RLE1_CAEEL
ID RLE1_CAEEL Reviewed; 952 AA.
AC O45962; F5GUI8; G5EDG1; Q93898;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2012, sequence version 4.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Regulation of longevity by E3 ubiquitin-protein ligase;
DE EC=2.3.2.27 {ECO:0000303|PubMed:17276341, ECO:0000303|PubMed:24448648};
DE AltName: Full=RING-type E3 ubiquitin transferase rle-1 {ECO:0000305};
GN Name=rle-1 {ECO:0000312|WormBase:M142.6a};
GN ORFNames=M142.6 {ECO:0000312|WormBase:M142.6a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, INTERACTION WITH DAF-16,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF CYS-34.
RX PubMed=17276341; DOI=10.1016/j.devcel.2006.12.002;
RA Li W., Gao B., Lee S.-M., Bennett K., Fang D.;
RT "RLE-1, an E3 ubiquitin ligase, regulates C. elegans aging by catalyzing
RT DAF-16 polyubiquitination.";
RL Dev. Cell 12:235-246(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
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 [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24448648; DOI=10.1126/scisignal.2004822;
RA Maruyama T., Araki T., Kawarazaki Y., Naguro I., Heynen S., Aza-Blanc P.,
RA Ronai Z., Matsuzawa A., Ichijo H.;
RT "Roquin-2 promotes ubiquitin-mediated degradation of ASK1 to regulate
RT stress responses.";
RL Sci. Signal. 7:RA8-RA8(2014).
CC -!- FUNCTION: E3 ubiquitin-protein ligase. Regulates the activity of daf-16
CC and is thereby involved in regulating aging and stress resistance
CC (PubMed:17276341). Regulates nsy-1 activity and thereby attenuates the
CC activation of sek-1 and pmk-1, two components of the p38 pathway, which
CC results in susceptibility to pathogenic bacterial infection
CC (PubMed:24448648). {ECO:0000269|PubMed:17276341,
CC ECO:0000269|PubMed:24448648}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000303|PubMed:17276341,
CC ECO:0000303|PubMed:24448648};
CC -!- PATHWAY: Protein degradation; proteasomal ubiquitin-dependent pathway.
CC {ECO:0000269|PubMed:17276341}.
CC -!- SUBUNIT: Interacts (via C-terminus) with daf-16.
CC {ECO:0000269|PubMed:17276341}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=a;
CC IsoId=O45962-1; Sequence=Displayed;
CC Name=c;
CC IsoId=O45962-2; Sequence=VSP_043605, VSP_043606;
CC Name=b;
CC IsoId=O45962-3; Sequence=VSP_043604;
CC -!- DISRUPTION PHENOTYPE: Increased lifespan, retarded growth and
CC development (PubMed:17276341). Increased survival rate upon
CC P.aeruginosa infection (PubMed:24448648). {ECO:0000269|PubMed:17276341,
CC ECO:0000269|PubMed:24448648}.
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DR EMBL; Z73428; CAA97810.3; -; Genomic_DNA.
DR EMBL; Z99276; CAA97810.3; JOINED; Genomic_DNA.
DR EMBL; Z73428; CCD31104.1; -; Genomic_DNA.
DR EMBL; Z99276; CCD31104.1; JOINED; Genomic_DNA.
DR EMBL; Z99276; CCA65670.1; -; Genomic_DNA.
DR PIR; T23764; T23764.
DR RefSeq; NP_001255093.1; NM_001268164.1.
DR RefSeq; NP_001255094.1; NM_001268165.1.
DR RefSeq; NP_001255095.1; NM_001268166.1.
DR AlphaFoldDB; O45962; -.
DR SMR; O45962; -.
DR BioGRID; 41711; 3.
DR DIP; DIP-24657N; -.
DR IntAct; O45962; 3.
DR MINT; O45962; -.
DR STRING; 6239.M142.6a; -.
DR EPD; O45962; -.
DR PaxDb; O45962; -.
DR PeptideAtlas; O45962; -.
