reviewed; 160 AA.
AC P12724; Q4VBC1; Q8WTP7; Q8WZ62; Q9GZN9;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
read moreDT 15-MAY-2007, sequence version 2.
DT 22-JAN-2014, entry version 142.
DE RecName: Full=Eosinophil cationic protein;
DE Short=ECP;
DE EC=3.1.27.-;
DE AltName: Full=Ribonuclease 3;
DE Short=RNase 3;
DE Flags: Precursor;
GN Name=RNASE3; Synonyms=ECP, RNS3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ARG-124.
RC TISSUE=Peripheral blood granulocyte;
RX PubMed=2473157; DOI=10.1084/jem.170.1.163;
RA Rosenberg H.F., Ackerman S.J., Tenen D.G.;
RT "Human eosinophil cationic protein. Molecular cloning of a cytotoxin
RT and helminthotoxin with ribonuclease activity.";
RL J. Exp. Med. 170:163-176(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ARG-124.
RC TISSUE=Fetal liver;
RX PubMed=2387583; DOI=10.1016/0888-7543(90)90197-3;
RA Hamann K.J., Ten R.M., Loegering D.A., Jenkins R.B., Heise M.T.,
RA Schad C.R., Pease L.R., Gleich G.J., Barker R.L.;
RT "Structure and chromosome localization of the human eosinophil-derived
RT neurotoxin and eosinophil cationic protein genes: evidence for
RT intronless coding sequences in the ribonuclease gene superfamily.";
RL Genomics 7:535-546(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ARG-124.
RX PubMed=2745977;
RA Barker R.L., Loegering D.A., Ten R.M., Hamann K.J., Pease L.R.,
RA Gleich G.J.;
RT "Eosinophil cationic protein cDNA. Comparison with other toxic
RT cationic proteins and ribonucleases.";
RL J. Immunol. 143:952-955(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ARG-124.
RC TISSUE=Colon;
RA Simonsen C.C., Kennedy J., Comstock L., Ashton N., McGrogan M.;
RL Submitted (OCT-1990) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ARG-124.
RX PubMed=11102386;
RA Zhang J., Rosenberg H.F.;
RT "Sequence variation at two eosinophil-associated ribonuclease loci in
RT humans.";
RL Genetics 156:1949-1958(2000).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
RA Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
RA Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
RA Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
RA Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
RA Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
RA Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
RA Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
RA Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
RA Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
RA Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
RA Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
RA Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
RA Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
RA Quetier F., Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-124.
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 20-160, AND VARIANTS CYS-72 AND
RP ARG-124.
RA Bystrom J., Molin D., Jonsson U.B., Enblad G., Sundstrom C.,
RA Hogbom E., Venge P.;
RT "Identification of polymorphisms in the ECP gene. Relation to disease
RT activity in Hodgkins lymphoma.";
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP PROTEIN SEQUENCE OF 28-87.
RX PubMed=3458170; DOI=10.1073/pnas.83.10.3146;
RA Gleich G.J., Loegering D.A., Bell M.P., Checkel J.L., Ackerman S.J.,
RA McKean D.J.;
RT "Biochemical and functional similarities between human eosinophil-
RT derived neurotoxin and eosinophil cationic protein: homology with
RT ribonuclease.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:3146-3150(1986).
RN [10]
RP PROTEIN SEQUENCE OF 28-47, AND FUNCTION AS AN ANTIMICROBIAL PROTEIN.
RX PubMed=2501794; DOI=10.1073/pnas.86.14.5610;
RA Gabay J.E., Scott R.W., Campanelli D., Griffith J., Wilde C.,
RA Marra M.N., Seeger M., Nathan C.F.;
RT "Antibiotic proteins of human polymorphonuclear leukocytes.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:5610-5614(1989).
RN [11]
RP NITRATION AT TYR-60.
