ID   ECP_PANTR               Reviewed;         160 AA.
AC   P47780; Q9GJQ9;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 2.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Eosinophil cationic protein;
DE            Short=ECP;
DE            EC=3.1.27.-;
DE   AltName: Full=Ribonuclease 3;
DE            Short=RNase 3;
DE   Flags: Precursor;
GN   Name=RNASE3; Synonyms=ECP, RNS3;
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7663519; DOI=10.1038/ng0695-219;
RA   Rosenberg H.F., Dyer K.D., Tiffany H.L., Gonzalez M.;
RT   "Rapid evolution of a unique family of primate ribonuclease genes.";
RL   Nat. Genet. 10:219-223(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11102386; DOI=10.1093/genetics/156.4.1949;
RA   Zhang J., Rosenberg H.F.;
RT   "Sequence variation at two eosinophil-associated ribonuclease loci in
RT   humans.";
RL   Genetics 156:1949-1958(2000).
CC   -!- FUNCTION: Cytotoxin and helminthotoxin with low-efficiency ribonuclease
CC       activity. Possesses a wide variety of biological activities. Exhibits
CC       antibacterial activity (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with bacterial lipopolysaccharide (LPS) and
CC       lipoteichoic acid (LTA). In vitro interacts with phospholipid bilayers.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Note=Located in the
CC       matrix of eosinophil large specific granule, which are released
CC       following activation by an immune stimulus. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the pancreatic ribonuclease family.
CC       {ECO:0000305}.
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DR   EMBL; U24103; AAC50150.1; -; Genomic_DNA.
DR   EMBL; AF294027; AAG09050.1; -; Genomic_DNA.
DR   EMBL; AF294028; AAG09051.1; -; Genomic_DNA.
DR   PIR; I61899; I61899.
DR   AlphaFoldDB; P47780; -.
DR   BMRB; P47780; -.
DR   SMR; P47780; -.
DR   InParanoid; P47780; -.
DR   Proteomes; UP000002277; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0004540; F:ribonuclease activity; IBA:GO_Central.
DR   GO; GO:0006935; P:chemotaxis; IBA:GO_Central.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IBA:GO_Central.
DR   GO; GO:0002227; P:innate immune response in mucosa; IBA:GO_Central.
DR   Gene3D; 3.10.130.10; -; 1.
DR   InterPro; IPR001427; RNaseA.
DR   InterPro; IPR036816; RNaseA-like_dom_sf.
DR   InterPro; IPR023411; RNaseA_AS.
DR   InterPro; IPR023412; RNaseA_domain.
DR   PANTHER; PTHR11437; PTHR11437; 1.
DR   Pfam; PF00074; RnaseA; 1.
DR   PRINTS; PR00794; RIBONUCLEASE.
DR   SMART; SM00092; RNAse_Pc; 1.
DR   SUPFAM; SSF54076; SSF54076; 1.
DR   PROSITE; PS00127; RNASE_PANCREATIC; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Endonuclease; Glycoprotein; Hydrolase; Nitration; Nuclease;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000250"
FT   CHAIN           28..160
FT                   /note="Eosinophil cationic protein"
FT                   /id="PRO_0000030864"
FT   REGION          28..72
FT                   /note="Required for nearly all of the bactericidal
FT                   activities; partially involved in LPS-binding"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        42
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        155
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         65..69
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         60
FT                   /note="3'-nitrotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P12724"
FT   CARBOHYD        84
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        92
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        119
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        50..110
FT                   /evidence="ECO:0000250"
FT   DISULFID        64..123
FT                   /evidence="ECO:0000250"
FT   DISULFID        82..138
FT                   /evidence="ECO:0000250"
FT   DISULFID        89..98
FT                   /evidence="ECO:0000250"
FT   CONFLICT        124
FT                   /note="R -> G (in Ref. 1; AAC50150)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        158
FT                   /note="A -> T (in Ref. 1; AAC50150)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   160 AA;  18410 MW;  C6DFE69DEB63D131 CRC64;
     MVPKLFTSQI CLLLLLGLMG VEGSLHARPP QFTRAQWFAI QHISLNPPRC TIAMRVINNY
     RWRCKNQNTF LRTTFANVVN VCGNQSIRCP HNRTLNNCHQ SRFRVPLLHC DLINPGAQNI
     SNCRYADRPG RRFYVVACDN RDPRDSPRYP VVPVHLDATI