WDR43_MOUSE
ID WDR43_MOUSE Reviewed; 677 AA.
AC Q6ZQL4; Q3U895;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=WD repeat-containing protein 43;
GN Name=Wdr43; Synonyms=Kiaa0007;
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=Bone marrow;
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] OF 13-677.
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [3]
RP FUNCTION, RNA-BINDING, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, DOMAIN,
RP AND INTERACTION WITH CDK9; DDX21 AND SUPT6H.
RX PubMed=31128943; DOI=10.1016/j.molcel.2019.05.007;
RA Bi X., Xu Y., Li T., Li X., Li W., Shao W., Wang K., Zhan G., Wu Z.,
RA Liu W., Lu J.Y., Wang L., Zhao J., Wu J., Na J., Li G., Li P., Shen X.;
RT "RNA Targets Ribogenesis Factor WDR43 to Chromatin for Transcription and
RT Pluripotency Control.";
RL Mol. Cell 0:0-0(2019).
CC -!- FUNCTION: Ribosome biogenesis factor that coordinates hyperactive
CC transcription and ribogenesis (PubMed:31128943). Involved in nucleolar
CC processing of pre-18S ribosomal RNA. Required for optimal pre-ribosomal
CC RNA transcription by RNA polymerase I (By similarity). Essential for
CC stem cell pluripotency and embryonic development (PubMed:31128943). In
CC the nucleoplasm, recruited by promoter-associated/nascent transcripts
CC and transcription to active promoters where it facilitates releases of
CC elongation factor P-TEFb and paused RNA polymerase II to allow
CC transcription elongation and maintain high-level expression of its
CC targets genes (PubMed:31128943). {ECO:0000250|UniProtKB:Q15061,
CC ECO:0000269|PubMed:31128943}.
CC -!- SUBUNIT: Interacts with UTP4 and UTP15. May be a component of the
CC proposed t-UTP subcomplex of the ribosomal small subunit (SSU)
CC processome containing at least UTP4, WDR43, HEATR1, UTP15, WDR75. Binds
CC to RNA; binding is required for its chromatin association
CC (PubMed:31128943). Interacts with CDK9, DDX21 and SUPT6H
CC (PubMed:31128943). Interacts with RNA polymerase II (PubMed:31128943).
CC {ECO:0000250|UniProtKB:Q15061, ECO:0000269|PubMed:31128943}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:31128943}.
CC Nucleus, nucleolus fibrillar center {ECO:0000250|UniProtKB:Q15061}.
CC Nucleus, nucleoplasm {ECO:0000269|PubMed:31128943}.
CC -!- TISSUE SPECIFICITY: Detected at low levels at least in heart, liver,
CC lung, spleen, thymus and hippocampus. {ECO:0000269|PubMed:31128943}.
CC -!- DEVELOPMENTAL STAGE: Expressed during embryonic development, expression
CC decreases at morula stage. {ECO:0000269|PubMed:31128943}.
CC -!- DOMAIN: N-terminal domain is required for nucleoplasm location and C-
CC terminal domain for nucleolus location. {ECO:0000269|PubMed:31128943}.
CC -!- SIMILARITY: Belongs to the UTP5 family. {ECO:0000305}.
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DR EMBL; AK152321; BAE31123.1; -; mRNA.
DR EMBL; AK129031; BAC97841.1; -; mRNA.
DR CCDS; CCDS50180.1; -.
DR RefSeq; NP_783570.1; NM_175639.1.
DR AlphaFoldDB; Q6ZQL4; -.
DR SMR; Q6ZQL4; -.
DR BioGRID; 215412; 48.
DR STRING; 10090.ENSMUSP00000048337; -.
DR iPTMnet; Q6ZQL4; -.
DR PhosphoSitePlus; Q6ZQL4; -.
DR SwissPalm; Q6ZQL4; -.
DR EPD; Q6ZQL4; -.
DR MaxQB; Q6ZQL4; -.
DR PaxDb; Q6ZQL4; -.
DR PeptideAtlas; Q6ZQL4; -.
DR PRIDE; Q6ZQL4; -.
DR ProteomicsDB; 299970; -.
DR Antibodypedia; 51059; 77 antibodies from 15 providers.
DR Ensembl; ENSMUST00000047086; ENSMUSP00000048337; ENSMUSG00000041057.
DR GeneID; 72515; -.
DR KEGG; mmu:72515; -.
DR UCSC; uc008dms.2; mouse.
DR CTD; 23160; -.
