ENDOU_CAEEL
ID ENDOU_CAEEL Reviewed; 307 AA.
AC Q21109; O02513;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=Endoribonuclease endu-1 {ECO:0000305};
DE EC=4.6.1.- {ECO:0000250|UniProtKB:P21128};
DE AltName: Full=Poly(U)-specific endoribonuclease homolog;
DE AltName: Full=Uridylate-specific endoribonuclease homolog;
DE Flags: Precursor;
GN Name=endu-1 {ECO:0000312|WormBase:K02A11.3};
GN ORFNames=K02A11.3 {ECO:0000312|WormBase:K02A11.3};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-201, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=12754521; DOI=10.1038/nbt829;
RA Kaji H., Saito H., Yamauchi Y., Shinkawa T., Taoka M., Hirabayashi J.,
RA Kasai K., Takahashi N., Isobe T.;
RT "Lectin affinity capture, isotope-coded tagging and mass spectrometry to
RT identify N-linked glycoproteins.";
RL Nat. Biotechnol. 21:667-672(2003).
RN [3]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-201, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA Taoka M., Takahashi N., Isobe T.;
RT "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT elegans and suggests an atypical translocation mechanism for integral
RT membrane proteins.";
RL Mol. Cell. Proteomics 6:2100-2109(2007).
CC -!- FUNCTION: Catalyzes RNA cleavage releasing a product with a 2',3'-
CC cyclic phosphate at the 3'-end. {ECO:0000250|UniProtKB:P21128}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleotidyl-ribonucleotide-RNA = a 3'-end 2',3'-
CC cyclophospho-ribonucleotide-RNA + a 5'-end dephospho-ribonucleoside-
CC RNA; Xref=Rhea:RHEA:67796, Rhea:RHEA-COMP:10464, Rhea:RHEA-
CC COMP:13936, Rhea:RHEA-COMP:17355, ChEBI:CHEBI:83064,
CC ChEBI:CHEBI:138284, ChEBI:CHEBI:173118; Evidence={ECO:0000305};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67797;
CC Evidence={ECO:0000305};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P21128};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q8JFY9}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ENDOU family. {ECO:0000305}.
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DR EMBL; Z75544; CAA99880.1; -; Genomic_DNA.
DR PIR; T23212; T23212.
DR RefSeq; NP_492590.1; NM_060189.1.
DR AlphaFoldDB; Q21109; -.
DR SMR; Q21109; -.
DR STRING; 6239.K02A11.3; -.
DR iPTMnet; Q21109; -.
DR EPD; Q21109; -.
DR PaxDb; Q21109; -.
DR PeptideAtlas; Q21109; -.
DR EnsemblMetazoa; K02A11.3.1; K02A11.3.1; WBGene00010488.
DR GeneID; 186864; -.
DR KEGG; cel:CELE_K02A11.3; -.
DR UCSC; K02A11.3; c. elegans.
DR CTD; 186864; -.
DR WormBase; K02A11.3; CE06057; WBGene00010488; endu-1.
DR eggNOG; KOG2849; Eukaryota.
DR GeneTree; ENSGT00530000063825; -.
DR HOGENOM; CLU_048034_1_0_1; -.
DR InParanoid; Q21109; -.
DR OMA; SETLFSW; -.
DR OrthoDB; 823332at2759; -.
DR PhylomeDB; Q21109; -.
DR PRO; PR:Q21109; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00010488; Expressed in material anatomical entity and 4 other tissues.
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 1: Evidence at protein level;
KW Endonuclease; Glycoprotein; Hydrolase; Lyase; Manganese; Metal-binding;
KW Nuclease; Reference proteome; RNA-binding; Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..307
FT /note="Endoribonuclease endu-1"
FT /id="PRO_0000394230"
FT DOMAIN 26..295
FT /note="EndoU"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01304"
FT ACT_SITE 175
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01304"
FT ACT_SITE 190
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01304"
FT ACT_SITE 231
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01304"
FT CARBOHYD 201
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754521,
FT ECO:0000269|PubMed:17761667"
SQ SEQUENCE 307 AA; 35495 MW; 3A7AF64368E98E74 CRC64;
MCSVLIFISI LTVLAQCQKI PRFDVSNSEL LAMAQKLRQV DTNRARPDQI KLNYQGHTVT
RDDSDAAQAK LFSKVDTSLF RKPSYELYIN LMDNFNRQTG VIEPRVSQAE EKNEVGKFLD
YVLESRPMQE LYNWFKAKGH PIATSPQVFR FWIGQLWFSH YSRALGRPDT SGFEHVFIGE
AKNGEISGMH NWVRFYVLEN NRTENFDYKG FTVKRFNIMA ALKFTWDGLL KRAGSILIGT
SPEFDMALYT MCFLSRRGRE TCDVEFDGCP LQITSFEIMQ QNKVYIGSIY PTAGRITDQC
RAQNRFN
