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 07-APR-2021, entry version 78. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 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. 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 eggNOG; KOG4155; Eukaryota. DR GeneTree; ENSGT00940000160298; -. DR HOGENOM; CLU_004362_0_0_1; -. DR InParanoid; D3YYM4; -. DR OMA; SPGNDIL; -. DR OrthoDB; 84170at2759; -. DR PhylomeDB; D3YYM4; -. DR TreeFam; TF313196; -. DR BioGRID-ORCS; 546144; 0 hits in 52 CRISPR screens. DR ChiTaRS; Wdr72; mouse. DR PRO; PR:D3YYM4; -. DR Proteomes; UP000000589; Chromosome 9. DR RNAct; D3YYM4; protein. DR Bgee; ENSMUSG00000044976; Expressed in adult mammalian kidney and 43 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: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; IPR017986; WD40_repeat_dom. 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 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 //