MEL26_CAEEL
ID MEL26_CAEEL Reviewed; 395 AA.
AC Q94420; Q94139;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Protein maternal effect lethal 26;
GN Name=mel-26; ORFNames=ZK858.4;
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 [GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9725834; DOI=10.1093/genetics/150.1.119;
RA Dow M.R., Mains P.E.;
RT "Genetic and molecular characterization of the Caenorhabditis elegans gene,
RT mel-26, a postmeiotic negative regulator of mei-1, a meiotic-specific
RT spindle component.";
RL Genetics 150:119-128(1998).
RN [2]
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 [3]
RP FUNCTION AS AN E3 UBIQUITIN-PROTEIN LIGASE, AND INTERACTION WITH CUL3 AND
RP MEI-1.
RX PubMed=14528312; DOI=10.1038/ncb1056;
RA Furukawa M., He Y.J., Borchers C., Xiong Y.;
RT "Targeting of protein ubiquitination by BTB-Cullin 3-Roc1 ubiquitin
RT ligases.";
RL Nat. Cell Biol. 5:1001-1007(2003).
RN [4]
RP FUNCTION AS AN E3 UBIQUITIN-PROTEIN LIGASE, AND INTERACTION WITH CUL3.
RX PubMed=13679922; DOI=10.1038/nature01985;
RA Xu L., Wei Y., Reboul J., Vaglio P., Shin T.H., Vidal M., Elledge S.J.,
RA Harper J.W.;
RT "BTB proteins are substrate-specific adaptors in an SCF-like modular
RT ubiquitin ligase containing CUL-3.";
RL Nature 425:316-321(2003).
RN [5]
RP FUNCTION, INTERACTION WITH UNC-89; CUL-3 AND MEI-1, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=22621901; DOI=10.1091/mbc.e12-01-0055;
RA Wilson K.J., Qadota H., Mains P.E., Benian G.M.;
RT "UNC-89 (obscurin) binds to MEL-26, a BTB-domain protein, and affects the
RT function of MEI-1 (katanin) in striated muscle of Caenorhabditis elegans.";
RL Mol. Biol. Cell 23:2623-2634(2012).
RN [6]
RP FUNCTION, INTERACTION WITH MEI-1 AND PPFR-1, AND MUTAGENESIS OF CYS-94.
RX PubMed=23918937; DOI=10.1083/jcb.201304174;
RA Gomes J.E., Tavernier N., Richaudeau B., Formstecher E., Boulin T.,
RA Mains P.E., Dumont J., Pintard L.;
RT "Microtubule severing by the katanin complex is activated by PPFR-1-
RT dependent MEI-1 dephosphorylation.";
RL J. Cell Biol. 202:431-439(2013).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=29769719; DOI=10.1038/s41586-018-0128-9;
RA Chen J., Ou Y., Yang Y., Li W., Xu Y., Xie Y., Liu Y.;
RT "KLHL22 activates amino-acid-dependent mTORC1 signalling to promote
RT tumorigenesis and ageing.";
RL Nature 557:585-589(2018).
CC -!- FUNCTION: Probable substrate-specific adapter of an E3 ubiquitin-
CC protein ligase complex which mediates the ubiquitination and subsequent
CC proteasomal degradation of target proteins (PubMed:14528312,
CC PubMed:13679922, PubMed:23918937). Controls degradation of microtubule
CC severing protein mei-1 after meiosis (PubMed:14528312). Controls
CC degradation of ppfr-1, the regulatory subunit of PP4 complex, after
CC meiosis (PubMed:23918937). In body wall muscles, involved in the
CC organization of myosin thick filaments, likely by regulating the
CC degradation of mei-1 downstream of unc-89 (PubMed:22621901). May also
CC activate the TORC1 pathway (PubMed:29769719).
CC {ECO:0000269|PubMed:13679922, ECO:0000269|PubMed:14528312,
CC ECO:0000269|PubMed:22621901, ECO:0000269|PubMed:23918937,
CC ECO:0000269|PubMed:29769719}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts (via BTB domain) with cul-3 (PubMed:13679922,
CC PubMed:14528312, PubMed:22621901). Seems to be a component of a E3
CC ubiquitin-protein ligase complex containing cul-3 (PubMed:13679922,
CC PubMed:14528312). Interacts (probably via MATH domain) with mei-1,
CC which targets mei-1 for ubiquitin-mediated proteolysis
CC (PubMed:14528312, PubMed:22621901, PubMed:23918937). Interacts
CC (probably via MATH domain) with ppfr-1, the regulatory subunit of the
CC PP4 complex; targets ppfr-1 for ubiquitin-mediated proteolysis
CC (PubMed:23918937). May interact (via MATH domain) with unc-89 (via Ig-
CC like C2-type domain 2/3 and, Ig-like C2-type domain 50 and fibronectin
CC type-III domain 2) (PubMed:22621901). {ECO:0000269|PubMed:13679922,
CC ECO:0000269|PubMed:14528312, ECO:0000269|PubMed:22621901,
CC ECO:0000269|PubMed:23918937}.
