MRG1_CAEEL
ID MRG1_CAEEL Reviewed; 337 AA.
AC A7DTF0; Q9XWW2;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Mortality factor related protein 1 {ECO:0000303|PubMed:12175490, ECO:0000312|WormBase:Y37D8A.9b};
GN Name=mrg-1 {ECO:0000303|PubMed:12175490, ECO:0000312|WormBase:Y37D8A.9b};
GN ORFNames=Y37D8A.9 {ECO:0000312|WormBase:Y37D8A.9b};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
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, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=12175490; DOI=10.1016/s0925-4773(02)00058-8;
RA Fujita M., Takasaki T., Nakajima N., Kawano T., Shimura Y., Sakamoto H.;
RT "MRG-1, a mortality factor-related chromodomain protein, is required
RT maternally for primordial germ cells to initiate mitotic proliferation in
RT C. elegans.";
RL Mech. Dev. 114:61-69(2002).
RN [3] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=17215300; DOI=10.1242/dev.02771;
RA Takasaki T., Liu Z., Habara Y., Nishiwaki K., Nakayama J., Inoue K.,
RA Sakamoto H., Strome S.;
RT "MRG-1, an autosome-associated protein, silences X-linked genes and
RT protects germline immortality in Caenorhabditis elegans.";
RL Development 134:757-767(2007).
RN [4] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=22172672; DOI=10.1016/j.devcel.2011.09.019;
RA Dombecki C.R., Chiang A.C., Kang H.J., Bilgir C., Stefanski N.A.,
RA Neva B.J., Klerkx E.P., Nabeshima K.;
RT "The chromodomain protein MRG-1 facilitates SC-independent homologous
RT pairing during meiosis in Caenorhabditis elegans.";
RL Dev. Cell 21:1092-1103(2011).
RN [5] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22212480; DOI=10.1038/cr.2012.2;
RA Xu J., Sun X., Jing Y., Wang M., Liu K., Jian Y., Yang M., Cheng Z.,
RA Yang C.;
RT "MRG-1 is required for genomic integrity in Caenorhabditis elegans germ
RT cells.";
RL Cell Res. 22:886-902(2012).
RN [6] {ECO:0000305}
RP INTERACTION WITH RFP-1, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=25564623; DOI=10.1242/dev.115147;
RA Gupta P., Leahul L., Wang X., Wang C., Bakos B., Jasper K., Hansen D.;
RT "Proteasome regulation of the chromodomain protein MRG-1 controls the
RT balance between proliferative fate and differentiation in the C. elegans
RT germ line.";
RL Development 142:291-302(2015).
RN [7] {ECO:0000305}
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=30929290; DOI=10.1111/gtc.12683;
RA Miwa T., Inoue K., Sakamoto H.;
RT "MRG-1 is required for both chromatin-based transcriptional silencing and
RT genomic integrity of primordial germ cells in Caenorhabditis elegans.";
RL Genes Cells 24:377-389(2019).
RN [8] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=30425042; DOI=10.1534/genetics.118.301674;
RA Hajduskova M., Baytek G., Kolundzic E., Gosdschan A., Kazmierczak M.,
RA Ofenbauer A., Beato Del Rosal M.L., Herzog S., Ul Fatima N., Mertins P.,
RA Seelk-Muethel S., Tursun B.;
RT "MRG-1/MRG15 Is a Barrier for Germ Cell to Neuron Reprogramming in
RT Caenorhabditis elegans.";
RL Genetics 211:121-139(2019).
RN [9] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=31118512; DOI=10.1038/s41586-019-1243-y;
RA Cabianca D.S., Munoz-Jimenez C., Kalck V., Gaidatzis D., Padeken J.,
RA Seeber A., Askjaer P., Gasser S.M.;
RT "Active chromatin marks drive spatial sequestration of heterochromatin in
RT C. elegans nuclei.";
RL Nature 569:734-739(2019).
