MOAG4_CAEEL
ID MOAG4_CAEEL Reviewed; 82 AA.
AC Q9BKU8;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Modifier of protein aggregation 4 {ECO:0000303|PubMed:20723760, ECO:0000312|WormBase:Y37E3.4};
DE AltName: Full=Small EDRK-rich factor {ECO:0000303|PubMed:20723760};
DE Short=SERF {ECO:0000303|PubMed:20723760};
GN Name=moag-4 {ECO:0000303|PubMed:20723760, ECO:0000312|WormBase:Y37E3.4};
GN ORFNames=Y37E3.4 {ECO:0000312|WormBase:Y37E3.4};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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 [2] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP MET-49.
RX PubMed=20723760; DOI=10.1016/j.cell.2010.07.020;
RA van Ham T.J., Holmberg M.A., van der Goot A.T., Teuling E.,
RA Garcia-Arencibia M., Kim H.E., Du D., Thijssen K.L., Wiersma M.,
RA Burggraaff R., van Bergeijk P., van Rheenen J., Jerre van Veluw G.,
RA Hofstra R.M., Rubinsztein D.C., Nollen E.A.;
RT "Identification of MOAG-4/SERF as a regulator of age-related
RT proteotoxicity.";
RL Cell 142:601-612(2010).
RN [3] {ECO:0000305}
RP FUNCTION.
RX PubMed=28336532; DOI=10.1074/jbc.m116.764886;
RA Yoshimura Y., Holmberg M.A., Kukic P., Andersen C.B., Mata-Cabana A.,
RA Falsone S.F., Vendruscolo M., Nollen E.A.A., Mulder F.A.A.;
RT "MOAG-4 promotes the aggregation of alpha-synuclein by competing with self-
RT protective electrostatic interactions.";
RL J. Biol. Chem. 292:8269-8278(2017).
CC -!- FUNCTION: Positive regulator of protein aggregation and age-related
CC proteotoxicity (PubMed:20723760, PubMed:28336532). Induces
CC conformational changes in aggregation-prone proteins, driving them into
CC compact formations preceding the formation of aggregates
CC (PubMed:20723760, PubMed:28336532). {ECO:0000269|PubMed:20723760,
CC ECO:0000269|PubMed:28336532}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:20723760}.
CC Nucleus {ECO:0000269|PubMed:20723760}.
CC -!- DISRUPTION PHENOTYPE: Suppresses protein aggregation and toxicity
CC caused by protein aggregates. {ECO:0000269|PubMed:20723760}.
CC -!- SIMILARITY: Belongs to the SERF family. {ECO:0000305}.
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DR EMBL; BX284601; CCD73424.1; -; Genomic_DNA.
DR RefSeq; NP_490924.1; NM_058523.4.
DR AlphaFoldDB; Q9BKU8; -.
DR STRING; 6239.Y37E3.4.2; -.
DR EPD; Q9BKU8; -.
DR PaxDb; Q9BKU8; -.
DR PeptideAtlas; Q9BKU8; -.
DR EnsemblMetazoa; Y37E3.4.1; Y37E3.4.1; WBGene00021348.
DR GeneID; 171764; -.
DR UCSC; Y37E3.4; c. elegans.
DR CTD; 171764; -.
DR WormBase; Y37E3.4; CE26771; WBGene00021348; moag-4.
DR eggNOG; KOG4488; Eukaryota.
DR HOGENOM; CLU_165034_1_0_1; -.
DR InParanoid; Q9BKU8; -.
DR OMA; DADIMRI; -.
DR OrthoDB; 1641955at2759; -.
DR PhylomeDB; Q9BKU8; -.
DR PRO; PR:Q9BKU8; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00021348; Expressed in embryo and 4 other tissues.
DR GO; GO:0005829; C:cytosol; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0031648; P:protein destabilization; IMP:UniProtKB.
DR InterPro; IPR007513; Uncharacterised_SERF_N.
DR Pfam; PF04419; 4F5; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Reference proteome.
FT CHAIN 1..82
FT /note="Modifier of protein aggregation 4"
FT /id="PRO_0000448245"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 63..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 49
FT /note="M->I: In pk2185; suppresses protein aggregation;
FT does not effect animal lifespan."
FT /evidence="ECO:0000269|PubMed:20723760"
SQ SEQUENCE 82 AA; 8895 MW; B91B862B5E7362FF CRC64;
MTRGNQRDLA REKNQKKLAD QKKRQGASGQ DGNAGLSMDA RMNRDADVMR IKQEKAAAKK
EAEAAAAAAN AKKVAKVDPL KM