RX PubMed=18694936; DOI=10.1074/jbc.M801196200;
RA Ulrich M., Petre A., Youhnovski N., Proemm F., Schirle M., Schumm M.,
RA Pero R.S., Doyle A., Checkel J., Kita H., Thiyagarajan N.,
RA Acharya K.R., Schmid-Grendelmeier P., Simon H.-U., Schwarz H.,
RA Tsutsui M., Shimokawa H., Bellon G., Lee J.J., Przybylski M.,
RA Doering G.;
RT "Post-translational tyrosine nitration of eosinophil granule toxins
RT mediated by eosinophil peroxidase.";
RL J. Biol. Chem. 283:28629-28640(2008).
RN [12]
RP FUNCTION, AND INTERACTION WITH LPS; LTA AND LIPID BILAYERS.
RX PubMed=19450231; DOI=10.1042/BJ20082330;
RA Torrent M., de la Torre B.G., Nogues V.M., Andreu D., Boix E.;
RT "Bactericidal and membrane disruption activities of the eosinophil
RT cationic protein are largely retained in an N-terminal fragment.";
RL Biochem. J. 421:425-434(2009).
RN [13]
RP IN VITRO FORMATION OF AMYLOID-LIKE AGGREGATES, AND MUTAGENESIS OF
RP ILE-40.
RX PubMed=20690710; DOI=10.1021/bm100334u;
RA Torrent M., Odorizzi F., Nogues M.V., Boix E.;
RT "Eosinophil cationic protein aggregation: identification of an N-
RT terminus amyloid prone region.";
RL Biomacromolecules 11:1983-1990(2010).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 28-160.
RX PubMed=10606511; DOI=10.1021/bi9919145;
RA Boix E., Leonidas D.D., Nikolovski Z., Nogues M.V., Cuchillo C.M.,
RA Acharya K.R.;
RT "Crystal structure of eosinophil cationic protein at 2.4 A
RT resolution.";
RL Biochemistry 38:16794-16801(1999).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 28-160.
RX PubMed=10903870; DOI=10.1006/jmbi.2000.3939;
RA Mallorqui-Fernandez G., Pous J., Peracaula R., Aymami J., Maeda T.,
RA Tada H., Yamada H., Seno M., de Llorens R., Gomis-Rueth F.-X.,
RA Coll M.;
RT "Three-dimensional crystal structure of human eosinophil cationic
RT protein (RNase 3) at 1.75 A resolution.";
RL J. Mol. Biol. 300:1297-1307(2000).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 28-160.
RX PubMed=12356310; DOI=10.1021/bi0264521;
RA Mohan C.G., Boix E., Evans H.R., Nikolovski Z., Nogues M.V.,
RA Cuchillo C.M., Acharya K.R.;
RT "The crystal structure of eosinophil cationic protein in complex with
RT 2',5'-ADP at 2.0 A resolution reveals the details of the
RT ribonucleolytic active site.";
RL Biochemistry 41:12100-12106(2002).
CC -!- FUNCTION: Cytotoxin and helminthotoxin with low-efficiency
CC ribonuclease activity. Possesses a wide variety of biological
CC activities. Exhibits antibacterial activity, including cytoplasmic
CC membrane depolarization of preferentially Gram-negative, but also
CC Gram-positive strains. Promotes E.coli outer membrane detachment,
CC alteration of the overall cell shape and partial loss of cell
CC content.
CC -!- SUBUNIT: Interacts with bacterial lipopolysaccharide (LPS) and
CC lipoteichoic acid (LTA). In vitro interacts with and insert into
CC lipid bilayers composed of dioleoyl phosphatidylcholine and
CC dioleoyl phosphatidylglycerol. In vitro, tends to form amyloid-
CC like aggregates at pH 3, but not at pH 5, nor 7.
CC -!- SUBCELLULAR LOCATION: Secreted. Note=Located in the matrix of
CC eosinophil large specific granule, which are released following
CC activation by an immune stimulus.
CC -!- SIMILARITY: Belongs to the pancreatic ribonuclease family.
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DR EMBL; X15161; CAA33251.1; -; mRNA.
DR EMBL; M28128; AAA50283.1; -; mRNA.
DR EMBL; X16545; CAA34545.1; -; Genomic_DNA.
