ID   ENDUA_DANRE             Reviewed;         303 AA.
AC   A1L237; A8E5A1;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Uridylate-specific endoribonuclease A {ECO:0000305};
DE            EC=4.6.1.- {ECO:0000250|UniProtKB:P21128};
DE   AltName: Full=Protein endoU-A;
DE   Flags: Precursor;
GN   Name=endoua; ORFNames=zgc:158628;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Endoribonuclease that cleaves single-stranded RNAs at 5' of
CC       uridylates and releases a product with a 2',3'-cyclic phosphate at the
CC       3'-end. The UU and GU sites are more efficiently cleaved than CU and AU
CC       sites. {ECO:0000250|UniProtKB:P21128}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ribonucleotidyl-uridine-RNA = a 3'-end 2',3'-cyclophospho-
CC         ribonucleotide-RNA + a 5'-end dephospho-uridine-RNA;
CC         Xref=Rhea:RHEA:67792, Rhea:RHEA-COMP:10464, Rhea:RHEA-COMP:17354,
CC         Rhea:RHEA-COMP:17356, ChEBI:CHEBI:83064, ChEBI:CHEBI:173117,
CC         ChEBI:CHEBI:173224; Evidence={ECO:0000250|UniProtKB:P21128};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67793;
CC         Evidence={ECO:0000250|UniProtKB:P21128};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ENDOU family. {ECO:0000305}.
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DR   EMBL; BC129332; AAI29333.1; -; mRNA.
DR   EMBL; BC153519; AAI53520.1; -; mRNA.
DR   RefSeq; NP_001074167.1; NM_001080698.1.
DR   AlphaFoldDB; A1L237; -.
DR   SMR; A1L237; -.
DR   STRING; 7955.ENSDARP00000104110; -.
DR   PaxDb; A1L237; -.
DR   PeptideAtlas; A1L237; -.
DR   GeneID; 791216; -.
DR   KEGG; dre:791216; -.
DR   CTD; 8909; -.
DR   ZFIN; ZDB-GENE-070112-2012; endou.
DR   eggNOG; KOG2849; Eukaryota.
DR   InParanoid; A1L237; -.
DR   OrthoDB; 823332at2759; -.
DR   PhylomeDB; A1L237; -.
DR   PRO; PR:A1L237; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004521; F:endoribonuclease activity; ISS:UniProtKB.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR   CDD; cd21159; XendoU; 1.
DR   InterPro; IPR039787; ENDOU.
DR   InterPro; IPR037227; EndoU-like.
DR   InterPro; IPR018998; EndoU_C.
DR   PANTHER; PTHR12439; PTHR12439; 1.
DR   Pfam; PF09412; XendoU; 1.
DR   SUPFAM; SSF142877; SSF142877; 1.
DR   PROSITE; PS51959; ENDOU; 1.
PE   2: Evidence at transcript level;
KW   Endonuclease; Glycoprotein; Hydrolase; Lyase; Manganese; Metal-binding;
KW   Nuclease; Reference proteome; RNA-binding; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..303
FT                   /note="Uridylate-specific endoribonuclease A"
FT                   /id="PRO_0000394223"
FT   DOMAIN          30..303
FT                   /note="EndoU"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01304"
FT   ACT_SITE        179
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01304"
FT   ACT_SITE        194
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01304"
FT   ACT_SITE        237
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01304"
FT   CARBOHYD        28
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        77
FT                   /note="P -> L (in Ref. 1; AAI53520)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        93
FT                   /note="E -> K (in Ref. 1; AAI53520)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        195
FT                   /note="S -> N (in Ref. 1; AAI53520)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        287
FT                   /note="S -> T (in Ref. 1; AAI53520)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   303 AA;  33845 MW;  8068CC6894B239C4 CRC64;
     MKIILILCLS ITLISQGHFD SLDLSLANVS DAEIKSLSET LYKLDSNRAT ASELLIDPQT
     LIPSSQTGSG NDLSPQPLFK VVSSTLLSKP TYEAFLDLLD NYKKMTGEVE DVPSHEEQEQ
     DSFLQQTMNT NLGKELFNFL HSKGVYGSQS EFLQDLKMMW FGLYSRSDGV KLDSSGFEHI
     FVGEIKGGKV SGFHSWVQFY QCEKQGILNY YSHSFDGPWT TYPDVLGMQF NWDGYFKELG
     SAFIGCSPEF DLAIYSLCYI TRPGKKCDVS LGGHSLGIQT YTWDKSSYGD GKKFIGSAYP
     ITP