DMP1_RAT
ID DMP1_RAT Reviewed; 489 AA.
AC P98193;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 91.
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;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Tooth;
RX PubMed=8509401; DOI=10.1016/s0021-9258(18)31434-0;
RA George A., Sabsay B., Simonian P.A., Veis A.;
RT "Characterization of a novel dentin matrix acidic phosphoprotein.
RT Implications for induction of biomineralization.";
RL J. Biol. Chem. 268:12624-12630(1993).
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 and
CC ameloblast.
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}.
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DR EMBL; L11354; AAS55638.1; -; mRNA.
DR PIR; A45988; A45988.
DR AlphaFoldDB; P98193; -.
DR STRING; 10116.ENSRNOP00000057936; -.
DR GlyGen; P98193; 3 sites.
DR PhosphoSitePlus; P98193; -.
DR PaxDb; P98193; -.
DR RGD; 2508; Dmp1.
DR eggNOG; KOG1181; Eukaryota.
DR InParanoid; P98193; -.
DR Reactome; R-RNO-3000178; ECM proteoglycans.
DR Reactome; R-RNO-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-RNO-8957275; Post-translational protein phosphorylation.
DR PRO; PR:P98193; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0031012; C:extracellular matrix; IDA:RGD.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0050840; F:extracellular matrix binding; ISO:RGD.
DR GO; GO:0030544; F:Hsp70 protein binding; IPI:RGD.
DR GO; GO:0031214; P:biomineral tissue development; IEA:UniProtKB-KW.
DR GO; GO:0030198; P:extracellular matrix organization; ISO:RGD.
DR GO; GO:0001503; P:ossification; IEA:InterPro.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; ISO:RGD.
DR GO; GO:0030500; P:regulation of bone mineralization; TAS:RGD.
DR GO; GO:0070173; P:regulation of enamel mineralization; ISO:RGD.
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..489
FT /note="Dentin matrix acidic phosphoprotein 1"
FT /id="PRO_0000021112"
FT REGION 22..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 334..336
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT COMPBIAS 22..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..99
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..176
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..264
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..291
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..347
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..387
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..413
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..438
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..482
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 340
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 378
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 443
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 489 AA; 53058 MW; 59F8381479DDA085 CRC64;
MKTVILLTFL WGLSCALPVA RYQNTESESS EERTGNLAQS PPPPMANSDH TDSSESGEEL
GSDRSQYRPA GGLSKSAGMD ADKEEDEDDS GDDTFGDEDN GPGPEERQWG GPSRLDSDED
SADTTQSSED STSQENSAQD TPSDSKDHHS DEADSRPEAG DSTQDSESEE YRVGGGSEGE
SSHGDGSEFD DEGMQSDDPG STRSDRGHTR MSSAGIRSEE SKGDHEPTST QDSDDSQDVE
FSSRKSFRRS RVSEEDDRGE LADSNSRETQ SVSTEDFRSK EESRSETQED TAETQSQEDS
PEGQDPSSES SEEAGEPSQE SSSESQEGVA SESRGDNPDN TSQTGDQRDS ESSEEDRLNT
FSSSESQSTE EQGDSESNES LSLSEESQES AQDEDSSSQE GLQSQSASRE SRSQESQSEQ
DSRSEENRDS DSQDSSRSKE ESNSTGSTSS SEEDNHPKNI EADNRKLIVD AYHNKPIGDQ
DDNDCQDGY
