ENDUC_DANRE
ID ENDUC_DANRE Reviewed; 309 AA.
AC Q1LUM3; A3KNG8; B0S8H8;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Uridylate-specific endoribonuclease C {ECO:0000305};
DE EC=4.6.1.- {ECO:0000250|UniProtKB:P21128};
DE AltName: Full=Protein endoU-C;
DE Flags: Precursor;
GN Name=endouc; ORFNames=si:dkey-103i16.2;
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 GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAR-2007) 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAQ14751.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BX928740; CAK04736.1; -; Genomic_DNA.
DR EMBL; BX928740; CAQ14751.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC133830; AAI33831.1; -; mRNA.
DR RefSeq; NP_001038439.1; NM_001044974.1.
DR AlphaFoldDB; Q1LUM3; -.
DR SMR; Q1LUM3; -.
DR STRING; 7955.ENSDARP00000099395; -.
DR PaxDb; Q1LUM3; -.
DR Ensembl; ENSDART00000180090; ENSDARP00000154126; ENSDARG00000109519.
DR Ensembl; ENSDART00000187847; ENSDARP00000154618; ENSDARG00000112234.
DR Ensembl; ENSDART00000189777; ENSDARP00000148981; ENSDARG00000110065.
DR GeneID; 562040; -.
DR KEGG; dre:562040; -.
DR CTD; 562040; -.
DR ZFIN; ZDB-GENE-060503-141; endouc.
DR eggNOG; KOG2849; Eukaryota.
DR GeneTree; ENSGT00530000063825; -.
DR HOGENOM; CLU_048034_1_0_1; -.
DR InParanoid; Q1LUM3; -.
DR OMA; SETLFSW; -.
DR OrthoDB; 823332at2759; -.
DR PhylomeDB; Q1LUM3; -.
DR TreeFam; TF319848; -.
DR PRO; PR:Q1LUM3; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 18.
DR Bgee; ENSDARG00000112234; Expressed in zone of skin and 31 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 2: Evidence at transcript level;
KW Endonuclease; Glycoprotein; Hydrolase; Lyase; Manganese; Metal-binding;
KW Nuclease; Reference proteome; RNA-binding; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..309
FT /note="Uridylate-specific endoribonuclease C"
FT /id="PRO_0000394225"
FT DOMAIN 27..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 197
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01304"
FT ACT_SITE 242
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01304"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 3
FT /note="S -> R (in Ref. 2; AAI33831)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 309 AA; 35239 MW; EE385B4344260FF7 CRC64;
MASGYDFGWI PVLLSLFTLT DASSQTVNQE LSNIFNELWK LDVNRMEPLT NYNISLQGKA
GYIPQGSTNV VDHASSPLFV NVDEAKLSSI TTYARFMKLL DNYERSTGVA ERVTAEEVTE
NNSFLDAILE TAVMKRAHQY LIGKGKSRSD LRQFKSQLYY MWFRLYHRER NGGEDSSGFE
HVFVGETKFG REIMGLHNWV QFYLQEKQNL LDYKGYKARA NDVPDADDHV LNVQFSWHGL
VKPVASAFVG VSPEFEMAVF TILFLTSTEK TTTAVVNLDE YQLEMVVHRH GRCIGTAYPK
LLSSNNRHM
