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P12724

- ECP_HUMAN

UniProt

P12724 - ECP_HUMAN

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Protein
Eosinophil cationic protein
Gene
RNASE3, ECP, RNS3
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei42 – 421Proton acceptor
Sitei60 – 601May be involved in LPS-binding
Sitei62 – 621May be involved in LPS- and LTA-binding
Active sitei155 – 1551Proton donor

GO - Molecular functioni

  1. endoribonuclease activity, producing 3'-phosphomonoesters Source: InterPro
  2. nucleic acid binding Source: InterPro
  3. ribonuclease activity Source: ProtInc
Complete GO annotation...

GO - Biological processi

  1. RNA catabolic process Source: ProtInc
  2. RNA phosphodiester bond hydrolysis Source: GOC
  3. antibacterial humoral response Source: UniProt
  4. defense response to Gram-positive bacterium Source: UniProt
  5. innate immune response in mucosa Source: UniProt
Complete GO annotation...

Keywords - Molecular functioni

Antibiotic, Antimicrobial, Endonuclease, Hydrolase, Nuclease

Names & Taxonomyi

Protein namesi
Recommended name:
Eosinophil cationic protein (EC:3.1.27.-)
Short name:
ECP
Alternative name(s):
Ribonuclease 3
Short name:
RNase 3
Gene namesi
Name:RNASE3
Synonyms:ECP, RNS3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:10046. RNASE3.

Subcellular locationi

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

GO - Cellular componenti

  1. extracellular region Source: ProtInc
  2. extracellular space Source: UniProt
  3. extracellular vesicular exosome Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi40 – 401I → A: Loss of in vitro formation of amyloid-like aggregates. 1 Publication

Organism-specific databases

PharmGKBiPA34414.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 27272 Publications
Add
BLAST
Chaini28 – 160133Eosinophil cationic protein
PRO_0000030862Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi50 ↔ 110
Modified residuei60 – 601Nitrated tyrosine1 Publication
Disulfide bondi64 ↔ 123
Disulfide bondi82 ↔ 138
Glycosylationi84 – 841N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi89 ↔ 98
Glycosylationi92 – 921N-linked (GlcNAc...) Reviewed prediction
Glycosylationi119 – 1191N-linked (GlcNAc...) Reviewed prediction

Keywords - PTMi

Disulfide bond, Glycoprotein, Nitration

Proteomic databases

PaxDbiP12724.
PRIDEiP12724.

PTM databases

PhosphoSiteiP12724.

Expressioni

Gene expression databases

BgeeiP12724.
CleanExiHS_RNASE3.
GenevestigatoriP12724.

Organism-specific databases

HPAiHPA056183.

Interactioni

Subunit structurei

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 7.1 Publication

Protein-protein interaction databases

BioGridi111966. 1 interaction.
STRINGi9606.ENSP00000302324.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi30 – 323
Helixi34 – 429
Helixi50 – 534
Helixi55 – 584
Beta strandi61 – 633
Beta strandi66 – 738
Helixi75 – 817
Turni93 – 953
Beta strandi98 – 1003
Beta strandi105 – 1139
Helixi120 – 1223
Beta strandi125 – 1328
Beta strandi134 – 1407
Turni143 – 1453
Beta strandi150 – 15910

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DYTX-ray1.75A/B28-160[»]
1H1HX-ray2.00A28-160[»]
1QMTX-ray2.40A28-160[»]
2KB5NMR-A28-160[»]
2LVZNMR-A28-160[»]
4A2OX-ray1.69A/B28-160[»]
4A2YX-ray1.70A/B28-160[»]
ProteinModelPortaliP12724.
SMRiP12724. Positions 28-160.

Miscellaneous databases

EvolutionaryTraceiP12724.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni28 – 7245Required for nearly all of the bactericidal activity; partially involved in LPS-binding and bacterial membrane depolarization
Add
BLAST
Regioni65 – 695Substrate binding

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG118739.
HOGENOMiHOG000276882.
HOVERGENiHBG008396.
InParanoidiP12724.
KOiK10787.
OMAiNISRNCH.
OrthoDBiEOG7KDFCP.
PhylomeDBiP12724.
TreeFamiTF333393.

