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ECP_RAT
ID   ECP_RAT                 Reviewed;         155 AA.
AC   P70709;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=Eosinophil cationic protein;
DE            Short=ECP;
DE            EC=3.1.27.-;
DE   AltName: Full=Eosinophil secondary granule ribonuclease 11;
DE            Short=EAR-11;
DE   AltName: Full=Ribonuclease 3;
DE            Short=RNase 3;
DE   Flags: Precursor;
GN   Name=Rnase3; Synonyms=Ear11, Rns3;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Bone marrow;
RX   PubMed=9116043; DOI=10.1016/s0167-4781(97)00024-9;
RA   Nittoh T., Hirakata M., Mue S., Ohuchi K.;
RT   "Identification of cDNA encoding rat eosinophil cationic
RT   protein/eosinophil-associated ribonuclease.";
RL   Biochim. Biophys. Acta 1351:42-46(1997).
CC   -!- FUNCTION: Cytotoxin and helminthotoxin with ribonuclease activity.
CC       Possesses a wide variety of biological activities (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic granule {ECO:0000250}. Note=Matrix of
CC       eosinophil's large specific granule. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the pancreatic ribonuclease family.
CC       {ECO:0000305}.
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DR   EMBL; D88586; BAA13648.1; -; mRNA.
DR   RefSeq; NP_620257.1; NM_138902.1.
DR   RefSeq; XP_002728238.1; XM_002728192.4.
DR   AlphaFoldDB; P70709; -.
DR   SMR; P70709; -.
DR   STRING; 10116.ENSRNOP00000044390; -.
DR   GlyGen; P70709; 2 sites.
DR   PaxDb; P70709; -.
DR   PRIDE; P70709; -.
DR   Ensembl; ENSRNOT00000105605; ENSRNOP00000076490; ENSRNOG00000068464.
DR   Ensembl; ENSRNOT00000119723; ENSRNOP00000084145; ENSRNOG00000064658.
DR   GeneID; 100361866; -.
DR   GeneID; 192264; -.
DR   KEGG; rno:100361866; -.
DR   KEGG; rno:192264; -.
DR   CTD; 6037; -.
DR   RGD; 621580; Rnase3.
DR   eggNOG; ENOG502TF52; Eukaryota.
DR   GeneTree; ENSGT00940000162253; -.
DR   HOGENOM; CLU_117006_0_1_1; -.
DR   InParanoid; P70709; -.
DR   OMA; PSCNIAM; -.
DR   OrthoDB; 1482425at2759; -.
DR   PhylomeDB; P70709; -.
DR   TreeFam; TF333393; -.
DR   Reactome; R-RNO-6798695; Neutrophil degranulation.
DR   PRO; PR:P70709; -.
DR   Proteomes; UP000002494; Chromosome 15.
DR   Bgee; ENSRNOG00000031445; Expressed in lung and 5 other tissues.
DR   ExpressionAtlas; P70709; baseline.
DR   Genevisible; P70709; RN.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0005615; C:extracellular space; ISO:RGD.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0001530; F:lipopolysaccharide binding; ISO:RGD.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0004540; F:ribonuclease activity; IBA:GO_Central.
DR   GO; GO:0019731; P:antibacterial humoral response; ISO:RGD.
DR   GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; ISO:RGD.
DR   GO; GO:0006935; P:chemotaxis; IBA:GO_Central.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; ISO:RGD.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; ISO:RGD.
DR   GO; GO:0043152; P:induction of bacterial agglutination; ISO:RGD.
DR   GO; GO:0045087; P:innate immune response; ISO:RGD.
DR   GO; GO:0002227; P:innate immune response in mucosa; ISO:RGD.
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   2: Evidence at transcript level;
KW   Disulfide bond; Endonuclease; Glycoprotein; Hydrolase; Nuclease;
KW   Reference proteome; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..155
FT                   /note="Eosinophil cationic protein"
FT                   /id="PRO_0000030866"
FT   ACT_SITE        38
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        150
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         62..66
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        88
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        107
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        47..106
FT                   /evidence="ECO:0000250"
FT   DISULFID        61..118
FT                   /evidence="ECO:0000250"
FT   DISULFID        79..133
FT                   /evidence="ECO:0000250"
FT   DISULFID        86..94
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   155 AA;  18007 MW;  F190864C34EA22C7 CRC64;
     MGLKLLESRL CLLLSLGLVL MLASCQPPTP SQWFEIQHIY NRAYPRCNDA MRHRNRFTGH
     CKDINTFLHT SFASVVGVCG NRNIPCGNRT YRNCHNSRYR VSITFCNLTT PARIYTQCRY
     QTTRSRKFYT VGCDPRTPRD SPMYPVVPVH LDRIF
 
 
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