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Protein

Eosinophil cationic protein

Gene

RNASE3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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)DescriptionActionsGraphical viewLength
Active sitei42Proton acceptor1
Sitei60May be involved in LPS-binding1
Sitei62May be involved in LPS- and LTA-binding1
Active sitei155Proton donor1

GO - Molecular functioni

  • endonuclease activity Source: GO_Central
  • lipopolysaccharide binding Source: UniProtKB
  • nucleic acid binding Source: InterPro
  • ribonuclease activity Source: ProtInc

GO - Biological processi

Keywordsi

Molecular functionAntibiotic, Antimicrobial, Endonuclease, Hydrolase, Nuclease

Enzyme and pathway databases

ReactomeiR-HSA-6798695 Neutrophil degranulation
R-HSA-6803157 Antimicrobial peptides

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
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

EuPathDBiHostDB:ENSG00000169397.3
HGNCiHGNC:10046 RNASE3
MIMi131398 gene
neXtProtiNX_P12724

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi40I → A: Loss of in vitro formation of amyloid-like aggregates. 1 Publication1

Organism-specific databases

DisGeNETi6037
OpenTargetsiENSG00000169397
PharmGKBiPA34414

Chemistry databases

DrugBankiDB02098 Adenosine-2'-5'-Diphosphate
DB04272 Citric Acid
DB01411 Pranlukast

Polymorphism and mutation databases

BioMutaiRNASE3
DMDMi147744558

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 272 PublicationsAdd BLAST27
ChainiPRO_000003086228 – 160Eosinophil cationic proteinAdd BLAST133

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi50 ↔ 110
Modified residuei60Nitrated tyrosine1 Publication1
Disulfide bondi64 ↔ 123
Disulfide bondi82 ↔ 138
Glycosylationi84N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi89 ↔ 98
Glycosylationi92N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi119N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein, Nitration

Proteomic databases

EPDiP12724
PaxDbiP12724
PeptideAtlasiP12724
PRIDEiP12724
ProteomicsDBi52864

PTM databases

iPTMnetiP12724
PhosphoSitePlusiP12724

Expressioni

Gene expression databases

BgeeiENSG00000169397 Expressed in 85 organ(s), highest expression level in bone marrow
CleanExiHS_RNASE3
GenevisibleiP12724 HS

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, 14 interactors
STRINGi9606.ENSP00000302324

Structurei

Secondary structure

1160
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP12724
SMRiP12724
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP12724

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni28 – 72Required for nearly all of the bactericidal activity; partially involved in LPS-binding and bacterial membrane depolarizationAdd BLAST45
Regioni65 – 69Substrate binding5

Sequence similaritiesi

Belongs to the pancreatic ribonuclease family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410JDT3 Eukaryota
ENOG411136R LUCA
GeneTreeiENSGT00900000140993
HOGENOMiHOG000276882
HOVERGENiHBG008396
InParanoidiP12724
KOiK10787
OMAiNQSIRCP
OrthoDBiEOG091G0SFK
PhylomeDBiP12724
TreeFamiTF333393

Family and domain databases

Gene3Di3.10.130.10, 1 hit
InterProiView protein in InterPro
IPR001427 RNaseA
IPR036816 RNaseA-like_dom_sf
IPR023411 RNaseA_AS
IPR023412 RNaseA_domain
PANTHERiPTHR11437 PTHR11437, 1 hit
PfamiView protein in Pfam
PF00074 RnaseA, 1 hit
PRINTSiPR00794 RIBONUCLEASE
ProDomiView protein in ProDom or Entries sharing at least one domain
PD000535 RNaseA, 1 hit
SMARTiView protein in SMART
SM00092 RNAse_Pc, 1 hit
SUPFAMiSSF54076 SSF54076, 1 hit
PROSITEiView protein in PROSITE
PS00127 RNASE_PANCREATIC, 1 hit

Sequencei

Sequence statusi: Complete.

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

P12724-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MVPKLFTSQI CLLLLLGLMG VEGSLHARPP QFTRAQWFAI QHISLNPPRC
60 70 80 90 100
TIAMRAINNY RWRCKNQNTF LRTTFANVVN VCGNQSIRCP HNRTLNNCHR
110 120 130 140 150
SRFRVPLLHC DLINPGAQNI SNCTYADRPG RRFYVVACDN RDPRDSPRYP
160
VVPVHLDTTI
Length:160
Mass (Da):18,385
Last modified:May 15, 2007 - v2
Checksum:iD7BED24F67B23FA9
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01410972R → C1 PublicationCorresponds to variant dbSNP:rs151169198Ensembl.1
Natural variantiVAR_013149124T → R7 PublicationsCorresponds to variant dbSNP:rs2073342Ensembl.1
Natural variantiVAR_029017130G → R. Corresponds to variant dbSNP:rs12147890Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.4 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiECP_HUMAN
AccessioniPrimary (citable) accession number: P12724
Secondary accession number(s): Q4VBC1
, Q8WTP7, Q8WZ62, Q9GZN9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: May 15, 2007
Last modified: September 12, 2018
This is version 180 of the entry and version 2 of the sequence. See 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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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