ECP2_MOUSE
ID ECP2_MOUSE Reviewed; 156 AA.
AC P97425; Q505C0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Eosinophil cationic protein 2;
DE Short=ECP 2;
DE EC=3.1.27.-;
DE AltName: Full=Eosinophil secondary granule ribonuclease 2;
DE Short=EAR-2;
DE AltName: Full=Ribonuclease 3-2;
DE Short=RNase 3-2;
DE Flags: Precursor;
GN Name=Ear2; Synonyms=Rnase2;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=11311552; DOI=10.1016/s0378-1119(01)00392-4;
RA McDevitt A.L., Deming M.S., Rosenberg H.F., Dyer K.D.;
RT "Gene structure and enzymatic activity of mouse eosinophil-associated
RT ribonuclease 2.";
RL Gene 267:23-30(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP INVOLVEMENT IN CHEMOTAXIS.
RX PubMed=12855582; DOI=10.1182/blood-2003-01-0151;
RA Yang D., Rosenberg H.F., Chen Q., Dyer K.D., Kurosaka K., Oppenheim J.J.;
RT "Eosinophil-derived neurotoxin (EDN), an antimicrobial protein with
RT chemotactic activities for dendritic cells.";
RL Blood 102:3396-3403(2003).
CC -!- FUNCTION: Cytotoxin and helminthotoxin with ribonuclease activity.
CC Selectively chemotactic for dendritic cells. Possesses a wide variety
CC of biological activities.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic granule {ECO:0000250}. Note=Matrix of
CC eosinophil's large specific granule. {ECO:0000250}.
CC -!- DOMAIN: The N-terminal region is necessary for mediating chemotactic
CC activity.
CC -!- SIMILARITY: Belongs to the pancreatic ribonuclease family.
CC {ECO:0000305}.
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DR EMBL; U72031; AAB37785.1; -; mRNA.
DR EMBL; AF306664; AAG25991.1; -; Genomic_DNA.
DR EMBL; AF306665; AAG25992.1; -; mRNA.
DR EMBL; BC065391; AAH65391.1; -; mRNA.
DR EMBL; BC094626; AAH94626.1; -; mRNA.
DR CCDS; CCDS26968.1; -.
DR PIR; JC6160; JC6160.
DR RefSeq; NP_031921.1; NM_007895.2.
DR AlphaFoldDB; P97425; -.
DR SMR; P97425; -.
DR STRING; 10090.ENSMUSP00000074386; -.
DR GlyGen; P97425; 3 sites.
DR PaxDb; P97425; -.
DR PeptideAtlas; P97425; -.
DR PRIDE; P97425; -.
DR ProteomicsDB; 277543; -.
DR DNASU; 13587; -.
DR Ensembl; ENSMUST00000074839; ENSMUSP00000074386; ENSMUSG00000072596.
DR GeneID; 13587; -.
DR KEGG; mmu:13587; -.
DR UCSC; uc007tdi.1; mouse.
DR CTD; 13587; -.
DR MGI; MGI:108020; Ear2.
DR VEuPathDB; HostDB:ENSMUSG00000072596; -.
DR eggNOG; ENOG502TF52; Eukaryota.
DR GeneTree; ENSGT00940000162253; -.
DR HOGENOM; CLU_117006_0_1_1; -.
DR InParanoid; P97425; -.
DR OMA; NQSIRCP; -.
DR OrthoDB; 1482425at2759; -.
DR PhylomeDB; P97425; -.
DR TreeFam; TF333393; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 13587; 2 hits in 36 CRISPR screens.
DR ChiTaRS; Ear2; mouse.
DR PRO; PR:P97425; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; P97425; protein.
DR Bgee; ENSMUSG00000072596; Expressed in granulocyte and 30 other tissues.
DR ExpressionAtlas; P97425; baseline and differential.
DR Genevisible; P97425; MM.
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; IDA:UniProtKB.
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 Chemotaxis; Disulfide bond; Endonuclease; Glycoprotein; Hydrolase;
KW Nuclease; Reference proteome; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..156
FT /note="Eosinophil cationic protein 2"
FT /id="PRO_0000030868"
FT ACT_SITE 38
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 151
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 62..66
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
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:0000250"
FT DISULFID 47..106
FT /evidence="ECO:0000250"
FT DISULFID 61..119
FT /evidence="ECO:0000250"
FT DISULFID 79..134
FT /evidence="ECO:0000250"
FT DISULFID 86..94
FT /evidence="ECO:0000250"
SQ SEQUENCE 156 AA; 17620 MW; A15E8C1133091053 CRC64;
MGPKLLESRL CLLLLLGLVL MLASCLGQTP SQWFAIQHIN NNANLQCNVE MQRINRFRRT
CKGLNTFLHT SFANAVGVCG NPSGLCSDNI SRNCHNSSSR VRITVCNITS RRRTPYTQCR
YQPRRSLEYY TVACNPRTPQ DSPMYPVVPV HLDGTF
