YJU2_DANRE
ID YJU2_DANRE Reviewed; 345 AA.
AC A8WHR3;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Splicing factor YJU2 {ECO:0000255|HAMAP-Rule:MF_03226};
GN Name=yju2 {ECO:0000255|HAMAP-Rule:MF_03226}; Synonyms=ccdc94;
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 (NOV-2008) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF 125-ARG--ASP-345.
RX PubMed=22952453; DOI=10.1371/journal.pgen.1002922;
RA Sorrells S., Carbonneau S., Harrington E., Chen A.T., Hast B., Milash B.,
RA Pyati U., Major M.B., Zhou Y., Zon L.I., Stewart R.A., Look A.T., Jette C.;
RT "Ccdc94 protects cells from ionizing radiation by inhibiting the expression
RT of p53.";
RL PLoS Genet. 8:E1002922-E1002922(2012).
CC -!- FUNCTION: Part of the spliceosome which catalyzes two sequential
CC transesterification reactions, first the excision of the non-coding
CC intron from pre-mRNA and then the ligation of the coding exons to form
CC the mature mRNA. Plays a role in stabilizing the structure of the
CC spliceosome catalytic core and docking of the branch helix into the
CC active site, producing 5'-exon and lariat intron-3'-intermediates (By
CC similarity). May protect cells from TP53-dependent apoptosis upon dsDNA
CC break damage through association with PRP19-CD5L complex
CC (PubMed:22952453). {ECO:0000255|HAMAP-Rule:MF_03226,
CC ECO:0000269|PubMed:22952453}.
CC -!- SUBUNIT: Component of the spliceosome. Present in the activated B
CC complex, the catalytically activated B* complex which catalyzes the
CC branching, the catalytic step 1 C complex catalyzing the exon ligation,
CC and the postcatalytic P complex containing the ligated exons (mRNA) and
CC the excised lariat intron. {ECO:0000255|HAMAP-Rule:MF_03226}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9BW85,
CC ECO:0000255|HAMAP-Rule:MF_03226}.
CC -!- DISRUPTION PHENOTYPE: Morpholino knockdown of the protein causes small
CC head and a curled tail by day 2. Knockdown causes increased sensitivity
CC to IR-induced apoptosis (PubMed:22952453). In double morpholino
CC knockdown of TP53 and YJU2, TP53 deficiency rescues animals from
CC developmental neurodegeneration observed on YJU2 mutants and
CC radiosensitivity (PubMed:22952453). {ECO:0000269|PubMed:22952453}.
CC -!- SIMILARITY: Belongs to the CWC16 family. YJU2 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03226}.
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DR EMBL; BX248231; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC171445; AAI71445.1; -; mRNA.
DR EMBL; BC171449; AAI71449.1; -; mRNA.
DR RefSeq; NP_001104303.1; NM_001110833.1.
DR AlphaFoldDB; A8WHR3; -.
DR SMR; A8WHR3; -.
DR STRING; 7955.ENSDARP00000035484; -.
DR PaxDb; A8WHR3; -.
DR PeptideAtlas; A8WHR3; -.
DR Ensembl; ENSDART00000036813; ENSDARP00000035484; ENSDARG00000026185.
DR GeneID; 393117; -.
DR KEGG; dre:393117; -.
DR CTD; 55702; -.
DR ZFIN; ZDB-GENE-040426-841; yju2.
DR eggNOG; KOG2989; Eukaryota.
DR GeneTree; ENSGT00530000063615; -.
DR HOGENOM; CLU_053603_0_0_1; -.
DR InParanoid; A8WHR3; -.
DR OMA; HYNADPY; -.
DR OrthoDB; 1583452at2759; -.
DR PhylomeDB; A8WHR3; -.
DR TreeFam; TF315070; -.
DR PRO; PR:A8WHR3; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 2.
DR Bgee; ENSDARG00000026185; Expressed in blastula and 29 other tissues.
DR GO; GO:0071006; C:U2-type catalytic step 1 spliceosome; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000349; P:generation of catalytic spliceosome for first transesterification step; IEA:UniProtKB-UniRule.
DR GO; GO:0043518; P:negative regulation of DNA damage response, signal transduction by p53 class mediator; IMP:ZFIN.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:ZFIN.
DR GO; GO:0008380; P:RNA splicing; IBA:GO_Central.
DR HAMAP; MF_03226; YJU2; 1.
DR InterPro; IPR007590; Saf4/Yju2.
DR InterPro; IPR043701; Yju2.
DR PANTHER; PTHR12111; PTHR12111; 1.
DR Pfam; PF04502; Saf4_Yju2; 1.
PE 1: Evidence at protein level;
KW Metal-binding; mRNA processing; mRNA splicing; Nucleus; Reference proteome;
KW Spliceosome; Zinc.
FT CHAIN 1..345
FT /note="Splicing factor YJU2"
FT /id="PRO_0000444891"
FT REGION 205..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..232
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..254
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..345
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 43
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03226"
FT BINDING 46
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03226"
FT BINDING 80
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03226"
FT BINDING 83
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03226"
FT MUTAGEN 125..345
FT /note="Missing: In rs7; mutant embryos have a small head
FT and a curled tail by day 2 and die by the end of day 3.
FT Mutation causes increased sensitivity to IR-induced
FT apoptosis. Mutants do not show changes in alternative
FT splicing."
FT /evidence="ECO:0000269|PubMed:22952453"
SQ SEQUENCE 345 AA; 38858 MW; 18AB1AC04DB39BEC CRC64;
MSERKVLNKY YPPDFDPSKI PKLKLPKDRQ YVVRLMAPFN MRCKTCGEYI YKGKKFNARK
ETVQNELYLG LPIFRFYIKC TRCLAEITFK TDPENTDYAM EHGATRNFQA EKLIEEEEKK
IQQEREDEEL NNPMKVLENR TRDSKLEMEV LENLQELKEL NQRQAQVDFE GMLGQYKELE
QRQKQREQEE DEQETKEMLE RALVKRLRDS DSEEEAENAK ERSKKHIADK PTDILTTDTS
TSSQGLSSAV AKKQSWDRSV GGLSVKGALG SLVVRKKPAD SASKPSHAAP PPAAAAAGTQ
TGAVKPESSI TSSSASSNIQ PVSCQNGSSL GLLGAYSDSD DSSSD
