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Dentin matrix acidic phosphoprotein 1 (DMP-1) (Dentin matrix protein 1)

 DMP1_HUMAN              Reviewed;         513 AA.
Q13316; A1L4L3; O43265;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 2.
07-NOV-2018, entry version 147.
RecName: Full=Dentin matrix acidic phosphoprotein 1;
Short=DMP-1;
Short=Dentin matrix protein 1;
Flags: Precursor;
Name=DMP1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Molar;
PubMed=9177774; DOI=10.1006/geno.1997.4700;
Hirst K.L., Simmons D., Feng J., Aplin H., Dixon M.J., McDougall M.;
"Elucidation of the sequence and the genomic organization of the human
dentin matrix acidic phosphoprotein 1 (DMP1) gene: exclusion of the
locus from a causative role in the pathogenesis of dentinogenesis
imperfecta type II.";
Genomics 42:38-45(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT CYS-69.
McDougall M., Juan X., Simmons D., Feng J.;
Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 462-513, AND GENE MAPPING.
PubMed=8586437; DOI=10.1006/geno.1995.9867;
Aplin H.M., Hirst K.L., Crosby A.H., Dixon M.J.;
"Mapping of the human dentin matrix acidic phosphoprotein gene (DMP1)
to the dentinogenesis imperfecta type II critical region at chromosome
4q21.";
Genomics 30:347-349(1995).
[6]
FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND INTERACTION WITH
IMPORTIN ALPHA.
PubMed=12615915; DOI=10.1074/jbc.M212700200;
Narayanan K., Ramachandran A., Hao J., He G., Park K.W., Cho M.,
George A.;
"Dual functional roles of dentin matrix protein 1. Implications in
biomineralization and gene transcription by activation of
intracellular Ca2+ store.";
J. Biol. Chem. 278:17500-17508(2003).
[7]
INVOLVEMENT IN ARHR1, AND VARIANTS CYS-69; ASN-117 AND HIS-272.
PubMed=17033625; DOI=10.1038/ng1868;
Lorenz-Depiereux B., Bastepe M., Benet-Pages A., Amyere M.,
Wagenstaller J., Mueller-Barth U., Badenhoop K., Kaiser S.M.,
Rittmaster R.S., Shlossberg A.H., Olivares J.L., Loris C., Ramos F.J.,
Glorieux F., Vikkula M., Jueppner H., Strom T.M.;
"DMP1 mutations in autosomal recessive hypophosphatemia implicate a
bone matrix protein in the regulation of phosphate homeostasis.";
Nat. Genet. 38:1248-1250(2006).
[8]
INVOLVEMENT IN ARHR1.
PubMed=17033621; DOI=10.1038/ng1905;
Feng J.Q., Ward L.M., Liu S., Lu Y., Xie Y., Yuan B., Yu X., Rauch F.,
Davis S.I., Zhang S., Rios H., Drezner M.K., Quarles L.D.,
Bonewald L.F., White K.E.;
"Loss of DMP1 causes rickets and osteomalacia and identifies a role
for osteocytes in mineral metabolism.";
Nat. Genet. 38:1310-1315(2006).
[9]
PHOSPHORYLATION BY FAM20C.
PubMed=22582013; DOI=10.1126/science.1217817;
Tagliabracci V.S., Engel J.L., Wen J., Wiley S.E., Worby C.A.,
Kinch L.N., Xiao J., Grishin N.V., Dixon J.E.;
"Secreted kinase phosphorylates extracellular proteins that regulate
biomineralization.";
Science 336:1150-1153(2012).
-!- FUNCTION: May have a dual function during osteoblast
differentiation. In the nucleus of undifferentiated osteoblasts,
unphosphorylated form acts as a transcriptional component for
activation of osteoblast-specific genes like osteocalcin. During
the osteoblast to osteocyte transition phase it is phosphorylated
and exported into the extracellular matrix, where it regulates
nucleation of hydroxyapatite. {ECO:0000269|PubMed:12615915}.
-!- SUBUNIT: Interacts with importin alpha.
