WDR18_MOUSE
ID WDR18_MOUSE Reviewed; 431 AA.
AC Q4VBE8;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=WD repeat-containing protein 18;
GN Name=Wdr18;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head, and Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NMRI; TISSUE=Mammary tumor;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP FUNCTION, IDENTIFICATION IN THE 5FMC COMPLEX, INTERACTION OF THE 5FMC
RP COMPLEX WITH CHTOP AND ZNF148, INTERACTION WITH NOL9, AND SUBCELLULAR
RP LOCATION.
RX PubMed=22872859; DOI=10.1074/mcp.m112.017194;
RA Fanis P., Gillemans N., Aghajanirefah A., Pourfarzad F., Demmers J.,
RA Esteghamat F., Vadlamudi R.K., Grosveld F., Philipsen S., van Dijk T.B.;
RT "Five friends of methylated chromatin target of protein-arginine-
RT methyltransferase[prmt]-1 (chtop), a complex linking arginine methylation
RT to desumoylation.";
RL Mol. Cell. Proteomics 11:1263-1273(2012).
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 (PubMed:22872859). Component of
CC the PELP1 complex involved in the nucleolar steps of 28S rRNA
CC maturation and the subsequent nucleoplasmic transit of the pre-60S
CC ribosomal subunit (By similarity). May play a role during development
CC (By similarity). {ECO:0000250|UniProtKB:Q68EI0,
CC ECO:0000250|UniProtKB:Q9BV38, ECO:0000269|PubMed:22872859}.
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 (PubMed:22872859). Component of
CC the PELP1 complex, composed of at least PELP1, TEX10 and WDR18. The
CC complex interacts with pre-60S ribosome particles (By similarity).
CC {ECO:0000250|UniProtKB:Q9BV38, ECO:0000269|PubMed:22872859}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q9BV38}. Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:22872859}. Cytoplasm {ECO:0000269|PubMed:22872859}.
CC Dynein axonemal particle {ECO:0000250|UniProtKB:A0A1L8HX76}.
CC Note=Mainly found in the nucleoplasm, with low levels detected in the
CC cytoplasmic and chromatin fractions. {ECO:0000269|PubMed:22872859}.
CC -!- SIMILARITY: Belongs to the WD repeat IPI3/WDR18 family. {ECO:0000305}.
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DR EMBL; AK133716; BAE21796.1; -; mRNA.
DR EMBL; AK160713; BAE35966.1; -; mRNA.
DR EMBL; AK168691; BAE40536.1; -; mRNA.
DR EMBL; BC095984; AAH95984.1; -; mRNA.
DR CCDS; CCDS24000.1; -.
DR RefSeq; NP_780659.2; NM_175450.4.
DR AlphaFoldDB; Q4VBE8; -.
DR SMR; Q4VBE8; -.
DR BioGRID; 229710; 9.
DR IntAct; Q4VBE8; 1.
DR STRING; 10090.ENSMUSP00000041049; -.
DR iPTMnet; Q4VBE8; -.
DR PhosphoSitePlus; Q4VBE8; -.
DR EPD; Q4VBE8; -.
DR MaxQB; Q4VBE8; -.
DR PaxDb; Q4VBE8; -.
DR PeptideAtlas; Q4VBE8; -.
DR PRIDE; Q4VBE8; -.
DR ProteomicsDB; 297938; -.
DR Antibodypedia; 22464; 149 antibodies from 27 providers.
DR DNASU; 216156; -.
DR Ensembl; ENSMUST00000045247; ENSMUSP00000041049; ENSMUSG00000035754.
DR GeneID; 216156; -.
DR KEGG; mmu:216156; -.
DR UCSC; uc007gat.1; mouse.
DR CTD; 57418; -.
DR MGI; MGI:2158400; Wdr18.
DR VEuPathDB; HostDB:ENSMUSG00000035754; -.
DR eggNOG; KOG0646; Eukaryota.
DR GeneTree; ENSGT00390000000289; -.
DR HOGENOM; CLU_029749_0_0_1; -.
DR InParanoid; Q4VBE8; -.
DR OMA; VNARIYT; -.
DR OrthoDB; 747023at2759; -.
DR PhylomeDB; Q4VBE8; -.
DR TreeFam; TF313046; -.
DR Reactome; R-MMU-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR BioGRID-ORCS; 216156; 27 hits in 74 CRISPR screens.
DR ChiTaRS; Wdr18; mouse.
DR PRO; PR:Q4VBE8; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q4VBE8; protein.
DR Bgee; ENSMUSG00000035754; Expressed in epiblast (generic) and 205 other tissues.
DR Genevisible; Q4VBE8; MM.
DR GO; GO:0120293; C:dynein axonemal particle; ISS:UniProtKB.
DR GO; GO:0005656; C:nuclear pre-replicative complex; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0097344; C:Rix1 complex; IBA:GO_Central.
DR GO; GO:0006261; P:DNA-templated DNA replication; IBA:GO_Central.
DR GO; GO:0006364; P:rRNA processing; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
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 InterPro; IPR045227; WDR18/Ipi3/RID3.
DR InterPro; IPR026987; Wdr18_C_dom.
DR PANTHER; PTHR18763; PTHR18763; 1.
DR Pfam; PF00400; WD40; 2.
DR Pfam; PF14077; WD40_alt; 1.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Developmental protein; Nucleus; Reference proteome; Repeat;
KW WD repeat.
FT CHAIN 1..431
FT /note="WD repeat-containing protein 18"
FT /id="PRO_0000233181"
FT REPEAT 36..75
FT /note="WD 1"
FT REPEAT 78..116
FT /note="WD 2"
FT REPEAT 119..158
FT /note="WD 3"
FT REPEAT 170..211
FT /note="WD 4"
FT REPEAT 213..257
FT /note="WD 5"
FT REPEAT 267..306
FT /note="WD 6"
SQ SEQUENCE 431 AA; 47211 MW; 0999A3469F3FD64A CRC64;
MAAPMEVVVC TDAAAQLWSC VVWELHSGAN LLTYRGGQAG PRGLALLNGE YLLAAQQGKN
YICAWELQRK DQLQQKIMCP GPVTCLTTAP NGLYVLAGIA ESIYLWEVCT GNLLVILSRH
YQDVSCLKFT GDGSHFVSAG KDCLALAWSL CSVLQADPSR ILAPRHVWSQ HTLPITDLHC
GFGGPMARVA TASLDQTVKL WAISSGDLLL SVLFDMGITS VTMDLAEHHI FCGGSDGSIF
QVDLCSWPGL REHSFQPEQN TGKVFKGHRN QVTCLSVSTD GSVLLSGSHD ESVRLWDVKS
KQCLRTVTLK GPVTNAAIIL APPSMLNPEF RPSLPLPHFN KHLLGAEHGD EAQGGGLRLQ
LGLHLQGKEP SYLERLEQLQ AVLSSYLEKN MLGSQMLPAR VFDLEDEVRS LRKINRDLFD
FSTRIITRPS K
