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Protein

Dentin matrix acidic phosphoprotein 1

Gene

Dmp1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

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 (By similarity).By similarity

GO - Biological processi

  1. biomineral tissue development Source: UniProtKB-KW
  2. extracellular matrix organization Source: InterPro
  3. ossification Source: InterPro
  4. regulation of bone mineralization Source: RGD
Complete GO annotation...

Keywords - Biological processi

Biomineralization

Names & Taxonomyi

Protein namesi
Recommended name:
Dentin matrix acidic phosphoprotein 1
Short name:
DMP-1
Short name:
Dentin matrix protein 1
Alternative name(s):
AG1
Gene namesi
Name:Dmp1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2508. Dmp1.

Subcellular locationi

Nucleus By similarity. Cytoplasm By similarity. Secretedextracellular spaceextracellular matrix By similarity
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 (By similarity).By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. nucleus Source: UniProtKB-SubCell
  3. proteinaceous extracellular matrix Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Extracellular matrix, Nucleus, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1616Sequence AnalysisAdd
BLAST
Chaini17 – 489473Dentin matrix acidic phosphoprotein 1PRO_0000021112Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi340 – 3401N-linked (GlcNAc...)Sequence Analysis
Glycosylationi378 – 3781N-linked (GlcNAc...)Sequence Analysis
Glycosylationi443 – 4431N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

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 (By similarity).By similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP98193.
PRIDEiP98193.

PTM databases

PhosphoSiteiP98193.

Expressioni

Tissue specificityi

Expressed in tooth particularly in odontoblast and ameloblast.

Gene expression databases

GenevestigatoriP98193.

Interactioni

Subunit structurei

Interacts with importin alpha.By similarity

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi334 – 3363Cell attachment siteSequence Analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi41 – 444Poly-Pro

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG86154.
HOGENOMiHOG000220909.
HOVERGENiHBG073257.
InParanoidiP98193.

Family and domain databases

InterProiIPR009889. DMP1.
[Graphical view]
PANTHERiPTHR23400. PTHR23400. 1 hit.
PfamiPF07263. DMP1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P98193-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKTVILLTFL WGLSCALPVA RYQNTESESS EERTGNLAQS PPPPMANSDH
60 70 80 90 100
TDSSESGEEL GSDRSQYRPA GGLSKSAGMD ADKEEDEDDS GDDTFGDEDN
110 120 130 140 150
GPGPEERQWG GPSRLDSDED SADTTQSSED STSQENSAQD TPSDSKDHHS
160 170 180 190 200
DEADSRPEAG DSTQDSESEE YRVGGGSEGE SSHGDGSEFD DEGMQSDDPG
210 220 230 240 250
STRSDRGHTR MSSAGIRSEE SKGDHEPTST QDSDDSQDVE FSSRKSFRRS
260 270 280 290 300
RVSEEDDRGE LADSNSRETQ SVSTEDFRSK EESRSETQED TAETQSQEDS
310 320 330 340 350
PEGQDPSSES SEEAGEPSQE SSSESQEGVA SESRGDNPDN TSQTGDQRDS
360 370 380 390 400
ESSEEDRLNT FSSSESQSTE EQGDSESNES LSLSEESQES AQDEDSSSQE
410 420 430 440 450
GLQSQSASRE SRSQESQSEQ DSRSEENRDS DSQDSSRSKE ESNSTGSTSS
460 470 480
SEEDNHPKNI EADNRKLIVD AYHNKPIGDQ DDNDCQDGY
Length:489
Mass (Da):53,058
Last modified:May 29, 2000 - v1
Checksum:i59F8381479DDA085
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L11354 mRNA. Translation: AAS55638.1.
PIRiA45988.
UniGeneiRn.19340.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L11354 mRNA. Translation: AAS55638.1.
PIRiA45988.
UniGeneiRn.19340.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

PTM databases

PhosphoSiteiP98193.

Proteomic databases

PaxDbiP98193.
PRIDEiP98193.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

RGDi2508. Dmp1.

Phylogenomic databases

eggNOGiNOG86154.
HOGENOMiHOG000220909.
HOVERGENiHBG073257.
InParanoidiP98193.

Miscellaneous databases

PROiP98193.

Gene expression databases

GenevestigatoriP98193.

Family and domain databases

InterProiIPR009889. DMP1.
[Graphical view]
PANTHERiPTHR23400. PTHR23400. 1 hit.
PfamiPF07263. DMP1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Characterization of a novel dentin matrix acidic phosphoprotein. Implications for induction of biomineralization."
    George A., Sabsay B., Simonian P.A., Veis A.
    J. Biol. Chem. 268:12624-12630(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Tooth.

Entry informationi

Entry nameiDMP1_RAT
AccessioniPrimary (citable) accession number: P98193
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2000
Last sequence update: May 29, 2000
Last modified: January 6, 2015
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.