RN [10] {ECO:0000305}
RP IDENTIFICATION IN THE SIN3S COMPLEX, INTERACTION WITH CFP-1, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=31602465; DOI=10.1093/nar/gkz880;
RA Beurton F., Stempor P., Caron M., Appert A., Dong Y., Chen R.A., Cluet D.,
RA Coute Y., Herbette M., Huang N., Polveche H., Spichty M., Bedet C.,
RA Ahringer J., Palladino F.;
RT "Physical and functional interaction between SET1/COMPASS complex component
RT CFP-1 and a Sin3S HDAC complex in C. elegans.";
RL Nucleic Acids Res. 47:11164-11180(2019).
CC -!- FUNCTION: Protein involved in the remodeling of chromatin thereby
CC regulating various processes including transcription, chromosome
CC synapsis and genome integrity (PubMed:22172672, PubMed:22212480,
CC PubMed:17215300, PubMed:30929290). Mainly binds genomic loci carrying
CC trimethylated histone H3 'Lys-36' (H3K36me3) or 'Lys-4' (H3K4me3), and
CC acetylated histone H3 'Lys-9' (H3K9ac), 'Lys-27' (H3K27ac)
CC (PubMed:30425042, PubMed:31118512). During meiosis, required for the
CC presynaptic pairing of homologous chromosomal regions outside of the
CC pairing center and for the progression of chromosome synapsis
CC (PubMed:22172672, PubMed:22212480). Essential maternal factor required
CC in postembryonic germline development and in maintaining germ cell
CC identity (PubMed:12175490, PubMed:30425042). Plays an important role in
CC maintaining genomic integrity in primordial germ cells (PGCs) during
CC meiosis by regulating DNA double-strand break (DSB) repair and synapsis
CC (PubMed:22212480, PubMed:30929290). Also, required for chromatin-based
CC transcriptional silencing in PGCs and for silencing of X-linked genes
CC in the maternal germ line (PubMed:17215300, PubMed:30929290). By
CC retaining histone acetyltransferase, cbp-1, in euchromatin, promotes
CC the anchoring of heterochromatin at the inner nuclear membrane in
CC intestinal and hypodermal cells (PubMed:31118512).
CC {ECO:0000269|PubMed:12175490, ECO:0000269|PubMed:17215300,
CC ECO:0000269|PubMed:22172672, ECO:0000269|PubMed:22212480,
CC ECO:0000269|PubMed:30425042, ECO:0000269|PubMed:30929290,
CC ECO:0000269|PubMed:31118512}.
CC -!- SUBUNIT: Component of the SIN3S complex, which contains at least sin-3,
CC hda-1, athp-1 and mrg-1 (PubMed:31602465). Interacts with cfp-1, a
CC component of the SET2 complex (PubMed:31602465). Interacts with rfp-1
CC (PubMed:25564623). {ECO:0000269|PubMed:25564623,
CC ECO:0000269|PubMed:31602465}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17215300,
CC ECO:0000269|PubMed:22172672}. Chromosome {ECO:0000269|PubMed:17215300,
CC ECO:0000269|PubMed:31118512}. Note=Concentrated on euchromatic regions
CC marked by H3K36me2/me3 and probably enriched on autosomes.
CC {ECO:0000269|PubMed:17215300, ECO:0000269|PubMed:31118512}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=b {ECO:0000312|WormBase:Y37D8A.9b};
CC IsoId=A7DTF0-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:Y37D8A.9a};
CC IsoId=A7DTF0-2; Sequence=VSP_060821;
CC -!- TISSUE SPECIFICITY: Expressed in oocytes (at protein level)
CC (PubMed:12175490). Expressed mainly in germ cells, but also at lower
CC levels in several somatic cell types, including intestinal cells
CC (PubMed:17215300). {ECO:0000269|PubMed:12175490,
CC ECO:0000269|PubMed:17215300}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryos, L1 larvae and adult
CC hermaphrodites and decreases drastically between the L2 and L4 larval
CC stages (at protein level) (PubMed:12175490, PubMed:17215300). In late
CC embryos and young larvae, expressed at higher levels in the two
CC primordial germ cells (PGCs), Z2 and Z3, than in somatic blastomeres
CC (PubMed:17215300, PubMed:30929290). Expressed at a relatively constant
CC level throughout the distal end of the gonad at the L1 stage, with no
CC decrease as cells enter into meiotic prophase (PubMed:25564623).
