DMP1_MOUSE
ID DMP1_MOUSE Reviewed; 503 AA.
AC O55188; Q3TZB6;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Dentin matrix acidic phosphoprotein 1;
DE Short=DMP-1;
DE Short=Dentin matrix protein 1;
DE AltName: Full=AG1;
DE Flags: Precursor;
GN Name=Dmp1; Synonyms=Dmp;
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 [MRNA].
RC STRAIN=Swiss Webster; TISSUE=Molar;
RX PubMed=9525343; DOI=10.1359/jbmr.1998.13.3.422;
RA McDougall M., Gu T.T., Luan X., Simmons D., Chen J.;
RT "Identification of a novel isoform of mouse dentin matrix protein 1:
RT spatial expression in mineralized tissues.";
RL J. Bone Miner. Res. 13:422-431(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/SvJ; TISSUE=Spleen;
RA Feng J.Q., Traianedes K., Luan X., McDougall M.;
RT "Study of murine Dmp-1 gene function and regulation.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head, and Inner ear;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=17033621; DOI=10.1038/ng1905;
RA Feng J.Q., Ward L.M., Liu S., Lu Y., Xie Y., Yuan B., Yu X., Rauch F.,
RA Davis S.I., Zhang S., Rios H., Drezner M.K., Quarles L.D., Bonewald L.F.,
RA White K.E.;
RT "Loss of DMP1 causes rickets and osteomalacia and identifies a role for
RT osteocytes in mineral metabolism.";
RL Nat. Genet. 38:1310-1315(2006).
CC -!- FUNCTION: May have a dual function during osteoblast differentiation.
CC In the nucleus of undifferentiated osteoblasts, unphosphorylated form
CC acts as a transcriptional component for activation of osteoblast-
CC specific genes like osteocalcin. During the osteoblast to osteocyte
CC transition phase it is phosphorylated and exported into the
CC extracellular matrix, where it regulates nucleation of hydroxyapatite
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with importin alpha. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Secreted, extracellular space, extracellular matrix {ECO:0000250}.
CC Note=In proliferating preosteoblasts it is nuclear, during early
CC maturation stage is cytoplasmic and in mature osteoblast localizes in
CC the mineralized matrix. Export from the nucleus of differentiating
CC osteoblast is triggered by the release of calcium from intracellular
CC stores followed by a massive influx of this pool of calcium into the
CC nucleus (By similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in tooth particularly in odontoblast,
CC ameloblast and cementoblast. Also expressed in bone particularly in
CC osteoblast.
CC -!- PTM: Phosphorylated in the cytosol and extracellular matrix and
CC unphosphorylated in the nucleus. Phosphorylation is necessary for
CC nucleocytoplasmic transport and may be catalyzed by a nuclear isoform
CC of CK2 and can be augmented by calcium. Phosphorylated (in vitro) by
CC FAM20C in the extracellular medium at sites within the S-x-E/pS motif
CC (By similarity). {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mice display rickets and osteomalacia with
CC isolated renal phosphate wasting associated with elevated FGF23 levels
CC and normocalciuria. {ECO:0000269|PubMed:17033621}.
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DR EMBL; U65020; AAB93764.1; -; mRNA.
DR EMBL; AJ242625; CAB59629.1; -; Genomic_DNA.
DR EMBL; AK132177; BAE21014.1; -; mRNA.
DR EMBL; AK157973; BAE34293.1; -; mRNA.
DR EMBL; CH466529; EDL20228.1; -; Genomic_DNA.
DR CCDS; CCDS19484.1; -.
DR RefSeq; NP_058059.2; NM_016779.2.
DR RefSeq; XP_006534829.1; XM_006534766.2.
DR AlphaFoldDB; O55188; -.
DR STRING; 10090.ENSMUSP00000068053; -.
DR GlyGen; O55188; 3 sites.
DR iPTMnet; O55188; -.
DR PhosphoSitePlus; O55188; -.
DR PaxDb; O55188; -.
DR PeptideAtlas; O55188; -.
DR PRIDE; O55188; -.
DR ProteomicsDB; 279387; -.
DR Antibodypedia; 25470; 322 antibodies from 36 providers.
DR DNASU; 13406; -.
DR Ensembl; ENSMUST00000066708; ENSMUSP00000068053; ENSMUSG00000029307.
DR GeneID; 13406; -.
DR KEGG; mmu:13406; -.
DR UCSC; uc008yke.1; mouse.
DR CTD; 1758; -.
DR MGI; MGI:94910; Dmp1.
DR VEuPathDB; HostDB:ENSMUSG00000029307; -.
DR eggNOG; KOG1181; Eukaryota.
DR GeneTree; ENSGT00730000111375; -.
DR HOGENOM; CLU_040174_0_0_1; -.
DR InParanoid; O55188; -.
DR OMA; GQPKNME; -.
DR OrthoDB; 1235561at2759; -.
DR TreeFam; TF337029; -.
