ID   ECP3_MOUSE              Reviewed;         156 AA.
AC   O35290;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Eosinophil cationic-type ribonuclease 3;
DE   AltName: Full=MR-3;
DE   Flags: Precursor;
GN   Name=Ear3; Synonyms=Rnase3;
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 [GENOMIC DNA].
RC   TISSUE=Fibroblast;
RX   PubMed=9336452; DOI=10.1093/nar/25.21.4235;
RA   Batten D., Dyer K.D., Domachowske J.B., Rosenberg H.F.;
RT   "Molecular cloning of four novel murine ribonuclease genes: unusual
RT   expansion within the ribonuclease A gene family.";
RL   Nucleic Acids Res. 25:4235-4239(1997).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue, Kidney, Lung, and Spleen;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- SIMILARITY: Belongs to the pancreatic ribonuclease family.
CC       {ECO:0000305}.
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DR   EMBL; AF017258; AAC53489.1; -; Genomic_DNA.
DR   RefSeq; NP_059084.1; NM_017388.1.
DR   AlphaFoldDB; O35290; -.
DR   SMR; O35290; -.
DR   GlyGen; O35290; 4 sites.
DR   PhosphoSitePlus; O35290; -.
DR   PeptideAtlas; O35290; -.
DR   PRIDE; O35290; -.
DR   ProteomicsDB; 277439; -.
DR   DNASU; 53876; -.
DR   GeneID; 53876; -.
DR   KEGG; mmu:53876; -.
DR   UCSC; uc011zjh.1; mouse.
DR   CTD; 53876; -.
DR   MGI; MGI:1858237; Ear3.
DR   InParanoid; O35290; -.
DR   BioGRID-ORCS; 53876; 3 hits in 16 CRISPR screens.
DR   ChiTaRS; Nr2f2; mouse.
DR   PRO; PR:O35290; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; O35290; protein.
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   1: Evidence at protein level;
KW   Disulfide bond; Endonuclease; Glycoprotein; Hydrolase; Nuclease;
KW   Reference proteome; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..156
FT                   /note="Eosinophil cationic-type ribonuclease 3"
FT                   /id="PRO_0000030869"
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        41
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        89
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   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;  17745 MW;  C9C2B6ECEB5DA06C CRC64;
     MGPKLLESRL CLLLLLRLVL MLASCLGQTP SRWFAIQHIN NNTNLRCNVE MLRINRFRRT
     CKGLNTFLHT SFANAVGVCG NPSGLCSDNI SRNCHNSSSR VHITVCNITS RRRIPYTQCR
     YQPRRSVEYY TVACNPRTSL DSPMYPVVPV HLDGTF