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 12-SEP-2018, entry version 65. 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; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; 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., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the 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., RA 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 RT 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., RA Pal S., Samann A.C., Hu J.C., Simmer J.P.; RT "Critical roles for WDR72 in calcium transport and matrix protein RT removal 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 CC the maturation phase of amelogenesis for normal formation of the CC enamel 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 CC (PubMed:26247047). {ECO:0000269|PubMed:25008349, CC 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 CC an opaque, chalky appearance, with reduced enamel thickness at CC occlusal surfaces (PubMed:25008349, PubMed:26247047). Body weight CC is reduced, probably due to problems with chewing hard foods CC (PubMed:25008349). Enamel formation is abnormal from the CC maturation stage onwards with significantly reduced mineral CC density and retention of proteinaceous material in the enamel CC matrix (PubMed:25008349, PubMed:26247047). Tooth enamel hardness CC is ten times lower than wild type (PubMed:26247047). Attachment of CC ameloblasts to the enamel layer may be weakened (PubMed:26247047). CC The calcium transporter SLC24A4 fails to localize to the distal CC 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 UniGene; Mm.335289; -. DR ProteinModelPortal; D3YYM4; -. DR STRING; 10090.ENSMUSP00000057320; -. DR iPTMnet; D3YYM4; -. DR PhosphoSitePlus; D3YYM4; -. DR MaxQB; D3YYM4; -. DR PaxDb; D3YYM4; -. DR PRIDE; D3YYM4; -. 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; ENOG410KDHE; Eukaryota. DR eggNOG; ENOG411264G; LUCA. DR GeneTree; ENSGT00520000055590; -. DR HOGENOM; HOG000168573; -. DR InParanoid; D3YYM4; -. DR OMA; SCLLPWG; -. DR OrthoDB; EOG091G01B8; -. DR PhylomeDB; D3YYM4; -. DR TreeFam; TF313196; -. DR PRO; PR:D3YYM4; -. DR Proteomes; UP000000589; Chromosome 9. DR Bgee; ENSMUSG00000044976; Expressed in 17 organ(s), highest expression level in adult mammalian kidney. 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 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; 3. DR SUPFAM; SSF50978; SSF50978; 2. 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; Complete proteome; Cytoplasmic vesicle; KW Phosphoprotein; Reference proteome; Repeat; WD repeat. FT CHAIN 1 1114 WD repeat-containing protein 72. FT /FTId=PRO_0000438188. FT REPEAT 15 54 WD 1. {ECO:0000255}. FT REPEAT 60 102 WD 2. {ECO:0000255}. FT REPEAT 160 197 WD 3. {ECO:0000255}. FT REPEAT 327 373 WD 4. {ECO:0000255}. FT REPEAT 413 452 WD 5. {ECO:0000255}. FT REPEAT 470 515 WD 6. {ECO:0000255}. FT REPEAT 566 605 WD 7. {ECO:0000255}. FT MOD_RES 1093 1093 Phosphoserine. FT {ECO:0000244|PubMed:21183079}. FT MOD_RES 1095 1095 Phosphoserine. FT {ECO:0000244|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 //