Caenorhabditis elegans CEL DPF-3 N-terminal processing of Argonaute (Ago) proteins
DPF-3 dipeptidase orthologous to mammalian dipeptidyl peptidase (DPP) 8\/9, processes the unusually proline-rich N termini of WAGO-1 and WAGO-3 Argonaute (Ago) proteins Without DPF-3 activity, these WAGO proteins lose their proper complement of 22G RNAs. Desilencing of repeat-containing and transposon-derived transcripts, DNA damage, and acute sterility ensue (Gudipati et al.2021)
Family : DPP4N_Peptidase_S9
Block : X
Position in NCBI Life Tree : Caenorhabditis elegans
(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.)
> cellular organisms N E > Eukaryota N E > Opisthokonta N E > Metazoa N E > Eumetazoa N E > Bilateria N E > Protostomia N E > Ecdysozoa N E > Nematoda N E > Chromadorea N E > Rhabditida N E > Rhabditoidea N E > Rhabditidae N E > Peloderinae N E > Caenorhabditis N E > Caenorhabditis elegans N EMMFNFYQFLY NLQNVSPFID FSVLKQLTHT KMRENEPARF ETRSFSQLID HARSWKTEVR GMTTQGFTKI SLMRAEKDRL NMYAISSVPG TNTQSIFSVT IPLELVEKAQ VADRKFELKL KSGYNVDSYI RMSCRKTPPS AEFTLQCERQ RSQVVTGISD YEIRNGKMIL MAGDQLFRYN PLNEALAAIP IAVPDDQSST EPMDISEGSI TSGTKGCSNE APQSSTVPPV TRIPIKKPTT STEKPATAPP TNNFVSSAKV CPADSSLLAY VLNKQVYIEK NGKIIHRTSS NSKHITNGVP SYIVQEELER FEGIWWSESK TRLLYEHVNE EKVAESQFGV NGDPPVAPMK YPRAGTKNAY STLRMVILEN GKAYDVPLKD EVIYKHCPFY EYITRAGFFS DGTTVWVQVM SRDQAQCSLL LIPYTDFLLP EELGGSIKED NLQLSTDLNM GVWDDKSHEE TMEKPPRGKL RGTVQIHKAR NDYWINTHNA IYPLKITDEE HPMYEFIYCL EKPNGSCLAL ISAELDQNGY CRHTEEKLLM AENFSINKSM GIVVDEVREL VYYVANESHP TEWNICVSHY RTGQHAQLTE SGICFKSERA NGKLALDLDH GFACYMTSVG SPAECRFYSF RWKENEVLPS TVYAANITVS GHPGQPDLHF DSPEMIEFQS KKTGLMHYAM ILRPSNFDPY KKYPVFHYVY GGPGIQIVHN DFSWIQYIRF CRLGYVVVFI DNRGSAHRGI EFERHIHKKM GTVEVEDQVE GLQMLAERTG GFMDMSRVVV HGWSYGGYMA LQMIAKHPNI YRAAIAGGAV SDWRLYDTAY TERYMGYPLE EHVYGASSIT GLVEKLPDEP NRLMLVHGLM DENVHFAHLT HLVDECIKKG KWHELVIFPN ERHGVRNNDA SIYLDARMMY FAQQAIQGFG PTTAAPRQGP L
Title : Dipeptidyl peptidase DPF-3 is a gatekeeper of microRNA Argonaute compensation in animals - Harvey_2025_Nat.Commun_16_2738 |
Author(s) : Harvey LM , Frederick PM , Gudipati RK , Michaud P , Houle F , Young D , Desbiens C , Ladouceur S , Dufour A , Grosshans H , Simard MJ |
Ref : Nat Commun , 16 :2738 , 2025 |
Abstract : |
PubMedSearch : Harvey_2025_Nat.Commun_16_2738 |
PubMedID: 40108168 |
Gene_locus related to this paper: caeel-K02F2.1 |
Title : Deep quantification of substrate turnover defines protease subsite cooperativity - Gudipati_2024_Mol.Syst.Biol__ |
Author(s) : Gudipati RK , Gaidatzis D , Seebacher J , Muehlhaeusser S , Kempf G , Cavadini S , Hess D , Soneson C , Grosshans H |
Ref : Mol Syst Biol , : , 2024 |
Abstract : |
PubMedSearch : Gudipati_2024_Mol.Syst.Biol__ |
PubMedID: 39468329 |
Gene_locus related to this paper: caeel-K02F2.1 , human-DPP4 |
Title : Protease-mediated processing of Argonaute proteins controls small RNA association - Gudipati_2021_Mol.Cell_81_2388 |
Author(s) : Gudipati RK , Braun K , Gypas F , Hess D , Schreier J , Carl SH , Ketting RF , Grosshans H |
Ref : Mol Cell , 81 :2388 , 2021 |
Abstract : |
PubMedSearch : Gudipati_2021_Mol.Cell_81_2388 |
PubMedID: 33852894 |
Gene_locus related to this paper: caeel-K02F2.1 |