ID G1PIU9_MYOLU Unreviewed; 362 AA.
AC G1PIU9;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=WD repeat-containing protein 18 {ECO:0000256|ARBA:ARBA00021267, ECO:0000256|RuleBase:RU369067};
GN Name=WDR18 {ECO:0000313|Ensembl:ENSMLUP00000010650.2};
OS Myotis lucifugus (Little brown bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000010650.2, ECO:0000313|Proteomes:UP000001074};
RN [1] {ECO:0000313|Ensembl:ENSMLUP00000010650.2, ECO:0000313|Proteomes:UP000001074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSMLUP00000010650.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Functions as a component of the Five Friends of Methylated
CC CHTOP (5FMC) complex; the 5FMC complex is recruited to ZNF148 by
CC methylated CHTOP, leading to desumoylation of ZNF148 and subsequent
CC transactivation of ZNF148 target genes. Component of the PELP1 complex
CC involved in the nucleolar steps of 28S rRNA maturation and the
CC subsequent nucleoplasmic transit of the pre-60S ribosomal subunit. May
CC play a role during development. {ECO:0000256|RuleBase:RU369067}.
CC -!- SUBUNIT: Component of the 5FMC complex, at least composed of PELP1,
CC LAS1L, TEX10, WDR18 and SENP3; the complex interacts with methylated
CC CHTOP and ZNF148. Interacts with NOL9. Component of the PELP1 complex,
CC composed of at least PELP1, TEX10 and WDR18. The complex interacts with
CC pre-60S ribosome particles. {ECO:0000256|RuleBase:RU369067}.
CC -!- SUBCELLULAR LOCATION: Dynein axonemal particle
CC {ECO:0000256|ARBA:ARBA00024190, ECO:0000256|RuleBase:RU369067}.
CC Nucleus, nucleolus {ECO:0000256|RuleBase:RU369067}. Nucleus,
CC nucleoplasm {ECO:0000256|RuleBase:RU369067}. Cytoplasm
CC {ECO:0000256|RuleBase:RU369067}. Note=Mainly found in the nucleoplasm,
CC with low levels detected in the cytoplasmic and chromatin fractions.
CC {ECO:0000256|RuleBase:RU369067}.
CC -!- SIMILARITY: Belongs to the WD repeat IPI3/WDR18 family.
CC {ECO:0000256|RuleBase:RU369067}.
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DR EMBL; AAPE02043761; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G1PIU9; -.
DR STRING; 59463.ENSMLUP00000010650; -.
DR Ensembl; ENSMLUT00000011693.2; ENSMLUP00000010650.2; ENSMLUG00000011688.2.
DR eggNOG; KOG0646; Eukaryota.
DR GeneTree; ENSGT00390000000289; -.
DR HOGENOM; CLU_029749_0_0_1; -.
DR InParanoid; G1PIU9; -.
DR OMA; YIWIIAT; -.
DR TreeFam; TF313046; -.
DR Proteomes; UP000001074; Unassembled WGS sequence.
DR GO; GO:0120293; C:dynein axonemal particle; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-UniRule.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
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 InterPro; IPR045227; WDR18/Ipi3/RID3.
DR InterPro; IPR026987; Wdr18_C_dom.
DR PANTHER; PTHR18763:SF0; WD REPEAT-CONTAINING PROTEIN 18; 1.
DR PANTHER; PTHR18763; WD-REPEAT PROTEIN 18; 1.
DR Pfam; PF00400; WD40; 3.
DR Pfam; PF14077; WD40_alt; 1.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 4.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 3: Inferred from homology;
KW Nucleus {ECO:0000256|RuleBase:RU369067};
KW Reference proteome {ECO:0000313|Proteomes:UP000001074};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW rRNA processing {ECO:0000256|RuleBase:RU369067};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}.
FT REPEAT 47..80
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 119..141
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 195..236
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT DOMAIN 313..360
FT /note="WD repeat-containing protein 18 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14077"
SQ SEQUENCE 362 AA; 40121 MW; FD7CB03527A8A5A3 CRC64;
DQLQQKIMCP GPVTCLTTSP NGLYMLAGIA ESIYLWEVST GNLLVILSRH YQDISCLQFT
GDSSHFLSGG KDCLVLVWSL CSVLQVDSSR TPAPRHVWSH HTLPITDMHC GFGGPLARVA
TASLDQTVKL WEISSGELLL SVLFDVGIMA VTMDLAEHHM FCGGSEGSIF QVDLCTWPGQ
SEKSFQSEQD SGKVFKGHRN QVTCLSVSTD GSVLLSGSHD ETVRVWDIQS KQCIRTVTLK
GPVTNAFIML APVSMLSSDF RPSLPLPHFN KHLLGAEHGD EQRRGGLTLR LGLHQQGSEP
SYLERAEQLH MVMCSTMEKN VLGGQDQLRI RITELEDEVQ NLRKINRDLF DFSTRIITRP
TK
//