{ECO:0000269|PubMed:12615915}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12615915}.
Cytoplasm {ECO:0000269|PubMed:12615915}. Secreted, extracellular
space, extracellular matrix {ECO:0000269|PubMed:12615915}. Note=In
proliferating preosteoblasts it is nuclear, during early
maturation stage is cytoplasmic and in mature osteoblast localizes
in the mineralized matrix. Export from the nucleus of
differentiating osteoblast is triggered by the release of calcium
from intracellular stores followed by a massive influx of this
pool of calcium into the nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q13316-1; Sequence=Displayed;
Name=2;
IsoId=Q13316-2; Sequence=VSP_004191;
-!- TISSUE SPECIFICITY: Expressed in tooth particularly in
odontoblast, ameloblast and cementoblast.
-!- PTM: Phosphorylated in the cytosol and extracellular matrix and
unphosphorylated in the nucleus. Phosphorylation is necessary for
nucleocytoplasmic transport and may be catalyzed by a nuclear
isoform of CK2 and can be augmented by calcium. Phosphorylated (in
vitro) by FAM20C in the extracellular medium at sites within the
S-x-E/pS motif. {ECO:0000269|PubMed:12615915,
ECO:0000269|PubMed:22582013}.
-!- DISEASE: Hypophosphatemic rickets, autosomal recessive, 1 (ARHR1)
[MIM:241520]: A hereditary form of hypophosphatemic rickets, a
disorder of proximal renal tubule function that causes phosphate
loss, hypophosphatemia and skeletal deformities, including rickets
and osteomalacia unresponsive to vitamin D. Symptoms are bone
pain, fractures and growth abnormalities.
{ECO:0000269|PubMed:17033621, ECO:0000269|PubMed:17033625}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
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EMBL; U89012; AAC51332.1; -; mRNA.
EMBL; U34037; AAA97602.1; -; Genomic_DNA.
EMBL; CH471057; EAX05996.1; -; Genomic_DNA.
EMBL; BC130581; AAI30582.1; -; mRNA.
EMBL; BC132865; AAI32866.1; -; mRNA.
EMBL; U65378; AAB87728.1; -; mRNA.
CCDS; CCDS3623.1; -. [Q13316-1]
CCDS; CCDS43249.1; -. [Q13316-2]
RefSeq; NP_001073380.1; NM_001079911.2. [Q13316-2]
RefSeq; NP_004398.1; NM_004407.3. [Q13316-1]
UniGene; Hs.652366; -.
ProteinModelPortal; Q13316; -.
IntAct; Q13316; 1.
STRING; 9606.ENSP00000340935; -.
iPTMnet; Q13316; -.
PhosphoSitePlus; Q13316; -.
BioMuta; DMP1; -.
DMDM; 7673998; -.
PaxDb; Q13316; -.
PeptideAtlas; Q13316; -.
PRIDE; Q13316; -.
ProteomicsDB; 59304; -.
ProteomicsDB; 59305; -. [Q13316-2]
DNASU; 1758; -.
Ensembl; ENST00000282479; ENSP00000282479; ENSG00000152592. [Q13316-2]
Ensembl; ENST00000339673; ENSP00000340935; ENSG00000152592. [Q13316-1]
GeneID; 1758; -.
KEGG; hsa:1758; -.
UCSC; uc003hqv.4; human. [Q13316-1]
CTD; 1758; -.
DisGeNET; 1758; -.
EuPathDB; HostDB:ENSG00000152592.13; -.
GeneCards; DMP1; -.
HGNC; HGNC:2932; DMP1.
HPA; HPA037465; -.
MalaCards; DMP1; -.
MIM; 241520; phenotype.
MIM; 600980; gene.
neXtProt; NX_Q13316; -.
OpenTargets; ENSG00000152592; -.
Orphanet; 289176; Autosomal recessive hypophosphatemic rickets.
PharmGKB; PA27379; -.
eggNOG; KOG1181; Eukaryota.
eggNOG; ENOG4111M3T; LUCA.
GeneTree; ENSGT00730000111375; -.
