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P12724 (ECP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 144. 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:
Eosinophil cationic protein

Short name=ECP
EC=3.1.27.-
Alternative name(s):
Ribonuclease 3
Short name=RNase 3
Gene names
Name:RNASE3
Synonyms:ECP, RNS3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length160 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cytotoxin and helminthotoxin with low-efficiency ribonuclease activity. Possesses a wide variety of biological activities. Exhibits antibacterial activity, including cytoplasmic membrane depolarization of preferentially Gram-negative, but also Gram-positive strains. Promotes E.coli outer membrane detachment, alteration of the overall cell shape and partial loss of cell content. Ref.10 Ref.12

Subunit structure

Interacts with bacterial lipopolysaccharide (LPS) and lipoteichoic acid (LTA). In vitro interacts with and insert into lipid bilayers composed of dioleoyl phosphatidylcholine and dioleoyl phosphatidylglycerol. In vitro, tends to form amyloid-like aggregates at pH 3, but not at pH 5, nor 7. Ref.12

Subcellular location

Secreted. Note: Located in the matrix of eosinophil large specific granule, which are released following activation by an immune stimulus.

Sequence similarities

Belongs to the pancreatic ribonuclease family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Ref.9 Ref.10
Chain28 – 160133Eosinophil cationic protein
PRO_0000030862

Regions

Region28 – 7245Required for nearly all of the bactericidal activity; partially involved in LPS-binding and bacterial membrane depolarization
Region65 – 695Substrate binding

Sites

Active site421Proton acceptor
Active site1551Proton donor
Site601May be involved in LPS-binding
Site621May be involved in LPS- and LTA-binding

Amino acid modifications

Modified residue601Nitrated tyrosine Ref.11
Glycosylation841N-linked (GlcNAc...) Potential
Glycosylation921N-linked (GlcNAc...) Potential
Glycosylation1191N-linked (GlcNAc...) Potential
Disulfide bond50 ↔ 110
Disulfide bond64 ↔ 123
Disulfide bond82 ↔ 138
Disulfide bond89 ↔ 98

Natural variations

Natural variant721R → C. Ref.8
Corresponds to variant rs151169198 [ dbSNP | Ensembl ].
VAR_014109
Natural variant1241T → R. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.7 Ref.8
Corresponds to variant rs2073342 [ dbSNP | Ensembl ].
VAR_013149
Natural variant1301G → R.
Corresponds to variant rs12147890 [ dbSNP | Ensembl ].
VAR_029017

Experimental info

Mutagenesis401I → A: Loss of in vitro formation of amyloid-like aggregates. Ref.13

Secondary structure

............................... 160
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P12724 [UniParc].

Last modified May 15, 2007. Version 2.
Checksum: D7BED24F67B23FA9

FASTA16018,385
        10         20         30         40         50         60 
MVPKLFTSQI CLLLLLGLMG VEGSLHARPP QFTRAQWFAI QHISLNPPRC TIAMRAINNY 

        70         80         90        100        110        120 
RWRCKNQNTF LRTTFANVVN VCGNQSIRCP HNRTLNNCHR SRFRVPLLHC DLINPGAQNI 