CC {ECO:0000269|PubMed:12175490, ECO:0000269|PubMed:17215300,
CC ECO:0000269|PubMed:25564623, ECO:0000269|PubMed:30929290}.
CC -!- DISRUPTION PHENOTYPE: Maternal-effect lethality and sterility
CC (PubMed:17215300). Primordial germ cells (PGCs) do not proliferate
CC normally and death of germ cells may be as a result of necrosis or
CC increased apoptosis (PubMed:17215300, PubMed:22212480). Increased
CC proportion of oocytes with fragmented chromosomes as a result of
CC irradiation (PubMed:22212480). Tumorous germline phenotype that is
CC suppressed on a rfp-1;glp-1 double mutant background (PubMed:25564623).
CC Germline progression from leptotene/zygotene to pachytene is defective
CC (PubMed:22212480). Perinuclear anchoring of heterochromatin in
CC intestinal or hypodermal cells is disrupted and exacerbated on a cec-4
CC mutant background, but is partially blocked by RNAi-mediated knockdown
CC of cbp-1 or atf-8 (PubMed:31118512). RNAi-mediated knockdown causes
CC defective homologous chromosome pairing, complete absence of the
CC germline in almost all adult F1 progeny and slight underdevelopment of
CC the somatic gonad (PubMed:12175490, PubMed:22172672). RNAi-mediated
CC knockdown strongly blocks mitosis of PGCs at early larval stages, and
CC the arrested PGCs may degenerate during late larval stages
CC (PubMed:12175490). RNAi-mediated knockdown induces germ cells to
CC undergo conversion into neuron-like cells (PubMed:30425042). RNAi-
CC mediated knockdown causes a slight increase in levels of the
CC constitutive heterochromatin mark, trimethylated histone H3 'Lys-9'
CC (H3K9me3), and an increase of acetylated histone H3 'Lys-14' (H3K14ac)
CC (PubMed:30425042). Simultaneous RNAi-mediated knockdown of mep-1
CC suppresses the ectopic expression of pgl-1 protein and the
CC overexpression of pgl-1 mRNA in larvae (PubMed:17215300). RNAi-mediated
CC knockdown induces germ cell apoptosis; however, on clk-2 or cep-1
CC mutant backgrounds apoptosis is reduced substantially
CC (PubMed:22212480). {ECO:0000269|PubMed:12175490,
CC ECO:0000269|PubMed:17215300, ECO:0000269|PubMed:22172672,
CC ECO:0000269|PubMed:22212480, ECO:0000269|PubMed:25564623,
CC ECO:0000269|PubMed:30425042, ECO:0000269|PubMed:31118512}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BX284603; CAA21528.1; -; Genomic_DNA.
DR EMBL; BX284603; CAO82072.1; -; Genomic_DNA.
DR PIR; T26627; T26627.
DR RefSeq; NP_001122727.1; NM_001129255.2. [A7DTF0-1]
DR RefSeq; NP_499675.1; NM_067274.3. [A7DTF0-2]
DR AlphaFoldDB; A7DTF0; -.
DR SMR; A7DTF0; -.
DR IntAct; A7DTF0; 5.
DR STRING; 6239.Y37D8A.9b; -.
DR iPTMnet; A7DTF0; -.
DR EPD; A7DTF0; -.
DR PaxDb; A7DTF0; -.
DR PeptideAtlas; A7DTF0; -.
DR EnsemblMetazoa; Y37D8A.9a.1; Y37D8A.9a.1; WBGene00003406. [A7DTF0-2]
DR EnsemblMetazoa; Y37D8A.9b.1; Y37D8A.9b.1; WBGene00003406. [A7DTF0-1]
DR GeneID; 176702; -.