HOGENOM; HOG000220909; -.
HOVERGEN; HBG073257; -.
InParanoid; Q13316; -.
OMA; HGDGSEF; -.
OrthoDB; EOG091G0U5E; -.
PhylomeDB; Q13316; -.
TreeFam; TF337029; -.
Reactome; R-HSA-3000178; ECM proteoglycans.
Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
SignaLink; Q13316; -.
ChiTaRS; DMP1; human.
GeneWiki; DMP1_(gene); -.
GenomeRNAi; 1758; -.
PRO; PR:Q13316; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000152592; Expressed in 80 organ(s), highest expression level in tibia.
CleanEx; HS_DMP1; -.
Genevisible; Q13316; HS.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0031012; C:extracellular matrix; TAS:ProtInc.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005509; F:calcium ion binding; TAS:ProtInc.
GO; GO:0050840; F:extracellular matrix binding; IEA:Ensembl.
GO; GO:0005178; F:integrin binding; TAS:ProtInc.
GO; GO:0031214; P:biomineral tissue development; IEA:UniProtKB-KW.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
GO; GO:0001503; P:ossification; TAS:ProtInc.
GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IEA:Ensembl.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0070173; P:regulation of enamel mineralization; IEA:Ensembl.
InterPro; IPR009889; DMP1.
PANTHER; PTHR23400; PTHR23400; 1.
Pfam; PF07263; DMP1; 1.
1: Evidence at protein level;
Alternative splicing; Biomineralization; Complete proteome; Cytoplasm;
Extracellular matrix; Glycoprotein; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Secreted; Signal.
SIGNAL 1 16 {ECO:0000255}.
CHAIN 17 513 Dentin matrix acidic phosphoprotein 1.
/FTId=PRO_0000021110.
MOTIF 364 366 Cell attachment site. {ECO:0000255}.
CARBOHYD 25 25 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 285 285 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 324 324 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 345 345 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 351 351 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 413 413 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 426 426 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 467 467 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 46 61 Missing (in isoform 2).
{ECO:0000303|Ref.2}.
/FTId=VSP_004191.
VARIANT 69 69 S -> C (in dbSNP:rs10019009).
{ECO:0000269|PubMed:17033625,
ECO:0000269|Ref.2}.
/FTId=VAR_030750.
VARIANT 117 117 D -> N (in one individual with tumoral
calcinosis; dbSNP:rs140719182).
{ECO:0000269|PubMed:17033625}.
/FTId=VAR_030751.
VARIANT 272 272 R -> H (in dbSNP:rs145237146).
{ECO:0000269|PubMed:17033625}.
/FTId=VAR_030752.
VARIANT 463 463 K -> R (in dbSNP:rs34661425).
/FTId=VAR_033848.
SEQUENCE 513 AA; 55782 MW; 2C1FDE319A5D106F CRC64;
MKISILLMFL WGLSCALPVT RYQNNESEDS EEWKGHLAQA PTPPLESSES SEGSKVSSEE
QANEDPSDST QSEEGLGSDD HQYIYRLAGG FSRSTGKGGD DKDDDEDDSG DDTFGDDDSG
PGPKDRQEGG NSRLGSDEDS DDTIQASEES APQGQDSAQD TTSESRELDN EDRVDSKPEG
GDSTQESESE EHWVGGGSDG ESSHGDGSEL DDEGMQSDDP ESIRSERGNS RMNSAGMKSK
ESGENSEQAN TQDSGGSQLL EHPSRKIFRK SRISEEDDRS ELDDNNTMEE VKSDSTENSN
SRDTGLSQPR RDSKGDSQED SKENLSQEES QNVDGPSSES SQEANLSSQE NSSESQEEVV
SESRGDNPDP TTSYVEDQED SDSSEEDSSH TLSHSKSESR EEQADSESSE SLNFSEESPE
SPEDENSSSQ EGLQSHSSSA ESQSEESHSE EDDSDSQDSS RSKEDSNSTE SKSSSEEDGQ
LKNIEIESRK LTVDAYHNKP IGDQDDNDCQ DGY


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