       130        140        150        160 
SNCTYADRPG RRFYVVACDN RDPRDSPRYP VVPVHLDTTI 

« Hide

References

« Hide 'large scale' references
[1]"Human eosinophil cationic protein. Molecular cloning of a cytotoxin and helminthotoxin with ribonuclease activity."
Rosenberg H.F., Ackerman S.J., Tenen D.G.
J. Exp. Med. 170:163-176(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ARG-124.
Tissue: Peripheral blood granulocyte.
[2]"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 [MRNA], VARIANT ARG-124.
Tissue: Fetal liver.
[3]"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 [GENOMIC DNA], VARIANT ARG-124.
[4]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], VARIANT ARG-124.
Tissue: Colon.
[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 ARG-124.
[6]"The DNA sequence and analysis of human chromosome 14."
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H. expand/collapse author list , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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], VARIANT ARG-124.
[8]"Identification of polymorphisms in the ECP gene. Relation to disease activity in Hodgkins lymphoma."
Bystrom J., Molin D., Jonsson U.B., Enblad G., Sundstrom C., Hogbom E., Venge P.
Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 20-160, VARIANTS CYS-72 AND ARG-124.
[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 28-87.
[10]"Antibiotic proteins of human polymorphonuclear leukocytes."
Gabay J.E., Scott R.W., Campanelli D., Griffith J., Wilde C., Marra M.N., Seeger M., Nathan C.F.
Proc. Natl. Acad. Sci. U.S.A. 86:5610-5614(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 28-47, FUNCTION AS AN ANTIMICROBIAL PROTEIN.
[11]"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.
[12]"Bactericidal and membrane disruption activities of the eosinophil cationic protein are largely retained in an N-terminal fragment."
Torrent M., de la Torre B.G., Nogues V.M., Andreu D., Boix E.
Biochem. J. 421:425-434(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH LPS; LTA AND LIPID BILAYERS.
[13]"Eosinophil cationic protein aggregation: identification of an N-terminus amyloid prone region."
Torrent M., Odorizzi F., Nogues M.V., Boix E.
Biomacromolecules 11:1983-1990(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IN VITRO FORMATION OF AMYLOID-LIKE AGGREGATES, MUTAGENESIS OF ILE-40.
[14]"Crystal structure of eosinophil cationic protein at 2.4 A resolution."
Boix E., Leonidas D.D., Nikolovski Z., Nogues M.V., Cuchillo C.M., Acharya K.R.
Biochemistry 38:16794-16801(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 28-160.
[15]"Three-dimensional crystal structure of human eosinophil cationic protein (RNase 3) at 1.75 A resolution."
Mallorqui-Fernandez G., Pous J., Peracaula R., Aymami J., Maeda T., Tada H., Yamada H., Seno M., de Llorens R., Gomis-Rueth F.-X., Coll M.
J. Mol. Biol. 300:1297-1307(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 28-160.
[16]"The crystal structure of eosinophil cationic protein in complex with 2',5'-ADP at 2.0 A resolution reveals the details of the ribonucleolytic active site."
Mohan C.G., Boix E., Evans H.R., Nikolovski Z., Nogues M.V., Cuchillo C.M., Acharya K.R.
Biochemistry 41:12100-12106(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 28-160.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X15161 mRNA. Translation: CAA33251.1.
M28128 mRNA. Translation: AAA50283.1.
X16545 Genomic DNA. Translation: CAA34545.1.
X55990 Genomic DNA. Translation: CAA39462.1.
AF294019 Genomic DNA. Translation: AAG31589.1.
AF294020 Genomic DNA. Translation: AAG31590.1.
AF294021 Genomic DNA. Translation: AAG31591.1.
AF294022 Genomic DNA. Translation: AAG31592.1.
AF294023 Genomic DNA. Translation: AAG31593.1.
AF294024 Genomic DNA. Translation: AAG31594.1.
AF294025 Genomic DNA. Translation: AAG31595.1.
AF294026 Genomic DNA. Translation: AAG31596.1.
AL133371 Genomic DNA. No translation available.
BC096060 mRNA. Translation: AAH96060.1.
BC096061 mRNA. Translation: AAH96061.1.
BC096062 mRNA. Translation: AAH96062.1.
AF441204 Genomic DNA. Translation: AAL35279.1.
AF441205 Genomic DNA. Translation: AAL35280.1.
AF441206 Genomic DNA. Translation: AAL35281.1.
PIRJL0106. B35328.
RefSeqNP_002926.2. NM_002935.2.
UniGeneHs.73839.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DYTX-ray1.75A/B28-160[»]
1H1HX-ray2.00A28-160[»]
1QMTX-ray2.40A27-160[»]
2KB5NMR-A28-160[»]
2LVZNMR-A28-160[»]
4A2OX-ray1.69A/B28-160[»]
4A2YX-ray1.70A/B28-160[»]
ProteinModelPortalP12724.
SMRP12724. Positions 28-160.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111966. 1 interaction.
STRING9606.ENSP00000302324.

Chemistry

DrugBankDB01411. Pranlukast.

PTM databases

PhosphoSiteP12724.

Polymorphism databases

DMDM147744558.

Proteomic databases

PaxDbP12724.
PRIDEP12724.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000304639; ENSP00000302324; ENSG00000169397.
GeneID6037.
KEGGhsa:6037.
UCSCuc001vyj.3. human.

Organism-specific databases

CTD6037.
GeneCardsGC14P021359.
H-InvDBHIX0037784.
HGNCHGNC:10046. RNASE3.
HPAHPA056183.
MIM131398. gene.
neXtProtNX_P12724.
PharmGKBPA34414.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG118739.
HOGENOMHOG000276882.
HOVERGENHBG008396.
InParanoidP12724.
KOK10787.
OMANISRNCH.
OrthoDBEOG7KDFCP.
PhylomeDBP12724.
TreeFamTF333393.

Gene expression databases

BgeeP12724.
CleanExHS_RNASE3.
GenevestigatorP12724.

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

EvolutionaryTraceP12724.
GeneWikiEosinophil_cationic_protein.
GenomeRNAi6037.
NextBio23529.
PROP12724.
SOURCESearch...

Entry information

Entry nameECP_HUMAN
AccessionPrimary (citable) accession number: P12724
Secondary accession number(s): Q4VBC1 expand/collapse secondary AC list , Q8WTP7, Q8WZ62, Q9GZN9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: May 15, 2007
Last modified: April 16, 2014
This is version 144 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