ID   ENDUC_XENLA             Reviewed;         303 AA.
AC   A8E624; Q7T2H8;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   25-MAY-2022, entry version 39.
DE   RecName: Full=Uridylate-specific endoribonuclease C;
DE            EC=4.6.1.- {ECO:0000250|UniProtKB:P21128};
DE   AltName: Full=Placental protein 11 homolog;
DE   AltName: Full=Protein endoU-C;
DE   AltName: Full=XendoU-C;
DE   Flags: Precursor;
GN   Name=endou-c; Synonyms=pp11;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Pancreas;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 35-127.
RX   PubMed=12752502; DOI=10.1034/j.1600-0854.2004.00683.x;
RA   Sogame A., Hayata T., Asashima M.;
RT   "Screening for novel pancreatic genes from in vitro-induced pancreas in
RT   Xenopus.";
RL   Dev. Growth Differ. 45:143-152(2003).
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. {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; BC153811; AAI53812.1; -; mRNA.
DR   EMBL; AB098554; BAC78386.1; -; mRNA.
DR   AlphaFoldDB; A8E624; -.
DR   SMR; A8E624; -.
DR   OMA; NSECARF; -.
DR   Proteomes; UP000186698; Genome assembly.
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..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..303
FT                   /note="Uridylate-specific endoribonuclease C"
FT                   /id="PRO_0000394227"
FT   DOMAIN          32..303
FT                   /note="EndoU"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01304"
FT   ACT_SITE        181
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01304"
FT   ACT_SITE        196
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01304"
FT   ACT_SITE        239
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01304"
FT   CARBOHYD        287
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   303 AA;  33756 MW;  7E1B8CA82BC34CBC CRC64;
     MVYLVFLCLL PSLISGASIL PEPRKDVRAS ATDAEIQSLA EQFYAADTNK AASGDITLNL
     QYKASSSQTS TGTDYANQKL FRYVNEAKLF ARPTFARLVN LLDNYAQKTG SAESVPTTEV
     NEQNAFLDEI FKTSIITKLS NFFISKGYYS SAASFKTDLK AMWFGLYTRT SGPLDSSGFE
     HVFHGEIHKG KVSGLHNWVK LYLLEKSGQV NYLSYSADGV WKGYPDIYAF QLKWSTYLKT
     IGSFFVGSSP EFDIAMYTLC YVTRPDSLCS VKMGGSIFKI QTYTWANSTY GNGKRFVASS
     YPI