DR Reactome; R-MMU-3000178; ECM proteoglycans.
DR Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
DR BioGRID-ORCS; 13406; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Dmp1; mouse.
DR PRO; PR:O55188; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; O55188; protein.
DR Bgee; ENSMUSG00000029307; Expressed in hindlimb long bone and 98 other tissues.
DR Genevisible; O55188; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0050840; F:extracellular matrix binding; IDA:MGI.
DR GO; GO:0030544; F:Hsp70 protein binding; ISO:MGI.
DR GO; GO:0031214; P:biomineral tissue development; IEA:UniProtKB-KW.
DR GO; GO:0030198; P:extracellular matrix organization; IDA:MGI.
DR GO; GO:0001503; P:ossification; IEA:InterPro.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IDA:MGI.
DR GO; GO:0070173; P:regulation of enamel mineralization; IDA:MGI.
DR InterPro; IPR009889; DMP1.
DR PANTHER; PTHR23400; PTHR23400; 1.
DR Pfam; PF07263; DMP1; 1.
PE 2: Evidence at transcript level;
KW Biomineralization; Cytoplasm; Extracellular matrix; Glycoprotein; Nucleus;
KW Phosphoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..503
FT /note="Dentin matrix acidic phosphoprotein 1"
FT /id="PRO_0000021111"
FT REGION 23..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 350..352
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT COMPBIAS 40..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..119
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..192
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..247
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..307
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..363
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..431
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..452
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..467
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..496
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 356
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 394
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 457
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 35
FT /note="G -> D (in Ref. 1; AAB93764)"
FT /evidence="ECO:0000305"
FT CONFLICT 59
FT /note="G -> A (in Ref. 1; AAB93764 and 2; CAB59629)"
FT /evidence="ECO:0000305"
FT CONFLICT 67
FT /note="D -> H (in Ref. 1; AAB93764 and 2; CAB59629)"
FT /evidence="ECO:0000305"
FT CONFLICT 99
FT /note="E -> D (in Ref. 1; AAB93764 and 2; CAB59629)"
FT /evidence="ECO:0000305"
FT CONFLICT 116
FT /note="D -> G (in Ref. 1; AAB93764)"
FT /evidence="ECO:0000305"
FT CONFLICT 116
FT /note="D -> Y (in Ref. 2; CAB59629)"
FT /evidence="ECO:0000305"
FT CONFLICT 137
FT /note="T -> A (in Ref. 1; AAB93764 and 2; CAB59629)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="H -> Q (in Ref. 1; AAB93764 and 2; CAB59629)"
FT /evidence="ECO:0000305"
FT CONFLICT 168..170
FT /note="EAD -> DAH (in Ref. 1; AAB93764 and 2; CAB59629)"
FT /evidence="ECO:0000305"
FT CONFLICT 174
FT /note="E -> D (in Ref. 1; AAB93764 and 2; CAB59629)"
FT /evidence="ECO:0000305"
FT CONFLICT 179..181
FT /note="TQD -> AQH (in Ref. 1; AAB93764 and 2; CAB59629)"
FT /evidence="ECO:0000305"
FT CONFLICT 196
FT /note="E -> Q (in Ref. 1; AAB93764 and 2; CAB59629)"
FT /evidence="ECO:0000305"
FT CONFLICT 241
FT /note="H -> R (in Ref. 1; AAB93764 and 2; CAB59629)"
FT /evidence="ECO:0000305"
FT CONFLICT 267
FT /note="H -> R (in Ref. 1; AAB93764 and 2; CAB59629)"
FT /evidence="ECO:0000305"
FT CONFLICT 360
FT /note="A -> T (in Ref. 1; AAB93764 and 2; CAB59629)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 503 AA; 53965 MW; A8FA932A126F8541 CRC64;
MKTVILLVFL WGLSCALPVA RYHNTESESS EERTGDLAGS PPPPTNSESS EESQASPEGQ
ANSDHTDSSE SGEELGYDRG QYRPAGGLSK STGTGADKED DEDDSGDDTF GDEDNDLGPE
EGQWGGPSKL DSDEDSTDTT QSSEDSTSQE NSAQDTPSDS KDHDSEDEAD SRPEAGDSTQ
DSESEEQRVG GGSEGESSHG DGSEFDDEGM QSDDPESTRS DRGHARMSSA GIRSEESKGD
HEPTSTQDSD DSQSVEFSSR KSFRRSHVSE EDYRGELTDS NSRETQSDST EDTASKEESR
SESQEDTAES QSQEDSPEGQ DPSSESSEEA GEPSQESSSE SQEGVTSESR GDNPDNTSQA
GDQEDSESSE EDSLNTFSSS ESQSTEEQAD SESNESLSLS EESQESAQDG DSSSQEGLQS
QSASTESRSQ ESQSEQDSRS EEDSDSQDSS RSKEESNSTG SASSSEEDIR PKNMEADSRK
LIVDAYHNKP IGDQDDNDCQ DGY
