WDR72_MOUSE
ID WDR72_MOUSE Reviewed; 1114 AA.
AC D3YYM4;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=WD repeat-containing protein 72 {ECO:0000250|UniProtKB:Q3MJ13};
GN Name=Wdr72 {ECO:0000312|MGI:MGI:3583957};
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 {ECO:0000312|Proteomes:UP000000589};
RN [1] {ECO:0000312|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000312|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2] {ECO:0000305}
RP TISSUE SPECIFICITY.
RX PubMed=19853237; DOI=10.1016/j.ajhg.2009.09.014;
RA El-Sayed W., Parry D.A., Shore R.C., Ahmed M., Jafri H., Rashid Y.,
RA Al-Bahlani S., Al Harasi S., Kirkham J., Inglehearn C.F., Mighell A.J.;
RT "Mutations in the beta propeller WDR72 cause autosomal-recessive
RT hypomaturation amelogenesis imperfecta.";
RL Am. J. Hum. Genet. 85:699-705(2009).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1093 AND SER-1095, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
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] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=25008349; DOI=10.1016/j.matbio.2014.06.005;
RA Katsura K.A., Horst J.A., Chandra D., Le T.Q., Nakano Y., Zhang Y.,
RA Horst O.V., Zhu L., Le M.H., DenBesten P.K.;
RT "WDR72 models of structure and function: a stage-specific regulator of
RT enamel mineralization.";
RL Matrix Biol. 38:48-58(2014).
RN [5] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26247047; DOI=10.1002/mgg3.143;
RA Wang S.K., Hu Y., Yang J., Smith C.E., Nunez S.M., Richardson A.S., Pal S.,
RA Samann A.C., Hu J.C., Simmer J.P.;
RT "Critical roles for WDR72 in calcium transport and matrix protein removal
RT during enamel maturation.";
RL Mol. Genet. Genomic Med. 3:302-319(2015).
CC -!- FUNCTION: Plays a major role in formation of tooth enamel
CC (PubMed:25008349, PubMed:26247047). Specifically required during the
CC maturation phase of amelogenesis for normal formation of the enamel
CC matrix and clearance of enamel proteins (PubMed:25008349,
CC PubMed:26247047). May be involved in localization of the calcium
CC transporter SLC24A4 to the ameloblast cell membrane (PubMed:26247047).
CC {ECO:0000269|PubMed:25008349, ECO:0000269|PubMed:26247047}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle
CC {ECO:0000269|PubMed:25008349}.
CC -!- TISSUE SPECIFICITY: Expressed in maturation stage ameloblasts (at
CC protein level) (PubMed:19853237, PubMed:25008349).
CC -!- DISRUPTION PHENOTYPE: Viable with no gross morpholgical defects
CC (PubMed:25008349, PubMed:26247047). At 6-7 weeks of age teeth have an
CC opaque, chalky appearance, with reduced enamel thickness at occlusal
CC surfaces (PubMed:25008349, PubMed:26247047). Body weight is reduced,
CC probably due to problems with chewing hard foods (PubMed:25008349).
CC Enamel formation is abnormal from the maturation stage onwards with
CC significantly reduced mineral density and retention of proteinaceous
CC material in the enamel matrix (PubMed:25008349, PubMed:26247047). Tooth
CC enamel hardness is ten times lower than wild type (PubMed:26247047).
CC Attachment of ameloblasts to the enamel layer may be weakened
CC (PubMed:26247047). The calcium transporter SLC24A4 fails to localize to
CC the distal ameloblast membrane (PubMed:26247047). In maturation stage
CC ameloblasts expression levels of amelogenin appear to be reduced,
CC although abnormally high amelogenin levels are found in the
CC extracellular enamel matrix (PubMed:25008349, PubMed:26247047).
CC {ECO:0000269|PubMed:25008349, ECO:0000269|PubMed:26247047}.
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DR EMBL; AC108944; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC111087; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS23338.2; -.
DR RefSeq; NP_001028672.2; NM_001033500.3.
DR RefSeq; XP_006511342.1; XM_006511279.2.
DR AlphaFoldDB; D3YYM4; -.
DR STRING; 10090.ENSMUSP00000057320; -.
DR iPTMnet; D3YYM4; -.
DR PhosphoSitePlus; D3YYM4; -.
DR MaxQB; D3YYM4; -.
DR PaxDb; D3YYM4; -.
DR PRIDE; D3YYM4; -.
DR ProteomicsDB; 299750; -.
DR Antibodypedia; 68374; 13 antibodies from 5 providers.
DR Ensembl; ENSMUST00000055879; ENSMUSP00000057320; ENSMUSG00000044976.
DR GeneID; 546144; -.
DR KEGG; mmu:546144; -.
DR UCSC; uc009qre.1; mouse.
