DSPP_MOUSE
ID DSPP_MOUSE Reviewed; 934 AA.
AC P97399; O70567;
DT 13-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 2.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=Dentin sialophosphoprotein;
DE AltName: Full=Dentin matrix protein 3;
DE Short=DMP-3;
DE Contains:
DE RecName: Full=Dentin phosphoprotein;
DE AltName: Full=Dentin phosphophoryn;
DE Short=DPP;
DE Contains:
DE RecName: Full=Dentin sialoprotein;
DE Short=DSP;
DE Flags: Precursor;
GN Name=Dspp; Synonyms=Dmp3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Swiss Webster; TISSUE=Molar;
RX PubMed=8995371; DOI=10.1074/jbc.272.2.835;
RA MacDougall M., Simmons D., Luan X., Nydegger J., Feng J.Q., Gu T.T.;
RT "Dentin phosphoprotein and dentin sialoprotein are cleavage products
RT expressed from a single transcript coded by a gene on human chromosome 4.
RT Dentin phosphoprotein DNA sequence determination.";
RL J. Biol. Chem. 272:835-842(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SEQUENCE REVISION TO C-TERMINUS.
RC STRAIN=129/SvJ; TISSUE=Liver;
RX PubMed=9545272; DOI=10.1074/jbc.273.16.9457;
RA Feng J.Q., Luan X., Wallace J., Jing D., Ohshima T., Kulkarni A.B.,
RA D'Souza R.N., Kozak C.A., MacDougall M.;
RT "Genomic organization, chromosomal mapping, and promoter analysis of the
RT mouse dentin sialophosphoprotein (Dspp) gene, which codes for both dentin
RT sialoprotein and dentin phosphoprotein.";
RL J. Biol. Chem. 273:9457-9464(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/SvJ; TISSUE=Liver;
RA Sfeir C., Butler S., Lin E., George A., Veis A.;
RT "From mouse to zebrafish -- dentin matrix proteins genomic
RT characterization.";
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE OF 406-418, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=9395101; DOI=10.1111/j.1600-0722.1997.tb02137.x;
RA Ritchie H.H., Berry J.E., Somerman M.J., Hanks C.T., Bronckers A.L.,
RA Hotton D., Papagerakis P., Berdal A., Butler W.T.;
RT "Dentin sialoprotein (DSP) transcripts: developmentally-sustained
RT expression in odontoblasts and transient expression in pre-ameloblasts.";
RL Eur. J. Oral Sci. 105:405-413(1997).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=11175790; DOI=10.1038/84848;
RA Xiao S., Yu C., Chou X., Yuan W., Wang Y., Bu L., Fu G., Qian M., Yang J.,
RA Shi Y., Hu L., Han B., Wang Z., Huang W., Liu J., Chen Z., Zhao G.,
RA Kong X.;
RT "Dentinogenesis imperfecta 1 with or without progressive hearing loss is
RT associated with distinct mutations in DSPP.";
RL Nat. Genet. 27:201-204(2001).
RN [7]
RP INTERACTION WITH FBLN7.
RX PubMed=17699513; DOI=10.1074/jbc.m705847200;
RA de Vega S., Iwamoto T., Nakamura T., Hozumi K., McKnight D.A., Fisher L.W.,
RA Fukumoto S., Yamada Y.;
RT "TM14 is a new member of the fibulin family (fibulin-7) that interacts with
RT extracellular matrix molecules and is active for cell binding.";
RL J. Biol. Chem. 282:30878-30888(2007).
CC -!- FUNCTION: DSP may be an important factor in dentinogenesis. DPP may
CC bind high amount of calcium and facilitate initial mineralization of
CC dentin matrix collagen as well as regulate the size and shape of the
CC crystals.
CC -!- SUBUNIT: Interacts with FBLN7. {ECO:0000269|PubMed:17699513}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in teeth, mainly in odontoblasts and
CC transiently in pre-ameloblasts. Found in the inner ear.
CC {ECO:0000269|PubMed:11175790, ECO:0000269|PubMed:9395101}.
CC -!- PTM: DSP is glycosylated.
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DR EMBL; U67916; AAC12787.1; -; mRNA.
DR EMBL; AJ002141; CAA05208.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF135799; AAD42781.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; P97399; -.
DR STRING; 10090.ENSMUSP00000108391; -.
DR GlyGen; P97399; 6 sites.
DR iPTMnet; P97399; -.
DR PhosphoSitePlus; P97399; -.
DR CPTAC; non-CPTAC-3974; -.
DR PaxDb; P97399; -.
DR PeptideAtlas; P97399; -.
DR PRIDE; P97399; -.
DR ProteomicsDB; 277507; -.
DR MGI; MGI:109172; Dspp.
DR eggNOG; ENOG502S0YS; Eukaryota.
DR InParanoid; P97399; -.
DR Reactome; R-MMU-3000178; ECM proteoglycans.
DR PRO; PR:P97399; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P97399; protein.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005518; F:collagen binding; ISO:MGI.
DR GO; GO:0036305; P:ameloblast differentiation; IMP:MGI.
DR GO; GO:0097186; P:amelogenesis; IMP:MGI.
DR GO; GO:0031214; P:biomineral tissue development; IEA:UniProtKB-KW.
DR GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IMP:MGI.
DR GO; GO:0071460; P:cellular response to cell-matrix adhesion; IDA:MGI.