DR EMBL; X55990; CAA39462.1; -; Genomic_DNA.
DR EMBL; AF294019; AAG31589.1; -; Genomic_DNA.
DR EMBL; AF294020; AAG31590.1; -; Genomic_DNA.
DR EMBL; AF294021; AAG31591.1; -; Genomic_DNA.
DR EMBL; AF294022; AAG31592.1; -; Genomic_DNA.
DR EMBL; AF294023; AAG31593.1; -; Genomic_DNA.
DR EMBL; AF294024; AAG31594.1; -; Genomic_DNA.
DR EMBL; AF294025; AAG31595.1; -; Genomic_DNA.
DR EMBL; AF294026; AAG31596.1; -; Genomic_DNA.
DR EMBL; AL133371; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC096060; AAH96060.1; -; mRNA.
DR EMBL; BC096061; AAH96061.1; -; mRNA.
DR EMBL; BC096062; AAH96062.1; -; mRNA.
DR EMBL; AF441204; AAL35279.1; -; Genomic_DNA.
DR EMBL; AF441205; AAL35280.1; -; Genomic_DNA.
DR EMBL; AF441206; AAL35281.1; -; Genomic_DNA.
DR PIR; B35328; JL0106.
DR RefSeq; NP_002926.2; NM_002935.2.
DR UniGene; Hs.73839; -.
DR PDB; 1DYT; X-ray; 1.75 A; A/B=28-160.
DR PDB; 1H1H; X-ray; 2.00 A; A=28-160.
DR PDB; 1QMT; X-ray; 2.40 A; A=27-160.
DR PDB; 2KB5; NMR; -; A=28-160.
DR PDB; 2LVZ; NMR; -; A=28-160.
DR PDB; 4A2O; X-ray; 1.69 A; A/B=28-160.
DR PDB; 4A2Y; X-ray; 1.70 A; A/B=28-160.
DR PDBsum; 1DYT; -.
DR PDBsum; 1H1H; -.
DR PDBsum; 1QMT; -.
DR PDBsum; 2KB5; -.
DR PDBsum; 2LVZ; -.
DR PDBsum; 4A2O; -.
DR PDBsum; 4A2Y; -.
DR ProteinModelPortal; P12724; -.
DR SMR; P12724; 28-160.
DR STRING; 9606.ENSP00000302324; -.
DR DrugBank; DB01411; Pranlukast.
DR PhosphoSite; P12724; -.
DR DMDM; 147744558; -.
DR PaxDb; P12724; -.
DR PRIDE; P12724; -.
DR Ensembl; ENST00000304639; ENSP00000302324; ENSG00000169397.
DR GeneID; 6037; -.
DR KEGG; hsa:6037; -.
DR UCSC; uc001vyj.3; human.
DR CTD; 6037; -.
DR GeneCards; GC14P021359; -.
DR H-InvDB; HIX0037784; -.
DR HGNC; HGNC:10046; RNASE3.
DR MIM; 131398; gene.
DR neXtProt; NX_P12724; -.
DR PharmGKB; PA34414; -.
DR eggNOG; NOG118739; -.
DR HOGENOM; HOG000276882; -.
DR HOVERGEN; HBG008396; -.
DR InParanoid; P12724; -.
DR KO; K10787; -.
DR OMA; NISRNCH; -.
DR OrthoDB; EOG7KDFCP; -.
DR PhylomeDB; P12724; -.
DR EvolutionaryTrace; P12724; -.
DR GeneWiki; Eosinophil_cationic_protein; -.
DR GenomeRNAi; 6037; -.
DR NextBio; 23529; -.
DR PRO; PR:P12724; -.
DR Bgee; P12724; -.
DR CleanEx; HS_RNASE3; -.
DR Genevestigator; P12724; -.
DR GO; GO:0005576; C:extracellular region; TAS:ProtInc.
DR GO; GO:0016892; F:endoribonuclease activity, producing 3'-phosphomonoesters; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0004540; F:ribonuclease activity; TAS:ProtInc.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0006401; P:RNA catabolic process; TAS:ProtInc.