DR KEGG; cel:CELE_Y37D8A.9; -.
DR UCSC; Y37D8A.9b.1; c. elegans.
DR CTD; 176702; -.
DR WormBase; Y37D8A.9a; CE20213; WBGene00003406; mrg-1.
DR WormBase; Y37D8A.9b; CE41465; WBGene00003406; mrg-1.
DR eggNOG; KOG3001; Eukaryota.
DR GeneTree; ENSGT00950000182965; -.
DR HOGENOM; CLU_039566_0_0_1; -.
DR InParanoid; A7DTF0; -.
DR OMA; EYHWKAV; -.
DR OrthoDB; 1624495at2759; -.
DR PhylomeDB; A7DTF0; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00003406; Expressed in germ line (C elegans) and 4 other tissues.
DR ExpressionAtlas; A7DTF0; baseline and differential.
DR GO; GO:0030849; C:autosome; IDA:WormBase.
DR GO; GO:0000785; C:chromatin; IMP:UniProtKB.
DR GO; GO:0000791; C:euchromatin; IDA:UniProtKB.
DR GO; GO:0000123; C:histone acetyltransferase complex; IBA:GO_Central.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IBA:GO_Central.
DR GO; GO:0097240; P:chromosome attachment to the nuclear envelope; IMP:UniProtKB.
DR GO; GO:0070192; P:chromosome organization involved in meiotic cell cycle; IMP:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0007281; P:germ cell development; IMP:UniProtKB.
DR GO; GO:0031507; P:heterochromatin assembly; IMP:UniProtKB.
DR GO; GO:0016573; P:histone acetylation; IBA:GO_Central.
DR GO; GO:0016575; P:histone deacetylation; IBA:GO_Central.
DR GO; GO:0043968; P:histone H2A acetylation; IBA:GO_Central.
DR GO; GO:0043967; P:histone H4 acetylation; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:WormBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:WormBase.
DR GO; GO:1905632; P:protein localization to euchromatin; IMP:UniProtKB.
DR Gene3D; 1.10.274.30; -; 1.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR008676; MRG.
DR InterPro; IPR038217; MRG_C_sf.
DR InterPro; IPR026541; MRG_dom.
DR InterPro; IPR025995; Tudor-knot.
DR PANTHER; PTHR10880; PTHR10880; 1.
DR Pfam; PF05712; MRG; 1.
DR Pfam; PF11717; Tudor-knot; 1.
DR PIRSF; PIRSF038133; HAT_Nua4_EAF3/MRG15; 1.
DR SUPFAM; SSF54160; SSF54160; 1.
DR PROSITE; PS51640; MRG; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromatin regulator; Chromosome; DNA damage;
KW DNA repair; Meiosis; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..337
FT /note="Mortality factor related protein 1"
FT /id="PRO_0000451596"
FT DOMAIN 7..55
FT /note="Tudor-knot"
FT /evidence="ECO:0000255"
FT DOMAIN 122..327
FT /note="MRG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00972"
FT REGION 75..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 216..217
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_060821"
SQ SEQUENCE 337 AA; 38461 MW; 2D24E60DF73C1E5D CRC64;
MSSKKNFEVG ENVACIYKGK PYDAKITDIK TNSDGKELYC VHFKGWNNRY DEKIPVGEEK
DRIFKGTASE YAEKHNAELP TTALKPKKKS LAAEAPRDDR DDTPGTSKGK KAKSVTIAPV
MTADDMKVEL PKPLRKILID DYDLVCRYFI NIVPHEYSVD QIIEDYIKTI PVSNEQMRTV
DDLLIEYEEA DIKITNLALI CTARGLVDYF NVTLGSSYQL LYKFERPQYN DLVKKRAMEK
GIDITNPTAL QDSGFRPSQE YGIVHFLRML AKLPDYLKLT QWNDHVINRI MIGVHDLIVF
LNKNHGKYYR GSSDYQGASN DYYRRSLAAD DGVGANQ