DR GO; GO:0061448; P:connective tissue development; IMP:MGI.
DR GO; GO:0097187; P:dentinogenesis; IMP:MGI.
DR GO; GO:0060350; P:endochondral bone morphogenesis; IMP:MGI.
DR GO; GO:1901148; P:gene expression involved in extracellular matrix organization; IMP:MGI.
DR GO; GO:0060425; P:lung morphogenesis; IMP:MGI.
DR GO; GO:0061978; P:mandibular condyle articular cartilage development; IMP:MGI.
DR GO; GO:0060231; P:mesenchymal to epithelial transition; IMP:MGI.
DR GO; GO:1903011; P:negative regulation of bone development; IMP:MGI.
DR GO; GO:1902731; P:negative regulation of chondrocyte proliferation; IMP:MGI.
DR GO; GO:0061914; P:negative regulation of growth plate cartilage chondrocyte proliferation; IMP:MGI.
DR GO; GO:2001054; P:negative regulation of mesenchymal cell apoptotic process; IMP:MGI.
DR GO; GO:0071895; P:odontoblast differentiation; IMP:MGI.
DR GO; GO:0042476; P:odontogenesis; IMP:MGI.
DR GO; GO:0090280; P:positive regulation of calcium ion import; ISO:MGI.
DR GO; GO:1902732; P:positive regulation of chondrocyte proliferation; IMP:MGI.
DR GO; GO:0070175; P:positive regulation of enamel mineralization; IDA:MGI.
DR GO; GO:1901329; P:regulation of odontoblast differentiation; ISO:MGI.
DR GO; GO:0072050; P:S-shaped body morphogenesis; IMP:MGI.
PE 1: Evidence at protein level;
KW Biomineralization; Calcium; Direct protein sequencing;
KW Extracellular matrix; Glycoprotein; Phosphoprotein; Reference proteome;
KW Secreted; Sialic acid; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..934
FT /note="Dentin sialophosphoprotein"
FT /id="PRO_0000021123"
FT CHAIN 18..451
FT /note="Dentin sialoprotein"
FT /id="PRO_0000021124"
FT CHAIN 452..934
FT /note="Dentin phosphoprotein"
FT /id="PRO_0000021125"
FT REGION 48..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 148..934
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 479..481
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT COMPBIAS 48..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..88
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..257
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..305
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..341
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..392
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..407
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..438
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..462
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..484
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..531
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..552
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..887
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 898..918
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 227
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000255"
FT MOD_RES 254
FT /note="Phosphoserine; by CK1"
FT /evidence="ECO:0000255"
FT MOD_RES 279
FT /note="Phosphoserine; by CK1"
FT /evidence="ECO:0000255"
FT MOD_RES 293
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000250|UniProtKB:Q62598"
FT MOD_RES 299
FT /note="Phosphoserine; by CK1"
FT /evidence="ECO:0000250|UniProtKB:Q62598"
FT MOD_RES 314
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000255"
FT MOD_RES 336
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000255"
FT MOD_RES 349
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000255"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 313
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 373
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 934 AA; 93903 MW; A618789D8A57249A CRC64;
MKMKIIIYIC IWATAWAIPV PQLVPLERDI VENSVAVPLL THPGTAAQNE LSINSTTSNS
NDSPDGSEIG EQVLSEDGYK RDGNGSESIH VGGKDFPTQP ILVNEQGNTA EEHNDIETYG
HDGVHARGEN STANGIRSQV GIVENAEEAE SSVHGQAGQN TKSGGASDVS QNGDATLVQE
NEPPEASIKN STNHEAGIHG SGVATHETTP QREGLGSENQ GTEVTPSIGE DAGLDDTDGS
PSGNGVEEDE DTGSGDGEGA EAGDGRESHD GTKGQGGQSH GGNTDHRGQS SVSTEDDDSK
EQEGFPNGHN GDNSSEENGV EEGDSTQATQ DKEKLSPKDT RDAEGGIISQ SEACPSGKSQ
DQGIETEGPN KGNKSIITKE SGKLSGSKDS NGHQGVELDK RNSPKQGESD KPQGTAEKSA
AHSNLGHSRI GSSSNSDGHD SYEFDDESMQ GDDPKSSDES NGSDESDTNS ESANESGSRG
DASYTSDESS DDDNDSDSHA GEDDSSDDSS GDGDSDSNGD GDSESEDKDE SDSSDHDNSS
DSESKSDSSD SSDDSSDSSD SSDSSDSSDS SDSSDSSDSS DSSDSNSSSD SSDSSGSSDS
SDSSDTCDSS DSSDSSDSSD SSDSSDSSDS SDSSDSSDSS DSSSSSDSSD SSSCSDSSDS
SDSSDSSDSS DSSDSSSSDS SSSSNSSDSS DSSDSSSSSD SSDSSDSSDS SDSSGSSDSS
DSSASSDSSS SSDSSDSSSS SDSSDSSDSS DSSDSSESSD SSNSSDSSDS SDSSDSSDSS
DSSDSSDSSD SSNSSDSSDS SDSSDSSDSS NSSDSSDSSD SSDSSDSSDS SDSSDSSDSS
DSSDSSDSSD SSDSSDSSDS SDSSDSSDSS DSSDSSDSSN SSDSSDSDSK DSSSDSSDGD
SKSGNGNSDS NSDSNSDSDS DSEGSDSNHS TSDD
