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P98193 (DMP1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified January 22, 2014. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Dentin matrix acidic phosphoprotein 1

Short name=DMP-1
Short name=Dentin matrix protein 1
Alternative name(s):
AG1
Gene names
Name:Dmp1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length489 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

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 By similarity.

Subunit structure

Interacts with importin alpha By similarity.

Subcellular location

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.

Tissue specificity

Expressed in tooth particularly in odontoblast and ameloblast.

Post-translational modification

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 ofCK2 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616 Potential
Chain17 – 489473Dentin matrix acidic phosphoprotein 1
PRO_0000021112

Regions

Motif334 – 3363Cell attachment site Potential
Compositional bias41 – 444Poly-Pro

Amino acid modifications

Glycosylation3401N-linked (GlcNAc...) Potential
Glycosylation3781N-linked (GlcNAc...) Potential
Glycosylation4431N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
P98193 [UniParc].

Last modified May 30, 2000. Version 1.
Checksum: 59F8381479DDA085

FASTA48953,058
        10         20         30         40         50         60 
MKTVILLTFL WGLSCALPVA RYQNTESESS EERTGNLAQS PPPPMANSDH TDSSESGEEL 

        70         80         90        100        110        120 
GSDRSQYRPA GGLSKSAGMD ADKEEDEDDS GDDTFGDEDN GPGPEERQWG GPSRLDSDED 

       130        140        150        160        170        180 
SADTTQSSED STSQENSAQD TPSDSKDHHS DEADSRPEAG DSTQDSESEE YRVGGGSEGE 

       190        200        210        220        230        240 
SSHGDGSEFD DEGMQSDDPG STRSDRGHTR MSSAGIRSEE SKGDHEPTST QDSDDSQDVE 

       250        260        270        280        290        300 
FSSRKSFRRS RVSEEDDRGE LADSNSRETQ SVSTEDFRSK EESRSETQED TAETQSQEDS 

       310        320        330        340        350        360 
PEGQDPSSES SEEAGEPSQE SSSESQEGVA SESRGDNPDN TSQTGDQRDS ESSEEDRLNT 

       370        380        390        400        410        420 
FSSSESQSTE EQGDSESNES LSLSEESQES AQDEDSSSQE GLQSQSASRE SRSQESQSEQ 

       430        440        450        460        470        480 
DSRSEENRDS DSQDSSRSKE ESNSTGSTSS SEEDNHPKNI EADNRKLIVD AYHNKPIGDQ 


DDNDCQDGY 

« Hide

References

[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(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Tooth.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L11354 mRNA. Translation: AAS55638.1.
PIRA45988.
UniGeneRn.19340.

3D structure databases

ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteP98193.

Proteomic databases

PaxDbP98193.
PRIDEP98193.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

RGD2508. Dmp1.

Phylogenomic databases

eggNOGNOG86154.
HOGENOMHOG000220909.
HOVERGENHBG073257.

Gene expression databases

GenevestigatorP98193.

Family and domain databases

InterProIPR009889. DMP1.
[Graphical view]
PANTHERPTHR23400. PTHR23400. 1 hit.
PfamPF07263. DMP1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROP98193.

Entry information

Entry nameDMP1_RAT
AccessionPrimary (citable) accession number: P98193
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2000
Last modified: January 22, 2014
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program