CC -!- INTERACTION:
CC Q94420; Q09230: C05C10.5; NbExp=4; IntAct=EBI-320790, EBI-314244;
CC Q94420; Q21648: CELE_R02F2.5; NbExp=3; IntAct=EBI-320790, EBI-314179;
CC Q94420; Q9NF71: CELE_Y105C5A.1; NbExp=4; IntAct=EBI-320790, EBI-332478;
CC Q94420; Q17391: cul-3; NbExp=3; IntAct=EBI-320790, EBI-593075;
CC Q94420; P34808: mei-1; NbExp=6; IntAct=EBI-320790, EBI-323248;
CC Q94420; P34808-2: mei-1; NbExp=3; IntAct=EBI-320790, EBI-521381;
CC Q94420; Q94420: mel-26; NbExp=7; IntAct=EBI-320790, EBI-320790;
CC Q94420; Q9GYQ9: ntl-4; NbExp=3; IntAct=EBI-320790, EBI-317604;
CC Q94420; G5ECH5: ppfr-1; NbExp=4; IntAct=EBI-320790, EBI-6691815;
CC Q94420; Q9XW53: rga-2; NbExp=3; IntAct=EBI-320790, EBI-2421364;
CC Q94420; P55853: smo-1; NbExp=5; IntAct=EBI-320790, EBI-313647;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, M line
CC {ECO:0000269|PubMed:22621901}. Cytoplasm, myofibril, sarcomere, I band
CC {ECO:0000269|PubMed:22621901}. Note=Colocalizes with unc-89 to the M
CC line. {ECO:0000269|PubMed:22621901}.
CC -!- TISSUE SPECIFICITY: Expressed in body wall muscles.
CC {ECO:0000269|PubMed:22621901}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown at L1 larval stage
CC results in the disorganization of myosin thick filaments in adult body
CC wall muscles characterized by the formation of abnormal myosin heavy
CC chain myo-3 aggregates and V-shaped crossing of A-bands
CC (PubMed:22621901). RNAi-mediated knockdown of mel-26 also results in
CC increased lifespan (PubMed:29769719). {ECO:0000269|PubMed:22621901,
CC ECO:0000269|PubMed:29769719}.
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DR EMBL; U67737; AAC63596.1; -; Genomic_DNA.
DR EMBL; Z79759; CAB02139.2; -; Genomic_DNA.
DR PIR; T28056; T28056.
DR RefSeq; NP_492449.2; NM_060048.8.
DR AlphaFoldDB; Q94420; -.
DR SMR; Q94420; -.
DR BioGRID; 38168; 71.
DR DIP; DIP-27179N; -.
DR IntAct; Q94420; 41.
DR MINT; Q94420; -.
DR STRING; 6239.ZK858.4b; -.
DR MoonDB; Q94420; Predicted.
DR EPD; Q94420; -.
DR PaxDb; Q94420; -.
DR EnsemblMetazoa; ZK858.4a.1; ZK858.4a.1; WBGene00003209.
DR GeneID; 172737; -.
DR UCSC; ZK858.4; c. elegans.
DR CTD; 172737; -.
DR WormBase; ZK858.4a; CE30580; WBGene00003209; mel-26.
DR eggNOG; KOG1987; Eukaryota.
DR InParanoid; Q94420; -.
DR PhylomeDB; Q94420; -.
DR Reactome; R-CEL-5632684; Hedgehog 'on' state.
DR SignaLink; Q94420; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q94420; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00003209; Expressed in germ line (C elegans) and 4 other tissues.
DR ExpressionAtlas; Q94420; baseline and differential.
DR GO; GO:0005938; C:cell cortex; IDA:WormBase.
DR GO; GO:0032154; C:cleavage furrow; IDA:WormBase.
DR GO; GO:0000793; C:condensed chromosome; IDA:WormBase.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0031674; C:I band; IDA:UniProtKB.
DR GO; GO:0031430; C:M band; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0097602; F:cullin family protein binding; IPI:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IPI:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR GO; GO:0071233; P:cellular response to leucine; ISS:UniProtKB.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:UniProtKB.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IMP:UniProtKB.
DR GO; GO:0010507; P:negative regulation of autophagy; ISS:UniProtKB.
DR GO; GO:0030307; P:positive regulation of cell growth; ISS:UniProtKB.
DR GO; GO:1904263; P:positive regulation of TORC1 signaling; IMP:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0030163; P:protein catabolic process; IMP:WormBase.
DR GO; GO:0000209; P:protein polyubiquitination; IDA:UniProtKB.
DR GO; GO:0032888; P:regulation of mitotic spindle elongation; IMP:UniProtKB.
DR GO; GO:0030162; P:regulation of proteolysis; IBA:GO_Central.
DR GO; GO:0071688; P:striated muscle myosin thick filament assembly; IMP:UniProtKB.
DR Gene3D; 2.60.210.10; -; 1.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR002083; MATH/TRAF_dom.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR008974; TRAF-like.
DR Pfam; PF00651; BTB; 1.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00061; MATH; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS50144; MATH; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..395
FT /note="Protein maternal effect lethal 26"
FT /id="PRO_0000312628"
FT DOMAIN 41..162
FT /note="MATH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00129"
FT DOMAIN 201..269
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT MUTAGEN 94
FT /note="C->Y: Severe loss of interaction with ppfr-1 and
FT mei-1."
FT /evidence="ECO:0000269|PubMed:23918937"
SQ SEQUENCE 395 AA; 44492 MW; 3AED944583A155AC CRC64;
MEPRIDGGVF IGGIGNSGNE MCSNGVPALG VSSQTEIKVE KVQHTWTVKN FSHCYQEYLE
NFVYLQRGDE QLTWSIKIYP KGNGENNKDF VFLCLNRVIN NNVKAGKIGF KSQFKLRTAE
NKDIEMRIHP NPSHSDYVSY IKRDVLFPQI MPRDMIIVNV EIDVAVETIT TTNEPIQFEP
TNSEQQLIED YQRLFSQELL CDFAINVNGK IIRAHKAVLA ARSPVFNAML THQDTDEAKS
SMMYINDMDY DVIYEMVYYI YCGRCNKDIT DMATALLIAA DKYRLEELKS HCEKYLVENI
NIENACSLLI IGDLYSAPKL RKRAVTYILA RPKNVTGTPG WEDILKGHPN LITDIFSQID
RQSSTGATSS VSNLPGVPMD IPGITGNIVP PPSGL
