ID MEP50_BOVIN Reviewed; 342 AA.
AC Q5E9I7;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 24-JAN-2024, entry version 104.
DE RecName: Full=Methylosome protein WDR77 {ECO:0000305};
DE AltName: Full=Methylosome protein 50 {ECO:0000250|UniProtKB:Q9BQA1};
DE Short=MEP-50 {ECO:0000250|UniProtKB:Q9BQA1};
DE AltName: Full=WD repeat-containing protein 77 {ECO:0000250|UniProtKB:Q9BQA1};
GN Name=WDR77 {ECO:0000250|UniProtKB:Q9BQA1};
GN Synonyms=MEP50 {ECO:0000250|UniProtKB:Q9BQA1};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
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 with
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 Interacts with TSC22D2 (By similarity). {ECO:0000250|UniProtKB:Q99J09,
CC ECO:0000250|UniProtKB:Q9BQA1}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9BQA1}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9BQA1}.
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DR EMBL; BT020933; AAX08950.1; -; mRNA.
DR EMBL; BC133485; AAI33486.1; -; mRNA.
DR RefSeq; NP_001015584.1; NM_001015584.1.
DR RefSeq; XP_015319200.1; XM_015463714.1.
DR AlphaFoldDB; Q5E9I7; -.
DR SMR; Q5E9I7; -.
DR STRING; 9913.ENSBTAP00000018753; -.
DR PaxDb; 9913-ENSBTAP00000018753; -.
DR Ensembl; ENSBTAT00000018753.4; ENSBTAP00000018753.4; ENSBTAG00000014102.4.
DR GeneID; 512993; -.
DR KEGG; bta:512993; -.
DR CTD; 79084; -.
DR VEuPathDB; HostDB:ENSBTAG00000014102; -.
DR VGNC; VGNC:36921; WDR77.
DR eggNOG; KOG0284; Eukaryota.
DR GeneTree; ENSGT00390000010711; -.
DR InParanoid; Q5E9I7; -.
DR OMA; QMGCNAS; -.
DR OrthoDB; 810251at2759; -.
DR Reactome; R-BTA-191859; snRNP Assembly.
DR Reactome; R-BTA-3214858; RMTs methylate histone arginines.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000014102; Expressed in oviduct epithelium and 105 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0034709; C:methylosome; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0008327; F:methyl-CpG binding; ISS:UniProtKB.
DR GO; GO:0007309; P:oocyte axis specification; IBA:GO_Central.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR46853; METHYLOSOME PROTEIN 50; 1.
DR PANTHER; PTHR46853:SF3; METHYLOSOME PROTEIN 50; 1.
DR Pfam; PF00400; WD40; 2.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Nucleus; Phosphoprotein; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..342
FT /note="Methylosome protein WDR77"
FT /id="PRO_0000331607"
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="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQA1"
SQ SEQUENCE 342 AA; 36789 MW; DDEF9A26BEDC0611 CRC64;
MRKETPPPLV PPAAREWNLP PNAPACMERQ LEAARYRSDG ALLLGASSLS GRCWAGSLWL
FKDPCAAPNE GFCSAGVQTE AGVADLTWVG DRGILVASDS GAVELWELDE NETLIVSKFC
KYEHDDIVST VSVLSSGTHA VSGSKDFCIK VWDLAQQMVL NSYRAHSGQV TCVAASPHKD
SVFLSCGEDN RILLWDTRCP KPASQMGCSA SGYLPTSLTW HPQQSEVFVF GDENGTVSLV
DTKSAGCAVS SVVHSQCVTG LVFSPHSAPF LASVSEDCSL AVLDSGLSEV FRSRAHRDFV
RDATWSPLNH SLLTTVGWDH QVIHHILPTE PLPEPGPKSA AE
//
