RNASE3

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 key	Position(s)	DescriptionActions	Length
Active siteⁱ	42	Proton acceptor	1
Siteⁱ	60	May be involved in LPS-binding	1
Siteⁱ	62	May be involved in LPS- and LTA-binding	1
Active siteⁱ	155	Proton donor	1

GO - Molecular functionⁱ

endonuclease activity Source: GO_Central
lipopolysaccharide binding
Source: UniProtKB
Inferred from direct assayⁱ
- 23992292
nucleic acid binding Source: InterPro
ribonuclease activity
Source: ProtInc
Traceable author statementⁱ
- 2745977

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

antibacterial humoral response
Source: UniProtKB
Inferred from direct assayⁱ
- 12860195
antimicrobial humoral immune response mediated by antimicrobial peptide
Source: UniProtKB
Inferred from direct assayⁱ
- 12860195
antimicrobial humoral response Source: Reactome
defense response to Gram-negative bacterium
Source: UniProtKB
Inferred from direct assayⁱ
- 23992292
defense response to Gram-positive bacterium
Source: UniProtKB
Inferred from direct assayⁱ
- 12860195
- 23992292
induction of bacterial agglutination
Source: UniProtKB
Inferred from direct assayⁱ
- 23992292
innate immune response
Source: UniProtKB
Inferred from direct assayⁱ
- 23992292
innate immune response in mucosa
Source: UniProtKB
Inferred from direct assayⁱ
- 12860195
neutrophil degranulation Source: Reactome
RNA catabolic process
Source: ProtInc
Traceable author statementⁱ
- 2745977

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Antibiotic, Antimicrobial, Endonuclease, Hydrolase, Nuclease

Molecular function

Antibiotic, Antimicrobial, Endonuclease, Hydrolase, Nuclease

Enzyme and pathway databases

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

Reactomeⁱ

R-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
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 14

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000169397.3
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:10046 RNASE3
MIMⁱ	131398 gene
neXtProtⁱ	NX_P12724

Keywords - Cellular componentⁱ

Secreted

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Mutagenesisⁱ	40	I → A: Loss of in vitro formation of amyloid-like aggregates. 1 Publication		1

Organism-specific databases

DisGeNET More...DisGeNETⁱ	6037
Open Targets More...OpenTargetsⁱ	ENSG00000169397
PharmGKBⁱ	PA34414

Chemistry databases

Drug and drug target database More...DrugBankⁱ	DB02098 Adenosine-2'-5'-Diphosphate DB04272 Citric Acid DB01411 Pranlukast

DrugBankⁱ

DB02098 Adenosine-2'-5'-Diphosphate
DB04272 Citric Acid
DB01411 Pranlukast

Polymorphism and mutation databases

BioMutaⁱ	RNASE3
DMDMⁱ	147744558

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Signal peptideⁱ	1 – 27	2 PublicationsAdd BLAST		27
ChainⁱPRO_0000030862	28 – 160	Eosinophil cationic proteinAdd BLAST		133

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Disulfide bondⁱ	50 ↔ 110
Modified residueⁱ	60	Nitrated tyrosine1 Publication	1
Disulfide bondⁱ	64 ↔ 123
Disulfide bondⁱ	82 ↔ 138
Glycosylationⁱ	84	N-linked (GlcNAc...) asparagineSequence analysis	1
Disulfide bondⁱ	89 ↔ 98
Glycosylationⁱ	92	N-linked (GlcNAc...) asparagineSequence analysis	1
Glycosylationⁱ	119	N-linked (GlcNAc...) asparagineSequence analysis	1

Keywords - PTMⁱ

Disulfide bond, Glycoprotein, Nitration

Proteomic databases

EPDⁱ	P12724
PaxDbⁱ	P12724
PeptideAtlas More...PeptideAtlasⁱ	P12724
PRIDEⁱ	P12724
ProteomicsDBⁱ	52864

PTM databases

iPTMnetⁱ	P12724
PhosphoSitePlusⁱ	P12724

Expressionⁱ

Gene expression databases

Bgeeⁱ	ENSG00000169397 Expressed in 85 organ(s), highest expression level in bone marrow
CleanExⁱ	HS_RNASE3
Genevisibleⁱ	P12724 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	HPA056183