DR EnsemblMetazoa; M142.6a.1; M142.6a.1; WBGene00010923. [O45962-1]
DR EnsemblMetazoa; M142.6b.1; M142.6b.1; WBGene00010923. [O45962-3]
DR EnsemblMetazoa; M142.6c.1; M142.6c.1; WBGene00010923. [O45962-2]
DR UCSC; M142.6; c. elegans. [O45962-1]
DR WormBase; M142.6a; CE45978; WBGene00010923; rle-1. [O45962-1]
DR WormBase; M142.6b; CE46027; WBGene00010923; rle-1. [O45962-3]
DR WormBase; M142.6c; CE46406; WBGene00010923; rle-1. [O45962-2]
DR eggNOG; KOG3161; Eukaryota.
DR InParanoid; O45962; -.
DR OMA; FFREADS; -.
DR OrthoDB; 309498at2759; -.
DR SignaLink; O45962; -.
DR UniPathway; UPA00144; -.
DR PRO; PR:O45962; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00010923; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0010494; C:cytoplasmic stress granule; IBA:GO_Central.
DR GO; GO:0003725; F:double-stranded RNA binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0035613; F:RNA stem-loop binding; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:UniProtKB.
DR GO; GO:0000288; P:nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IBA:GO_Central.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0009408; P:response to heat; IMP:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:WormBase.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR041523; ROQ_II.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR Pfam; PF18386; ROQ_II; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Metal-binding; Reference proteome;
KW Stress response; Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..952
FT /note="Regulation of longevity by E3 ubiquitin-protein
FT ligase"
FT /id="PRO_0000377381"
FT ZN_FING 16..57
FT /note="RING-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 410..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 445..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 80..113
FT /evidence="ECO:0000255"
FT COILED 882..922
FT /evidence="ECO:0000255"
FT COMPBIAS 445..468
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..511
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..822
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_043604"
FT VAR_SEQ 793..812
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_043605"
FT VAR_SEQ 813
FT /note="S -> A (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_043606"
FT MUTAGEN 34
FT /note="C->A: Abrogates E3 ubiquitin-protein ligase activity
FT for daf-16."
FT /evidence="ECO:0000269|PubMed:17276341"
SQ SEQUENCE 952 AA; 104766 MW; C901A7D70DB1CD39 CRC64;
MAPTGQGGQW QEVLCCSICN RHFNETFLPV SLICGHVICR KCAEKPENQT KPCPHDDWKT
THSPSEYPNN VALLSVIFPR KQCMTLSGAV SEAEKRVDQL SIQIAKFFRE ADSERGGTVS
SREISRTLQR KVLALLCYQW REVDGRLKTL KMCRGISERV MIEIILSIQS NTHVSSQLWS
AVRARGCQFL GPAMQDDVLR LILMTLETGE CIARKNLVMY VVQTLASDYP QVSKTCVGHV
VQLLYRASCF NVLKRDGESS LMQLKEEFRT YESLRREHDS QIVQIAFESG LRIGPDQWSA
LLYADQSHRS HMQSIIDKLQ SKNSYQQGVE ELRALAGSQT SMLVPAYRYF LTQVIPCLEF
FAGIEHEDTS MRMIGDALHQ IRILLKLHCS QDDLRKMPKE ERRGVILQAE VPGGMGGGPG
GSGGAEAGRI GGLHPLYSQI DETGRSISRT NPKDNSHNSP QTPPKQPRQK RYQMGIPPNR
MGYSSDAPPF IPSHQQQPPP QFFNSQHLPQ RFRGGRQRGA PPPPPPQPMP MLIGYDMPGA
PMMQATEVLT ADGQMVNGTP QRVVIMQSPT HLPGGPVVMI PQQQMVPPPQ SMTPVGGPMG
PMGPMTPSIP VQVPPNTMWT ATSPTGSVIY PAASPPGQPP HTIWIQSTDG NMFPMFDRGS
GGMVWGPGTM LRESGADAEQ LLAKRYEILK RLQPSEDDDD PEDGGIGHVS YTVASSVLDD
RMDHHPLTMI PVPTIDLPAI PISFANMPTE ETMTMIGEMV QNRPRAPSLT APSSNQPMNV
NASASATVQA ECGTMSVMDS ICQPISTSAI HNSATIPQPV IPMVQVPVQV PIVPAENFNP
NVPPPPPPPQ GQPMLVDSAI GLLTPIRPIL VAHPQNVVSN SLDKIVDVKE RISEAQGNAS
EAENAHLRME LRMAESQMAH LDPYTKNNCL LRALQQVDME LQQLHLNPTV EG
