ECP1_MOUSE
ID ECP1_MOUSE Reviewed; 155 AA.
AC P97426;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Eosinophil cationic protein 1;
DE Short=ECP 1;
DE EC=3.1.27.-;
DE AltName: Full=Eosinophil secondary granule ribonuclease 1;
DE Short=EAR-1;
DE AltName: Full=Ribonuclease 3-1;
DE Short=RNase 3-1;
DE Flags: Precursor;
GN Name=Ear1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=8901588; DOI=10.1073/pnas.93.22.12370;
RA Larson K.A., Olson E.V., Madden B.J., Gleich G.J., Lee N.A., Lee J.J.;
RT "Two highly homologous ribonuclease genes expressed in mouse eosinophils
RT identify a larger subgroup of the mammalian ribonuclease superfamily.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:12370-12375(1996).
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; U72032; AAB37786.1; -; mRNA.
DR CCDS; CCDS26964.1; -.
DR PIR; JC6159; JC6159.
DR RefSeq; NP_031920.1; NM_007894.2.
DR AlphaFoldDB; P97426; -.
DR SMR; P97426; -.
DR STRING; 10090.ENSMUSP00000098256; -.
DR GlyGen; P97426; 4 sites.
DR PhosphoSitePlus; P97426; -.
DR PaxDb; P97426; -.
DR PRIDE; P97426; -.
DR ProteomicsDB; 277542; -.
DR DNASU; 13586; -.
DR Ensembl; ENSMUST00000100691; ENSMUSP00000098256; ENSMUSG00000072601.
DR Ensembl; ENSMUST00000179200; ENSMUSP00000136385; ENSMUSG00000072601.
DR GeneID; 13586; -.
DR KEGG; mmu:13586; -.
DR UCSC; uc007tdd.2; mouse.
DR CTD; 13586; -.
DR MGI; MGI:108021; Ear1.
DR VEuPathDB; HostDB:ENSMUSG00000072601; -.
DR eggNOG; ENOG502TF52; Eukaryota.
DR GeneTree; ENSGT00940000162253; -.
DR HOGENOM; CLU_117006_0_1_1; -.
DR InParanoid; P97426; -.
DR OMA; KSECKAS; -.
DR OrthoDB; 1482425at2759; -.
DR PhylomeDB; P97426; -.
DR TreeFam; TF333393; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 13586; 4 hits in 38 CRISPR screens.
DR PRO; PR:P97426; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; P97426; protein.
DR Bgee; ENSMUSG00000072601; Expressed in right lung lobe and 56 other tissues.
DR ExpressionAtlas; P97426; baseline and differential.
DR Genevisible; P97426; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
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; ISO:MGI.
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 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 1"
FT /id="PRO_0000030867"
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 33
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 62..66
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 41
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 114
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; 17296 MW; F8264E7A32B20D87 CRC64;
MGPKLLESRL CLLLLLGLVL MLASCLGQTP SQKFAIQHIN NNTNLQCNVE MMRINRARRT
CKGLNTFLHT SFANAVGVCG NPSGLCSDKR SQNCHNSSSR VHITVCNITS RATNYTQCRY
QSRRSLEYYT VACDPRTPQD SPMYPVVPVH LDGTF