HPAⁱ

HPA056183

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

BioGridⁱ	111966, 14 interactors
STRINGⁱ	9606.ENSP00000302324

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	30 – 32	Combined sources	3
Helixⁱ	34 – 42	Combined sources	9
Helixⁱ	50 – 53	Combined sources	4
Helixⁱ	55 – 58	Combined sources	4
Beta strandⁱ	61 – 63	Combined sources	3
Beta strandⁱ	66 – 73	Combined sources	8
Helixⁱ	75 – 81	Combined sources	7
Beta strandⁱ	90 – 92	Combined sources	3
Turnⁱ	93 – 95	Combined sources	3
Beta strandⁱ	98 – 100	Combined sources	3
Beta strandⁱ	105 – 113	Combined sources	9
Helixⁱ	120 – 122	Combined sources	3
Beta strandⁱ	125 – 132	Combined sources	8
Beta strandⁱ	134 – 140	Combined sources	7
Turnⁱ	143 – 145	Combined sources	3
Beta strandⁱ	150 – 159	Combined sources	10

Show more details

3D structure databases

ProteinModelPortalⁱ	P12724
SMRⁱ	P12724
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P12724

EvolutionaryTraceⁱ

P12724

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	28 – 72	Required for nearly all of the bactericidal activity; partially involved in LPS-binding and bacterial membrane depolarizationAdd BLAST		45
Regionⁱ	65 – 69	Substrate binding		5

Sequence similaritiesⁱ

Belongs to the pancreatic ribonuclease family.Curated

Keywords - Domainⁱ

Signal

Phylogenomic databases

eggNOGⁱ	ENOG410JDT3 Eukaryota ENOG411136R LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00900000140993
HOGENOMⁱ	HOG000276882
HOVERGENⁱ	HBG008396
InParanoidⁱ	P12724
KEGG Orthology (KO) More...KOⁱ	K10787
OMAⁱ	NQSIRCP
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G0SFK
PhylomeDBⁱ	P12724
TreeFamⁱ	TF333393

Family and domain databases

Gene3Dⁱ	3.10.130.10, 1 hit
InterProⁱ	View protein in InterPro IPR001427 RNaseA IPR036816 RNaseA-like_dom_sf IPR023411 RNaseA_AS IPR023412 RNaseA_domain
PANTHERⁱ	PTHR11437 PTHR11437, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00074 RnaseA, 1 hit
PRINTSⁱ	PR00794 RIBONUCLEASE
ProDomⁱ	View protein in ProDom or Entries sharing at least one domain PD000535 RNaseA, 1 hit
SMARTⁱ	View protein in SMART SM00092 RNAse_Pc, 1 hit
SUPFAMⁱ	SSF54076 SSF54076, 1 hit
PROSITEⁱ	View 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]FASTA Add 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 key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_014109	72	R → C1 PublicationCorresponds to variant dbSNP:rs151169198Ensembl.	1
Natural variantⁱVAR_013149	124	T → R7 PublicationsCorresponds to variant dbSNP:rs2073342Ensembl.	1
Natural variantⁱVAR_029017	130	G → 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
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS9560.1
PIRⁱ	B35328 JL0106
NCBI Reference Sequences More...RefSeqⁱ	NP_002926.2, NM_002935.2
UniGeneⁱ	Hs.73839

Genome annotation databases

Ensemblⁱ	ENST00000304639; ENSP00000302324; ENSG00000169397
GeneIDⁱ	6037
KEGGⁱ	hsa:6037
UCSC genome browser More...UCSCⁱ	uc001vyj.4 human

Keywords - Coding sequence diversityⁱ

Polymorphism

Similar proteinsⁱ

90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P12724	Eosinophil cationic protein		GORGO		160	UniRef90_P12724
Eosinophil cationic protein		PANTR		160
Eosinophil cationic protein		western gorilla		160
Ribonuclease A F1		HUMAN		160
UPI0000044D0E		HUMAN		133
+3

Protein	Similar proteins		Species	Score	Length	Source
P12724	Eosinophil cationic protein		PANTR		160	UniRef50_P12724
Eosinophil cationic protein		GORGO		160
Eosinophil cationic protein		PONPY		160
Non-secretory ribonuclease	)	HUMAN		161
Non-secretory ribonuclease		NOMLE		161
+75

Entry informationⁱ

Entry nameⁱ	ECP_HUMAN
Accessionⁱ	P12724Primary (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 12, 2018
	This is version 180 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any 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

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P12724 (ECP_HUMAN)

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Eosinophil cationic protein

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted

Extracellular region or secreted

Lysosome

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Organism-specific databases

Chemistry databases

Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Natural variant

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Keywords - Coding sequence diversityⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