AMPDB_154 | Eosinophil cationic protein
PEPTIDE SUMMARY
Eosinophil cationic protein
1 General Description
AMPDB ID: AMPDB_154
Protein Names: Eosinophil cationic protein (ECP) (EC 3.1.27.-) (Ribonuclease 3) (RNase 3)
Protein Family: Pancreatic ribonuclease family
Gene Name: RNASE3 ECP RNS3
Source Organism: Homo sapiens (Human)
Protein Length: 160 AA
Protein Existence: Evidence at protein level
2 Protein Sequence & Composition
2.1 Sequence
MVPKLFTSQICLLLLLGLMGVEGSLHARPPQFTRAQWFAIQHISLNPPRCTIAMRAINNYRWRCKNQNTFLRTTFANVVNVCGNQSIRCPHNRTLNNCHRSRFRVPLLHCDLINPGAQNISNCTYADRPGRRFYVVACDNRDPRDSPRYPVVPVHLDTTI
FASTA format
2.2 Composition
Counts of Amino Acids
'A': 9, 'R': 18, 'N': 15, 'D': 6, 'C': 9, 'Q': 7, 'E': 1, 'G': 6, 'H': 6, 'I': 9, 'L': 15, 'K': 2, 'M': 3, 'F': 7, 'P': 13, 'S': 7, 'T': 10, 'W': 2, 'Y': 4, 'V': 11
Frequencies of Amino Acids
'A': 5.63%, 'R': 11.25%, 'N': 9.38%, 'D': 3.75%, 'C': 5.63%, 'Q': 4.38%, 'E': 0.63%, 'G': 3.75%, 'H': 3.75%, 'I': 5.63%, 'L': 9.38%, 'K': 1.25%, 'M': 1.88%, 'F': 4.38%, 'P': 8.13%, 'S': 4.38%, 'T': 6.25%, 'W': 1.25%, 'Y': 2.5%, 'V': 6.88%
Missing Amino Acid(s)
No Amino Acid(s) are missing in this protein
Most Occurring Amino Acid(s)
R
Less Occurring Amino Acid(s)
E
Hydrophobic Amino Acid(s) Count
75
Hydrophilic Amino Acid(s) Count
85
Basic Amino Acid(s) Count
7
Acidic Amino Acid(s) Count
26
Modified Amino Acid(s) Count
0
Modified Amino Acid(s) Frequencies
0
Computed by biopython (version 1.79) & proteinAnalysis (version 1)
3 Physicochemical Properties
Sl. No. Properties Values Reference
1. Molecular Mass 18385.3 Da Computed by ProtParam module (biopython 1.79)
2. Aliphatic Index 84.063 Computed by ProtParam module (biopython 1.79)
3. Instability Index (Half Life) 59.056 Computed by ProtParam module (biopython 1.79)
4. Hydrophobicity (GRAVY) -0.279 Computed by ProtParam module (biopython 1.79)
5. Hydrophobic Moment 0.732 Computed by ProtParam module (biopython 1.79)
6. Isoelectric Point 10.332 Computed by ProtParam module (biopython 1.79)
7. Charge (at pH 7) 12.986 Computed by ProtParam module (biopython 1.79)
8. Secondary Structure Fraction 0.3, 0.256, 0.175 [Helix, Turn, Sheet] Computed by ProtParam module (biopython 1.79)
9. Aromaticity 0.081 Computed by ProtParam module (biopython 1.79)
10. Molar Extinction Coefficient (cysteine|cystine) 16960, 17460 Computed by ProtParam module (biopython 1.79)
4 Activity Details
4.1 Target Organism(s)
E.coli (Gram-negative)
4.2 Antimicrobial Activity
Antibiotic, Antimicrobial, Anti-gram-negative
4.3 Enzymatic Activity
Endonuclease, Hydrolase, Nuclease
4.4 Inhibitory Effect
Not found
4.5 Other Biological Activity
Cytotoxin, Non-hemolytic, Non-ribosomal
Activity data manually curated from Literature and UniProt
5 Database Cross-references
5.1 Literature Database
5.1.1 PubMed
Citation 1: Rosenberg HF, Ackerman SJ, Tenen DG, et al. Human eosinophil cationic protein. Molecular cloning of a cytotoxin and helminthotoxin with ribonuclease activity. J Exp Med. 1989;170(1):163-76. Published 1989 Jul 1. doi:10.1084/jem.170.1.163
PMID: 2473157
Citation 2: Hamann KJ, Ten RM, Loegering DA, et al. 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. 1990;7(4):535-46. Published 1990 Aug. doi:10.1016/0888-7543(90)90197-3
PMID: 2387583
Citation 3: Barker RL, Loegering DA, Ten RM, et al. Eosinophil cationic protein cDNA. Comparison with other toxic cationic proteins and ribonucleases. J Immunol. 1989;143(3):952-5. Published 1989 Aug 1. doi:
PMID: 2745977
Citation 4: Zhang J, Rosenberg HF, Rosenberg HF. Sequence variation at two eosinophil-associated ribonuclease loci in humans. Genetics. 2000;156(4):1949-58. Published 2000 Dec. doi:10.1093/genetics/156.4.1949
PMID: 11102386
Citation 5: Heilig R, Eckenberg R, Petit JL, et al. The DNA sequence and analysis of human chromosome 14. Nature. 2003;421(6923):601-7. Published 2003 Feb 6. doi:10.1038/nature01348