DR Gene3D; 3.10.130.10; -; 1.
DR InterPro; IPR001427; RNaseA.
DR InterPro; IPR023411; RNaseA_AS.
DR InterPro; IPR023412; RNaseA_domain.
DR PANTHER; PTHR11437; PTHR11437; 1.
DR Pfam; PF00074; RnaseA; 1.
DR PRINTS; PR00794; RIBONUCLEASE.
DR ProDom; PD000535; RNaseA; 1.
DR SMART; SM00092; RNAse_Pc; 1.
DR SUPFAM; SSF54076; SSF54076; 1.
DR PROSITE; PS00127; RNASE_PANCREATIC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic; Antimicrobial; Complete proteome;
KW Direct protein sequencing; Disulfide bond; Endonuclease; Glycoprotein;
KW Hydrolase; Nitration; Nuclease; Polymorphism; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1 27
FT CHAIN 28 160 Eosinophil cationic protein.
FT /FTId=PRO_0000030862.
FT REGION 28 72 Required for nearly all of the
FT bactericidal activity; partially involved
FT in LPS-binding and bacterial membrane
FT depolarization.
FT REGION 65 69 Substrate binding.
FT ACT_SITE 42 42 Proton acceptor.
FT ACT_SITE 155 155 Proton donor.
FT SITE 60 60 May be involved in LPS-binding.
FT SITE 62 62 May be involved in LPS- and LTA-binding.
FT MOD_RES 60 60 Nitrated tyrosine.
FT CARBOHYD 84 84 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 92 92 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 119 119 N-linked (GlcNAc...) (Potential).
FT DISULFID 50 110
FT DISULFID 64 123
FT DISULFID 82 138
FT DISULFID 89 98
FT VARIANT 72 72 R -> C (in dbSNP:rs151169198).
FT /FTId=VAR_014109.
FT VARIANT 124 124 T -> R (in dbSNP:rs2073342).
FT /FTId=VAR_013149.
FT VARIANT 130 130 G -> R (in dbSNP:rs12147890).
FT /FTId=VAR_029017.
FT MUTAGEN 40 40 I->A: Loss of in vitro formation of
FT amyloid-like aggregates.
FT STRAND 30 32
FT HELIX 34 42
FT HELIX 50 53
FT HELIX 55 58
FT STRAND 61 63
FT STRAND 66 73
FT HELIX 75 81
FT TURN 93 95
FT STRAND 98 100
FT STRAND 105 113
FT HELIX 120 122
FT STRAND 125 132
FT STRAND 134 140
FT TURN 143 145
FT STRAND 150 159
SQ SEQUENCE 160 AA; 18385 MW; D7BED24F67B23FA9 CRC64;
MVPKLFTSQI CLLLLLGLMG VEGSLHARPP QFTRAQWFAI QHISLNPPRC TIAMRAINNY
RWRCKNQNTF LRTTFANVVN VCGNQSIRCP HNRTLNNCHR SRFRVPLLHC DLINPGAQNI
SNCTYADRPG RRFYVVACDN RDPRDSPRYP VVPVHLDTTI
//
MIM
131398
*RECORD*
*FIELD* NO
131398
*FIELD* TI
*131398 RIBONUCLEASE A FAMILY, 3; RNASE3
;;RNS3;;
EOSINOPHIL CATIONIC PROTEIN; ECP
read more*FIELD* TX
Eosinophil cationic protein, like eosinophil-derived neurotoxin, is
localized to the granule matrix of the eosinophil. Both proteins possess
neurotoxic, helminthotoxic, and ribonucleolytic activities. The cDNA
sequences of the genes encoding these 2 proteins and the deduced amino
acid sequences indicate that the genes belong to the ribonuclease gene
superfamily. Hamann et al. (1990) demonstrated remarkable similarities
of eosinophil-derived neurotoxin and eosinophil cationic protein,
symbolized RNS2 (131410) and RNS3, respectively, in noncoding sequences,
introns, and flanking regions, as well as the previously known coding
regions. A single intron in the 5-prime untranslated region and an
intronless coding region appear to be features common to many members of
the RNase gene superfamily. Both genes were mapped to 14q24-q31 by a
combination of analysis of somatic cell hybrids and in situ
hybridization (Hamann et al., 1990). Mastrianni et al. (1992) confirmed
the assignment of both RNS2 and RNS3 to chromosome 14 by Southern
analysis of DNAs from mouse-human cell hybrids. They commented on the
fact that another eosinophil granule protein is encoded by a gene on
chromosome 19 (CLC; 153310) and yet another, eosinophil peroxidase
(131399), by a gene on chromosome 17.