DR MGI; MGI:1919765; Wdr43.
DR VEuPathDB; HostDB:ENSMUSG00000041057; -.
DR eggNOG; KOG4547; Eukaryota.
DR GeneTree; ENSGT00390000004254; -.
DR HOGENOM; CLU_020516_1_0_1; -.
DR InParanoid; Q6ZQL4; -.
DR OMA; KRNADNH; -.
DR OrthoDB; 1032141at2759; -.
DR PhylomeDB; Q6ZQL4; -.
DR TreeFam; TF313160; -.
DR Reactome; R-MMU-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR BioGRID-ORCS; 72515; 27 hits in 71 CRISPR screens.
DR ChiTaRS; Wdr43; mouse.
DR PRO; PR:Q6ZQL4; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q6ZQL4; protein.
DR Bgee; ENSMUSG00000041057; Expressed in embryonic post-anal tail and 274 other tissues.
DR ExpressionAtlas; Q6ZQL4; baseline and differential.
DR Genevisible; Q6ZQL4; MM.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0001650; C:fibrillar center; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000993; F:RNA polymerase II complex binding; IDA:UniProtKB.
DR GO; GO:0003711; F:transcription elongation regulator activity; IMP:UniProtKB.
DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR GO; GO:2000234; P:positive regulation of rRNA processing; ISO:MGI.
DR GO; GO:0045943; P:positive regulation of transcription by RNA polymerase I; ISO:MGI.
DR GO; GO:2000036; P:regulation of stem cell population maintenance; IMP:UniProtKB.
DR GO; GO:0034243; P:regulation of transcription elongation from RNA polymerase II promoter; IMP:UniProtKB.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR007148; SSU_processome_Utp12.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF04003; Utp12; 1.
DR Pfam; PF00400; WD40; 2.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Ribosome biogenesis; RNA-binding; rRNA processing; Transcription;
KW Transcription regulation; Ubl conjugation; WD repeat.
FT CHAIN 1..677
FT /note="WD repeat-containing protein 43"
FT /id="PRO_0000051393"
FT REPEAT 13..51
FT /note="WD 1"
FT REPEAT 57..119
FT /note="WD 2"
FT REPEAT 124..163
FT /note="WD 3"
FT REPEAT 166..205
FT /note="WD 4"
FT REPEAT 207..258
FT /note="WD 5"
FT REPEAT 266..308
FT /note="WD 6"
FT REGION 581..677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..652
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..667
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15061"
FT MOD_RES 320
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q15061"
FT MOD_RES 393
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q15061"
FT MOD_RES 398
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15061"
FT MOD_RES 588
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15061"
FT MOD_RES 658
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15061"
FT CROSSLNK 308
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q15061"
FT CROSSLNK 308
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q15061"
SQ SEQUENCE 677 AA; 75381 MW; 794B650FD87E9547 CRC64;
MAAGGGGSYD PLAPAGVPCA FSPDSQAYFA LASSDGQLRV WETANNRLHQ EYVPSAHLSG
TCTCLAWAPA RLQAKESHQR KKRKSEVTGT KDQADLLALG TAVGSILLYS TVRGELHSKL
TSGGHENRVN CIQWHQDNDC LYSCSDDKYI VEWSTQTCKV KCKWKGDNSS VSSLCISPDG
KMLLSAGRTI KLWVLETKEV YRHFTGHATP VSSLRFTTIR PNESQPSDGI TGLYFLSGAV
HDRLLNVWQV RSENKEKSAV MSFTVTDEPV YVDLTLSENK EEPVKLAVVC RDGQVHLFEH
ILNGHCKKPL TSNCTIQIAT PGKGKKVTPK PIPILAASFC LDKMSLLLVY GNWFQPTIER
VALNSKDTHI CLERDISNCW APTVETAITK VKTPVMNSEA KVLVPGIPGH HAPIKLPPAQ
PKEAENKRKL GSTEATIEER LGAMDLDRKG RKDDLQTNSF AVLLTQGLES NDFEILNKVL
QTKNVNLIKR TVLRIPLRVV IPLLQELTKR LQGHPNSAAL MIQWLKCVLT IHASYLSTLP
DLVEQLGTLY QLMESRVKTF QKLSNLHGKL ILLVTQVTAS EKSKKMTSPG QKAKLVYEEE
SSEEESDDEV PEKDSDDNWD EDEDKDSEKD EGVDEDNEEE DEDMEDKEEN EEDREVSSEK
ELNGDSDLDP ENESEEE