Family and domain databases

Gene3Di3.10.130.10. 1 hit.
InterProiIPR001427. RNaseA.
IPR023411. RNaseA_AS.
IPR023412. RNaseA_domain.
[Graphical view]
PANTHERiPTHR11437. PTHR11437. 1 hit.
PfamiPF00074. RnaseA. 1 hit.
[Graphical view]
PRINTSiPR00794. RIBONUCLEASE.
ProDomiPD000535. RNaseA. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00092. RNAse_Pc. 1 hit.
[Graphical view]
SUPFAMiSSF54076. SSF54076. 1 hit.
PROSITEiPS00127. RNASE_PANCREATIC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P12724-1 [UniParc]FASTAAdd to Basket

« Hide

MVPKLFTSQI CLLLLLGLMG VEGSLHARPP QFTRAQWFAI QHISLNPPRC    50
TIAMRAINNY RWRCKNQNTF LRTTFANVVN VCGNQSIRCP HNRTLNNCHR 100
SRFRVPLLHC DLINPGAQNI SNCTYADRPG RRFYVVACDN RDPRDSPRYP 150
VVPVHLDTTI 160
Length:160
Mass (Da):18,385
Last modified:May 15, 2007 - v2
Checksum:iD7BED24F67B23FA9
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti72 – 721R → C.1 Publication
Corresponds to variant rs151169198 [ dbSNP | Ensembl ].
VAR_014109
Natural varianti124 – 1241T → R.7 Publications
Corresponds to variant rs2073342 [ dbSNP | Ensembl ].
VAR_013149
Natural varianti130 – 1301G → R.
Corresponds to variant rs12147890 [ dbSNP | Ensembl ].
VAR_029017

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS9560.1.
PIRiB35328. JL0106.
RefSeqiNP_002926.2. NM_002935.2.
UniGeneiHs.73839.

Genome annotation databases

EnsembliENST00000304639; ENSP00000302324; ENSG00000169397.
GeneIDi6037.
KEGGihsa:6037.
UCSCiuc001vyj.3. human.

Polymorphism databases

DMDMi147744558.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS9560.1.
PIRi B35328. JL0106.
RefSeqi NP_002926.2. NM_002935.2.
UniGenei Hs.73839.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1DYT X-ray 1.75 A/B 28-160 [» ]
1H1H X-ray 2.00 A 28-160 [» ]
1QMT X-ray 2.40 A 28-160 [» ]
2KB5 NMR - A 28-160 [» ]
2LVZ NMR - A 28-160 [» ]
4A2O X-ray 1.69 A/B 28-160 [» ]
4A2Y X-ray 1.70 A/B 28-160 [» ]
ProteinModelPortali P12724.
SMRi P12724. Positions 28-160.
ModBasei Search...

Protein-protein interaction databases

BioGridi 111966. 1 interaction.
STRINGi 9606.ENSP00000302324.

Chemistry

DrugBanki DB01411. Pranlukast.

PTM databases

PhosphoSitei P12724.

Polymorphism databases

DMDMi 147744558.

Proteomic databases

PaxDbi P12724.
PRIDEi P12724.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000304639 ; ENSP00000302324 ; ENSG00000169397 .
GeneIDi 6037.
KEGGi hsa:6037.
UCSCi uc001vyj.3. human.

Organism-specific databases

CTDi 6037.
GeneCardsi GC14P021359.
H-InvDB HIX0037784.
HGNCi HGNC:10046. RNASE3.
HPAi HPA056183.
MIMi 131398. gene.
neXtProti NX_P12724.
PharmGKBi PA34414.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG118739.
HOGENOMi HOG000276882.
HOVERGENi HBG008396.
InParanoidi P12724.
KOi K10787.
OMAi NISRNCH.
OrthoDBi EOG7KDFCP.
PhylomeDBi P12724.
TreeFami TF333393.

Miscellaneous databases

EvolutionaryTracei P12724.
GeneWikii Eosinophil_cationic_protein.
GenomeRNAii 6037.
NextBioi 23529.
PROi P12724.
SOURCEi Search...

Gene expression databases

Bgeei P12724.
CleanExi HS_RNASE3.
Genevestigatori P12724.

Family and domain databases

Gene3Di 3.10.130.10. 1 hit.
InterProi IPR001427. RNaseA.
IPR023411. RNaseA_AS.
IPR023412. RNaseA_domain.
[Graphical view ]
PANTHERi PTHR11437. PTHR11437. 1 hit.
Pfami PF00074. RnaseA. 1 hit.
[Graphical view ]
PRINTSi PR00794. RIBONUCLEASE.
ProDomi PD000535. RNaseA. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SMARTi SM00092. RNAse_Pc. 1 hit.
[Graphical view ]
SUPFAMi SSF54076. SSF54076. 1 hit.
PROSITEi PS00127. RNASE_PANCREATIC. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: PROTEIN SEQUENCE OF 28-47, FUNCTION AS AN ANTIMICROBIAL PROTEIN.
  11. 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.

Entry informationi

Entry nameiECP_HUMAN
AccessioniPrimary (citable) accession number: P12724
Secondary accession number(s): Q4VBC1
, Q8WTP7, Q8WZ62, Q9GZN9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: May 15, 2007
Last modified: September 3, 2014
This is version 147 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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