DMP1_BOVIN
ID DMP1_BOVIN Reviewed; 510 AA.
AC Q95120;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Dentin matrix acidic phosphoprotein 1;
DE Short=DMP-1;
DE Short=Dentin matrix protein 1;
DE Flags: Precursor;
GN Name=DMP1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Tooth;
RX PubMed=9109824; DOI=10.1177/00220345970760030701;
RA Hirst K.L., Ibaraki-O'Connor K., Young M.F., Dixon M.J.;
RT "Cloning and expression analysis of the bovine dentin matrix acidic
RT phosphoprotein gene.";
RL J. Dent. Res. 76:754-760(1997).
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 fetal brain, bone and tooth
CC particularly in odontoblast, but not in ameloblast. Not expressed in
CC liver and skin.
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; U47636; AAB09412.1; -; mRNA.
DR AlphaFoldDB; Q95120; -.
DR SMR; Q95120; -.
DR STRING; 9913.ENSBTAP00000025468; -.
DR PaxDb; Q95120; -.
DR eggNOG; KOG1181; Eukaryota.
DR InParanoid; Q95120; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0050840; F:extracellular matrix binding; IBA:GO_Central.
DR GO; GO:0031214; P:biomineral tissue development; IEA:UniProtKB-KW.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0001503; P:ossification; IEA:InterPro.
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..510
FT /note="Dentin matrix acidic phosphoprotein 1"
FT /id="PRO_0000021109"
FT REGION 23..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 364..366
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT COMPBIAS 101..118
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..197
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..291
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..332
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..354
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..421
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..441
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..462
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..503
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 351
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 370
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 427
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 464
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 510 AA; 55491 MW; 9BFA9A74F6450865 CRC64;
MKTTILLMFL WGLSCALPVA RYQNTESKSS EEWKGHLAQT PTPPLESSES SEESKLSSEE
QANEDPSDST ESEEVLGLDD QQHVHRPAGG LSRRGGSEGD NKDDDEDESG DDTFGDDDGG
PGPEERRSGG DSRLGSDEDS ADTTRSREDS TPQGDEGARD TTSESRDLDR EDEGNSRPEG
GDSTPDSDSE EHWVGGGSEG DSSHGDGSEF DDEGMQSDDP GAYRSERGNS RISDAGLKST
QSKGDDEEQA STQDSHESPA AAYPRRKFFR KSRLPEEDGR GELDDSRTIE VMSDSTENPD
SKEAGLGQSR EHSKSESRQE SEENRSPEDS QDVQDPSSES SQEVDLPSQE NSSESQEEAL
HESRGDNPDN ATSHSREHQA DSESSEEDVL DKPSDSESTS TEEQADSESH ESLRSSEESP
ESTEEQNSSS QEGAQTQSRS QESPSEEDDG SDSQDSSRSK EDSNSTESVS SSEEEAQTKN
TEVESRKLTV DAYHNKPIGD QDDNDCQDGY
