ECP_MACFA
ID ECP_MACFA Reviewed; 160 AA.
AC P47779;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=RNS3;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
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).
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; U24098; AAC50146.1; -; Genomic_DNA.
DR PIR; I61895; I61895.
DR AlphaFoldDB; P47779; -.
DR BMRB; P47779; -.
DR SMR; P47779; -.
DR STRING; 9541.XP_005560775.1; -.
DR PRIDE; P47779; -.
DR eggNOG; ENOG502TF52; Eukaryota.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0016070; P:RNA metabolic process; IEA:UniProt.
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_0000030863"
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 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"
SQ SEQUENCE 160 AA; 18620 MW; 80B78E4EB795EDA0 CRC64;
MVPKLFTSQI CLLLLLGLMG VEGSLHARPP QFTKAQWFAI QHINVNPPRC TIAMRVINNY
QRRCKNQNTF LRTTFAYTAN VCRNERIRCP RNRTLHNCHR SRYRVPLLHC DLINPGAQNI
STCRYADRPG RRFYVVACES RDPRDSPRYP VVPVHLDTTI