*FIELD* RF
1. 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.
2. Mastrianni, D. M.; Eddy, R. L.; Rosenberg, H. F.; Corrette, S.
E.; Shows, T. B.; Tenen, D. G.; Ackerman, S. J.: Localization of
the human eosinophil Charcot-Leyden crystal protein (lysophospholipase)
gene (CLC) to chromosome 19 and the human ribonuclease 2 (eosinophil-derived
neurotoxin) and ribonuclease 3 (eosinophil cationic protein) genes
(RNS2 and RNS3) to chromosome 14. Genomics 13: 240-242, 1992.
*FIELD* CD
Victor A. McKusick: 8/22/1990
*FIELD* ED
dholmes: 09/16/1997
dholmes: 9/16/1997
mark: 3/25/1997
carol: 5/22/1992
supermim: 3/16/1992
carol: 2/16/1992
carol: 8/22/1990
*RECORD*
*FIELD* NO
131398
*FIELD* TI
*131398 RIBONUCLEASE A FAMILY, 3; RNASE3
;;RNS3;;
EOSINOPHIL CATIONIC PROTEIN; ECP
read more*FIELD* TX
Eosinophil cationic protein, like eosinophil-derived neurotoxin, is
localized to the granule matrix of the eosinophil. Both proteins possess
neurotoxic, helminthotoxic, and ribonucleolytic activities. The cDNA
sequences of the genes encoding these 2 proteins and the deduced amino
acid sequences indicate that the genes belong to the ribonuclease gene
superfamily. Hamann et al. (1990) demonstrated remarkable similarities
of eosinophil-derived neurotoxin and eosinophil cationic protein,
symbolized RNS2 (131410) and RNS3, respectively, in noncoding sequences,
introns, and flanking regions, as well as the previously known coding
regions. A single intron in the 5-prime untranslated region and an
intronless coding region appear to be features common to many members of
the RNase gene superfamily. Both genes were mapped to 14q24-q31 by a
combination of analysis of somatic cell hybrids and in situ
hybridization (Hamann et al., 1990). Mastrianni et al. (1992) confirmed
the assignment of both RNS2 and RNS3 to chromosome 14 by Southern
analysis of DNAs from mouse-human cell hybrids. They commented on the
fact that another eosinophil granule protein is encoded by a gene on
chromosome 19 (CLC; 153310) and yet another, eosinophil peroxidase
(131399), by a gene on chromosome 17.
*FIELD* RF
1. 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.
2. Mastrianni, D. M.; Eddy, R. L.; Rosenberg, H. F.; Corrette, S.
E.; Shows, T. B.; Tenen, D. G.; Ackerman, S. J.: Localization of
the human eosinophil Charcot-Leyden crystal protein (lysophospholipase)
gene (CLC) to chromosome 19 and the human ribonuclease 2 (eosinophil-derived
neurotoxin) and ribonuclease 3 (eosinophil cationic protein) genes
(RNS2 and RNS3) to chromosome 14. Genomics 13: 240-242, 1992.
*FIELD* CD
Victor A. McKusick: 8/22/1990
*FIELD* ED
dholmes: 09/16/1997
dholmes: 9/16/1997
mark: 3/25/1997
carol: 5/22/1992
supermim: 3/16/1992
carol: 2/16/1992
carol: 8/22/1990