MEP50_XENLA
ID MEP50_XENLA Reviewed; 333 AA.
AC Q6NUD0;
DT 24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Methylosome protein 50;
DE Short=MEP-50;
DE AltName: Full=WD repeat-containing protein 77;
GN Name=wdr77; Synonyms=mep50;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND TISSUE SPECIFICITY.
RX PubMed=22009756; DOI=10.1074/jbc.m111.303677;
RA Wilczek C., Chitta R., Woo E., Shabanowitz J., Chait B.T., Hunt D.F.,
RA Shechter D.;
RT "Protein arginine methyltransferase Prmt5-Mep50 methylates histones H2A and
RT H4 and the histone chaperone nucleoplasmin in Xenopus laevis eggs.";
RL J. Biol. Chem. 286:42221-42231(2011).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) IN COMPLEX WITH PRMT5, ELECTRON
RP MICROSCOPY, FUNCTION, AND SUBUNIT.
RX PubMed=23451136; DOI=10.1371/journal.pone.0057008;
RA Ho M.C., Wilczek C., Bonanno J.B., Xing L., Seznec J., Matsui T.,
RA Carter L.G., Onikubo T., Kumar P.R., Chan M.K., Brenowitz M., Cheng R.H.,
RA Reimer U., Almo S.C., Shechter D.;
RT "Structure of the arginine methyltransferase PRMT5-MEP50 reveals a
RT mechanism for substrate specificity.";
RL PLoS ONE 8:E57008-E57008(2013).
CC -!- FUNCTION: Non-catalytic component of the 20S prmt5-containing
CC methyltransferase complex, which modifies specific arginines to
CC dimethylarginines in several spliceosomal Sm proteins and histones.
CC Required for normal prmt5 methyltransferase activity.
CC {ECO:0000269|PubMed:22009756, ECO:0000269|PubMed:23451136}.
CC -!- SUBUNIT: Heterotetramer; dimer of heterodimer with prmt5. Interacts
CC with histone h2a and h4 and with nucleoplasmin.
CC {ECO:0000269|PubMed:22009756, ECO:0000269|PubMed:23451136}.
CC -!- INTERACTION:
CC Q6NUD0; Q6NUA1: prmt5; NbExp=5; IntAct=EBI-21229433, EBI-21229405;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22009756}. Nucleus
CC {ECO:0000269|PubMed:22009756}. Note=Enriched on chromatin.
CC -!- TISSUE SPECIFICITY: Detected in egg (at protein level).
CC {ECO:0000269|PubMed:22009756}.
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DR EMBL; BC068665; AAH68665.1; -; mRNA.
DR RefSeq; NP_001084703.1; NM_001091234.1.
DR PDB; 4G56; X-ray; 2.95 A; B/D=2-333.
DR PDBsum; 4G56; -.
DR AlphaFoldDB; Q6NUD0; -.
DR SMR; Q6NUD0; -.
DR BioGRID; 101086; 3.
DR IntAct; Q6NUD0; 1.
DR MaxQB; Q6NUD0; -.
DR DNASU; 414664; -.
DR GeneID; 414664; -.
DR KEGG; xla:414664; -.
DR CTD; 414664; -.
DR Xenbase; XB-GENE-972901; wdr77.S.
DR OrthoDB; 774546at2759; -.
DR Proteomes; UP000186698; Chromosome 2S.
DR Bgee; 414664; Expressed in oocyte and 19 other tissues.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0035097; C:histone methyltransferase complex; IDA:UniProtKB.
DR GO; GO:0034709; C:methylosome; ISS:UniProtKB.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF00400; WD40; 2.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Nucleus; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..333
FT /note="Methylosome protein 50"
FT /id="PRO_0000422973"
FT REPEAT 16..59
FT /note="WD 1"
FT REPEAT 68..106
FT /note="WD 2"
FT REPEAT 113..152
FT /note="WD 3"
FT REPEAT 155..195
FT /note="WD 4"
FT REPEAT 199..240
FT /note="WD 5"
FT REPEAT 243..283
FT /note="WD 6"
FT REPEAT 285..328
FT /note="WD 7"
FT STRAND 19..26
FT /evidence="ECO:0007829|PDB:4G56"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:4G56"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:4G56"
FT STRAND 39..43
FT /evidence="ECO:0007829|PDB:4G56"
FT STRAND 46..53
FT /evidence="ECO:0007829|PDB:4G56"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:4G56"
FT STRAND 64..68
FT /evidence="ECO:0007829|PDB:4G56"
FT STRAND 73..79
FT /evidence="ECO:0007829|PDB:4G56"
FT TURN 80..82
FT /evidence="ECO:0007829|PDB:4G56"
FT STRAND 83..88
FT /evidence="ECO:0007829|PDB:4G56"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:4G56"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:4G56"
FT TURN 100..103
FT /evidence="ECO:0007829|PDB:4G56"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:4G56"
FT STRAND 118..123
FT /evidence="ECO:0007829|PDB:4G56"
FT STRAND 125..134
FT /evidence="ECO:0007829|PDB:4G56"
FT STRAND 139..143
FT /evidence="ECO:0007829|PDB:4G56"
FT TURN 144..147
FT /evidence="ECO:0007829|PDB:4G56"
FT STRAND 148..153
FT /evidence="ECO:0007829|PDB:4G56"
FT STRAND 160..165
FT /evidence="ECO:0007829|PDB:4G56"
FT STRAND 173..177
FT /evidence="ECO:0007829|PDB:4G56"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:4G56"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:4G56"
FT STRAND 205..210
FT /evidence="ECO:0007829|PDB:4G56"
FT STRAND 217..225
FT /evidence="ECO:0007829|PDB:4G56"
FT STRAND 227..233
FT /evidence="ECO:0007829|PDB:4G56"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:4G56"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:4G56"
FT STRAND 248..253
FT /evidence="ECO:0007829|PDB:4G56"
FT STRAND 255..258
FT /evidence="ECO:0007829|PDB:4G56"
FT STRAND 261..265
FT /evidence="ECO:0007829|PDB:4G56"
FT STRAND 270..273
FT /evidence="ECO:0007829|PDB:4G56"
FT STRAND 279..283
FT /evidence="ECO:0007829|PDB:4G56"
FT STRAND 290..295
FT /evidence="ECO:0007829|PDB:4G56"
FT STRAND 297..299
FT /evidence="ECO:0007829|PDB:4G56"
FT STRAND 302..307
FT /evidence="ECO:0007829|PDB:4G56"
FT STRAND 312..316
FT /evidence="ECO:0007829|PDB:4G56"
SQ SEQUENCE 333 AA; 36052 MW; 74673EB8C5765293 CRC64;
MSKGSAWGRP VTAPACMEVQ IGAVRYRRDG ALLLAASSLS SRTWGGSIWV FKDPEGAPNE
SLCTAGVQTE AGVTDVAWVS EKGILVASDS GAVELWEILE KESLLVNKFA KYEHDDIVKT
LSVFSDGTQA VSGGKDFSVK VWDLSQKAVL KSYNAHSSEV NCVAACPGKD TIFLSCGEDG
RILLWDTRKP KPATRIDFCA SDTIPTSVTW HPEKDDTFAC GDETGNVSLV NIKNPDSAQT
SAVHSQNITG LAYSYHSSPF LASISEDCTV AVLDADFSEV FRDLSHRDFV TGVAWSPLDH
SKFTTVGWDH KVLHHHLPSE GRTENLIATK AED