PMID: 12508121
Citation 6: Gerhard DS, Wagner L, Feingold EA, et al. The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004;14(10B):2121-7. Published 2004 Oct. doi:10.1101/gr.2596504
PMID: 15489334
Citation 7: Gleich GJ, Loegering DA, Bell MP, et al. Biochemical and functional similarities between human eosinophil-derived neurotoxin and eosinophil cationic protein: homology with ribonuclease. Proc Natl Acad Sci U S A. 1986;83(10):3146-50. Published 1986 May. doi:10.1073/pnas.83.10.3146
PMID: 3458170
Citation 8: Gabay JE, Scott RW, Campanelli D, et al. Antibiotic proteins of human polymorphonuclear leukocytes. Proc Natl Acad Sci U S A. 1989;86(14):5610-4. Published 1989 Jul. doi:10.1073/pnas.86.14.5610
PMID: 2501794
Citation 9: Ulrich M, Petre A, Youhnovski N, et al. Post-translational tyrosine nitration of eosinophil granule toxins mediated by eosinophil peroxidase. J Biol Chem. 2008;283(42):28629-40. Published 2008 Oct 17. doi:10.1074/jbc.M801196200
PMID: 18694936
Citation 10: Torrent M, de la Torre BG, Nogués VM, et al. Bactericidal and membrane disruption activities of the eosinophil cationic protein are largely retained in an N-terminal fragment. Biochem J. 2009;421(3):425-34. Published 2009 Jul 15. doi:10.1042/BJ20082330
PMID: 19450231
Citation 11: Torrent M, Odorizzi F, Nogués MV, et al. Eosinophil cationic protein aggregation: identification of an N-terminus amyloid prone region. Biomacromolecules. 2010;11(8):1983-90. Published 2010 Aug 9. doi:10.1021/bm100334u
PMID: 20690710
Citation 12: Vaca Jacome AS, Rabilloud T, Schaeffer-Reiss C, et al. N-terminome analysis of the human mitochondrial proteome. Proteomics. 2015;15(14):2519-24. Published 2015 Jul. doi:10.1002/pmic.201400617
PMID: 25944712
Citation 13: Boix E, Leonidas DD, Nikolovski Z, et al. Crystal structure of eosinophil cationic protein at 2.4 A resolution. Biochemistry. 1999;38(51):16794-801. Published 1999 Dec 21. doi:10.1021/bi9919145
PMID: 10606511
Citation 14: Mallorquí-Fernández G, Pous J, Peracaula R, et al. Three-dimensional crystal structure of human eosinophil cationic protein (RNase 3) at 1.75 A resolution. J Mol Biol. 2000;300(5):1297-307. Published 2000 Jul 28. doi:10.1006/jmbi.2000.3939
PMID: 10903870
Citation 15: Mohan CG, Boix E, Evans HR, et al. 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. Biochemistry. 2002;41(40):12100-6. Published 2002 Oct 8. doi:10.1021/bi0264521
PMID: 12356310
5.2 Protein Sequence Databases
UniProt: P12724
5.3 3D Structure Databases
Sl. no. PDB ID Method Resolution Access Links 3D View
AlphaFoldDB: P12724
5.4 Nucleotide Sequence Databases
Sl. no. Accession(s) Access Link(s)
1. X15161 GenBank || EMBL
2. M28128 GenBank || EMBL
3. X16545 GenBank || EMBL
4. X55990 GenBank || EMBL
5. AF294019 GenBank || EMBL
6. AF294020 GenBank || EMBL
7. AF294021 GenBank || EMBL
8. AF294022 GenBank || EMBL
9. AF294023 GenBank || EMBL
10. AF294024 GenBank || EMBL
11. AF294025 GenBank || EMBL
12. AF294026 GenBank || EMBL
13. AL133371 GenBank || EMBL
14. BC096060 GenBank || EMBL
15. BC096061 GenBank || EMBL
16. BC096062 GenBank || EMBL
17. AF441204 GenBank || EMBL
18. AF441205 GenBank || EMBL
19. AF441206 GenBank || EMBL
CCDS: CCDS9560.1
RefSeq: NP_002926.2
5.5 Protein-Protein Interaction Databases
STRING: 9606.ENSP00000302324
IntAct: P12724
MINT: Not found
DIP: Not found
BioGRID: 111966
5.6 Ligand Databases
BindingDB: Not found
DrugBank: DB02098, DB04272, DB01411
ChEMBL: Not found
5.7 Family & Domain Databases
InterPro: IPR001427, IPR036816, IPR023411, IPR023412
PANTHER: PTHR11437
PROSITE: PS00127
5.8 Genome Annotation Databases
Ensembl: ENSGT00940000162253
KEGG: hsa:6037
5.9 Phylogenomic Databases
GeneTree: ENSGT00940000162253
5.10 Enzyme & Pathway Databases
BRENDA: Not found
BioCyc: Not found
5.11 Protein-RNA Interaction Databases
RNAct: P12724




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