DR CTD; 256764; -.
DR MGI; MGI:3583957; Wdr72.
DR VEuPathDB; HostDB:ENSMUSG00000044976; -.
DR eggNOG; KOG4155; Eukaryota.
DR GeneTree; ENSGT00940000160298; -.
DR HOGENOM; CLU_004362_0_0_1; -.
DR InParanoid; D3YYM4; -.
DR OMA; CTEFCKS; -.
DR OrthoDB; 84170at2759; -.
DR PhylomeDB; D3YYM4; -.
DR TreeFam; TF313196; -.
DR BioGRID-ORCS; 546144; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Wdr72; mouse.
DR PRO; PR:D3YYM4; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; D3YYM4; protein.
DR Bgee; ENSMUSG00000044976; Expressed in right kidney and 34 other tissues.
DR ExpressionAtlas; D3YYM4; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005768; C:endosome; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0070166; P:enamel mineralization; IMP:MGI.
DR GO; GO:0022617; P:extracellular matrix disassembly; IMP:MGI.
DR GO; GO:0072659; P:protein localization to plasma membrane; IMP:MGI.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR011044; Quino_amine_DH_bsu.
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 SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50969; SSF50969; 1.
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; 2.
PE 1: Evidence at protein level;
KW Biomineralization; Cytoplasmic vesicle; Phosphoprotein; Reference proteome;
KW Repeat; WD repeat.
FT CHAIN 1..1114
FT /note="WD repeat-containing protein 72"
FT /id="PRO_0000438188"
FT REPEAT 15..54
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 60..102
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 160..197
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 327..373
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT REPEAT 413..452
FT /note="WD 5"
FT /evidence="ECO:0000255"
FT REPEAT 470..515
FT /note="WD 6"
FT /evidence="ECO:0000255"
FT REPEAT 566..605
FT /note="WD 7"
FT /evidence="ECO:0000255"
FT REGION 634..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 749..798
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 749..773
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1093
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1095
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 1114 AA; 124410 MW; 209D3BF22B75E72C CRC64;
MRGALQAVAL WGRKAPPHSI TAIMITDDQQ TIVTGSQEGQ LCLWSLSPEL KISAKELLFG
HSASVTCLAR ARDFSKQPYV VSAAENGEMC MWNVSSGQCV EKTSLPYRHT AICYYHCSFR
MTGEGWLLCC GEYQDVLVLD AGTLAVLHTF TSLQSPDWMK CMCIVHSVRI QEDSLLVVSI
TGELKVWDLS SSINSIQEKQ DVHEKESKFL DSFNCQTIRF CPYTERLLLV VFSKCWKIYD
YCDFSLLWTE VSRDGQFFAG GEVLAAHRIL VWTEDGHSYI YQLLNRWAQM GATLRTFSGL
SKCVCPADGG VLKGTVYPHL LCSTSVEENK SLHFVMGYMN ERKEPFYKVL FSGEVSGRIT
LWHIPDVPIS KFDGSPREIP ITTTWTLQDN FDKHQMVSQS ITDHFSGSRD EVGMTATITS
SEYIPNLDKL ICGCEDGTIF ITKALNAAKA GLLEGDSLLK DSPCHTLLRG HHQSVTSLLY
PHNLASKLDQ SWMVSGDRGS YVILWDIFTE EILHTFFLEA GPVTRLLMSP ENLKRSDGQI
LCCVCGDHSV ALLHLEGRRC LLRARKHLFP VRMIRWHPVE NFLIVGCTDD SVYIWEIETG
TLERHETGER ARIILNCGDD AQLIRSEPTL SVASETHKHK SIEQKSSNSH QPGPVPCPSV
QLESSCKVAD ASSVPRPFNV LPVKTKWSHI GFHVLLFDLE NLVELLLPTP LSDVDPSGSF
YGGDILRRAK STVEKKTLTI RRNKASCSSL QTEAQAKPSG DSLVLGDSTS KFSEENNGIK
RQKKMKSSKK AHPKPPRKVD ASLTIDMAKL FLSCILPWGV DKDLDSLCTR HLSILKLQGP
VSLGLASNED LFSLMLPGWD ACSTEMKEYS GVNLCSRKVL DLSSKYTATL LHQTGIPRGL
ESHCDSVQQS DAIVYLLSRL FLVNKLVNMP LDLACEIDRP FKMETVHSKA RFPGSDILNI
SSFYGHPKNG GNECRAPEAD LSLLKLISCW RDQSVQVTEA IQAVLLAEVQ QHMKSLRNTP
VSSQPDPVAE HSICERMQIS AKMEWTEELE LQYVGKSSPL KTSVSPVKHG NDLNSANFQD
TEDILDRCVL EESESAGQPR HRPWIAKVCS CRMC
