ID   MEP50_RAT               Reviewed;         342 AA.
AC   Q4QR85;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Methylosome protein 50;
DE            Short=MEP-50;
DE   AltName: Full=WD repeat-containing protein 77;
GN   Name=Wdr77; Synonyms=Mep50;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Placenta;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PROTEIN SEQUENCE OF 3-15; 180-198 AND 244-260, PHOSPHORYLATION AT SER-5,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Fibroblast;
RA   Bienvenut W.V., von Kriegsheim A., Kolch W.;
RL   Submitted (JUN-2009) to UniProtKB.
CC   -!- FUNCTION: Non-catalytic component of the methylosome complex, composed
CC       of PRMT5, WDR77 and CLNS1A, which modifies specific arginines to
CC       dimethylarginines in several spliceosomal Sm proteins and histones.
CC       This modification targets Sm proteins to the survival of motor neurons
CC       (SMN) complex for assembly into small nuclear ribonucleoprotein core
CC       particles. Might play a role in transcription regulation. The
CC       methylosome complex also methylates the Piwi proteins (PIWIL1, PIWIL2
CC       and PIWIL4), methylation of Piwi proteins being required for the
CC       interaction with Tudor domain-containing proteins and subsequent
CC       localization to the meiotic nuage. {ECO:0000250|UniProtKB:Q99J09,
CC       ECO:0000250|UniProtKB:Q9BQA1}.
CC   -!- SUBUNIT: Component of the methylosome complex composed of PRMT5, WDR77
CC       and CLNS1A (By similarity). Found in a complex composed of PRMT5, WDR77
CC       and RIOK1 (By similarity). RIOK1 and CLNS1A bound directly to PRMT5 at
CC       the same binding site, in a mutually exclusive manner, which allows the
CC       recruitment of distinct methylation substrates, such as nucleolin/NCL
CC       and Sm proteins, respectively (By similarity). Found in a complex wit
CC       the component of the methylosome, PRMT5, CLNS1A, WDR77, PRMT1 and ERH.
CC       Directly interacts with PRMT5, as well as with several Sm proteins,
CC       including SNRPB and SNRPD2 and, more weakly, SNRPD3 and SNRPE. Forms a
CC       compact hetero-octamer with PRMT5, decorating the outer surface of a
CC       PRMT5 tetramer. Interacts with SUZ12 and histone H2A/H2AC20, but not
CC       with histones H2B, H3 nor H4. Interacts with CTDP1 and LSM11. Interacts
CC       with APEX1, AR and NKX3-1. Interacts with CHTOP. Interacts with FAM47E.
CC       {ECO:0000250|UniProtKB:Q99J09, ECO:0000250|UniProtKB:Q9BQA1}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9BQA1}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q9BQA1}.
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DR   EMBL; BC097367; AAH97367.1; -; mRNA.
DR   RefSeq; NP_001008771.2; NM_001008771.3.
DR   RefSeq; XP_017446815.1; XM_017591326.1.
DR   AlphaFoldDB; Q4QR85; -.
DR   SMR; Q4QR85; -.
DR   STRING; 10116.ENSRNOP00000022571; -.
DR   iPTMnet; Q4QR85; -.
DR   PhosphoSitePlus; Q4QR85; -.
DR   jPOST; Q4QR85; -.
DR   PaxDb; Q4QR85; -.
DR   PRIDE; Q4QR85; -.
DR   Ensembl; ENSRNOT00000076654; ENSRNOP00000068445; ENSRNOG00000016394.
DR   GeneID; 310769; -.
DR   KEGG; rno:310769; -.
DR   UCSC; RGD:1310479; rat.
DR   CTD; 79084; -.
DR   RGD; 1310479; Wdr77.
DR   eggNOG; KOG0284; Eukaryota.
DR   GeneTree; ENSGT00390000010711; -.
DR   HOGENOM; CLU_051285_0_0_1; -.
DR   InParanoid; Q4QR85; -.
DR   OrthoDB; 774546at2759; -.
DR   Reactome; R-RNO-191859; snRNP Assembly.
DR   Reactome; R-RNO-3214858; RMTs methylate histone arginines.
DR   PRO; PR:Q4QR85; -.
DR   Proteomes; UP000002494; Chromosome 2.
DR   Bgee; ENSRNOG00000016394; Expressed in skeletal muscle tissue and 20 other tissues.
DR   ExpressionAtlas; Q4QR85; baseline and differential.
DR   Genevisible; Q4QR85; RN.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR   GO; GO:0034709; C:methylosome; ISS:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0008327; F:methyl-CpG binding; ISS:UniProtKB.
DR   GO; GO:0030374; F:nuclear receptor coactivator activity; ISO:RGD.
DR   GO; GO:0060767; P:epithelial cell proliferation involved in prostate gland development; IEA:Ensembl.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:RGD.
DR   GO; GO:0060770; P:negative regulation of epithelial cell proliferation involved in prostate gland development; ISO:RGD.
DR   GO; GO:0007309; P:oocyte axis specification; IBA:GO_Central.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:RGD.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:RGD.
DR   GO; GO:0060528; P:secretory columnal luminar epithelial cell differentiation involved in prostate glandular acinus development; ISO:RGD.
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   Cytoplasm; Direct protein sequencing; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat; WD repeat.
FT   CHAIN           1..342
FT                   /note="Methylosome protein 50"
FT                   /id="PRO_0000331609"
FT   REPEAT          22..75
FT                   /note="WD 1"
FT   REPEAT          78..116
FT                   /note="WD 2"
FT   REPEAT          123..162
FT                   /note="WD 3"
FT   REPEAT          165..205
FT                   /note="WD 4"
FT   REPEAT          209..250
FT                   /note="WD 5"
FT   REPEAT          253..293
FT                   /note="WD 6"
FT   REPEAT          295..330
FT                   /note="WD 7"
FT   MOD_RES         5
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|Ref.2"
SQ   SEQUENCE   342 AA;  37076 MW;  E0BC151387C5AE61 CRC64;
     MRKESPPPLV PPAAREWNLP PNAPACMERQ LEAARYRSDG SLLLGASSLS GRCWAGSLWF
     FKDPSAAPNE GFCSAGVQTE AGVADLTWVG DKGILVASDS GAVELWELDE NETLIVSKFC
     KYEHDDIVST VTVLSSGTQA VSGSKDFCIK IWDLAQQMSL NSYRAHAGQV TCVAASPHRE
     TVFLSCSEDS RILLWDTRCP KPASQMGCNA SGYLPTSLAW HPQQSEIFVF GDENGSVSLV
     DTKNASCTLS SAVHSQCVTR LVFSPHSVPF LASLSEDCSL AVLDSSFSEV FRSRAHRDFV
     RDATWSPLNH SLLTTVGWDH QVIHHVVPLE PLPAPGPDSV VE