DSPP_RAT
ID DSPP_RAT Reviewed; 687 AA.
AC Q62598; P70578; Q9R057;
DT 13-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 13-DEC-2001, sequence version 2.
DT 25-MAY-2022, entry version 121.
DE RecName: Full=Dentin sialophosphoprotein;
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=Rdsp2;
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] (ISOFORM DPP-2).
RC STRAIN=Sprague-Dawley;
RX PubMed=10978503; DOI=10.1016/s0167-4781(00)00150-0;
RA Ritchie H.H., Wang L.-H.;
RT "The presence of multiple rat DSP-PP transcripts.";
RL Biochim. Biophys. Acta 1493:27-32(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-387, AND PROTEIN SEQUENCE OF 18-26.
RC STRAIN=Sprague-Dawley; TISSUE=Odontoblast;
RX PubMed=8106414; DOI=10.1016/s0021-9258(17)41916-8;
RA Ritchie H.H., Hou H., Veis A., Butler W.T.;
RT "Cloning and sequence determination of rat dentin sialoprotein, a novel
RT dentin protein.";
RL J. Biol. Chem. 269:3698-3702(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 421-687 (ISOFORM DPP-1).
RC STRAIN=Sprague-Dawley;
RX PubMed=8702961; DOI=10.1074/jbc.271.36.21695;
RA Ritchie H.H., Wang L.-H.;
RT "Sequence determination of an extremely acidic rat dentin phosphoprotein.";
RL J. Biol. Chem. 271:21695-21698(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-19.
RC STRAIN=Sprague-Dawley;
RX PubMed=10403786; DOI=10.1006/bbrc.1999.0875;
RA Yamazaki H., Kunisada T., Miyamoto A., Tagaya H., Hayashi S.;
RT "Tooth-specific expression conferred by the regulatory sequences of rat
RT dentin sialoprotein gene in transgenic mice.";
RL Biochem. Biophys. Res. Commun. 260:433-440(1999).
RN [5]
RP PROTEIN SEQUENCE OF 29-33; 70-79; 93-109; 136-148; 162-188; 266-308;
RP 398-423 AND 426-438, AND PHOSPHORYLATION AT SER-292 AND SER-298.
RX PubMed=11042175; DOI=10.1074/jbc.m006271200;
RA Qin C., Cook R.G., Orkiszewski R.S., Butler W.T.;
RT "Identification and characterization of the carboxyl-terminal region of rat
RT dentin sialoprotein.";
RL J. Biol. Chem. 276:904-909(2001).
RN [6]
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 [7]
RP INDUCTION.
RX PubMed=15308669; DOI=10.1074/jbc.m405031200;
RA Narayanan K., Ramachandran A., Peterson M.C., Hao J., Kolstoe A.B.,
RA Friedman A.D., George A.;
RT "The CCAAT enhancer-binding protein (C/EBP)beta and Nrf1 interact to
RT regulate dentin sialophosphoprotein (DSPP) gene expression during
RT odontoblast differentiation.";
RL J. Biol. Chem. 279:45423-45432(2004).
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:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=DPP-1; Synonyms=PP240;
CC IsoId=Q62598-1; Sequence=Displayed;
CC Name=DPP-2; Synonyms=PP171;
CC IsoId=Q62598-2; Sequence=VSP_003855;
CC -!- TISSUE SPECIFICITY: Specifically expressed in teeth, mainly in
CC odontoblasts and transiently in pre-ameloblasts.
CC {ECO:0000269|PubMed:9395101}.
CC -!- INDUCTION: Down-regulated by the CEBPB-NFE2L1 heterodimer during
CC odontoblast differentiation. {ECO:0000269|PubMed:15308669}.
CC -!- PTM: DSP is glycosylated.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA18932.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF247187; AAK96895.1; -; mRNA.
DR EMBL; U02074; AAA18932.1; ALT_FRAME; mRNA.
DR EMBL; U63111; AAC52774.1; -; mRNA.
DR EMBL; AF114987; AAD48588.1; ALT_TERM; Genomic_DNA.
DR PIR; A53053; A53053.
DR AlphaFoldDB; Q62598; -.
DR STRING; 10116.ENSRNOP00000002946; -.
DR GlyGen; Q62598; 6 sites.
DR iPTMnet; Q62598; -.
DR PhosphoSitePlus; Q62598; -.
DR PaxDb; Q62598; -.
DR PRIDE; Q62598; -.
DR RGD; 2525; Dspp.
DR eggNOG; ENOG502S0YS; Eukaryota.
DR InParanoid; Q62598; -.
DR PhylomeDB; Q62598; -.
DR Reactome; R-RNO-3000178; ECM proteoglycans.
DR PRO; PR:Q62598; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0031012; C:extracellular matrix; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0005518; F:collagen binding; IDA:RGD.
DR GO; GO:0036305; P:ameloblast differentiation; ISO:RGD.
DR GO; GO:0097186; P:amelogenesis; ISO:RGD.
DR GO; GO:0031214; P:biomineral tissue development; IEP:RGD.
DR GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; ISO:RGD.
DR GO; GO:0051216; P:cartilage development; IEP:RGD.
DR GO; GO:0030154; P:cell differentiation; IEP:RGD.
DR GO; GO:0071460; P:cellular response to cell-matrix adhesion; ISO:RGD.
DR GO; GO:0071549; P:cellular response to dexamethasone stimulus; IEP:RGD.
DR GO; GO:0032870; P:cellular response to hormone stimulus; IEP:RGD.
DR GO; GO:0061448; P:connective tissue development; ISO:RGD.
DR GO; GO:0097187; P:dentinogenesis; IEP:RGD.
DR GO; GO:0060350; P:endochondral bone morphogenesis; ISO:RGD.
DR GO; GO:1901148; P:gene expression involved in extracellular matrix organization; ISO:RGD.
DR GO; GO:0048820; P:hair follicle maturation; IEP:RGD.
DR GO; GO:0060425; P:lung morphogenesis; ISO:RGD.
DR GO; GO:0061978; P:mandibular condyle articular cartilage development; IEP:RGD.
DR GO; GO:0060231; P:mesenchymal to epithelial transition; ISO:RGD.
DR GO; GO:1903011; P:negative regulation of bone development; ISO:RGD.
DR GO; GO:1902731; P:negative regulation of chondrocyte proliferation; ISO:RGD.
DR GO; GO:0061914; P:negative regulation of growth plate cartilage chondrocyte proliferation; ISO:RGD.
DR GO; GO:2001054; P:negative regulation of mesenchymal cell apoptotic process; ISO:RGD.
DR GO; GO:0071895; P:odontoblast differentiation; IEP:RGD.
DR GO; GO:0042476; P:odontogenesis; IEP:RGD.
DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEP:RGD.
DR GO; GO:0090280; P:positive regulation of calcium ion import; IDA:MGI.
DR GO; GO:1902732; P:positive regulation of chondrocyte proliferation; ISO:RGD.
DR GO; GO:0070175; P:positive regulation of enamel mineralization; ISO:RGD.
DR GO; GO:1901329; P:regulation of odontoblast differentiation; IDA:UniProtKB.
DR GO; GO:0009743; P:response to carbohydrate; IEP:RGD.
DR GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR GO; GO:0009612; P:response to mechanical stimulus; IEP:RGD.
DR GO; GO:0071559; P:response to transforming growth factor beta; IEP:RGD.
DR GO; GO:0072050; P:S-shaped body morphogenesis; ISO:RGD.
PE 1: Evidence at protein level;
KW Alternative splicing; Biomineralization; Calcium;
KW Direct protein sequencing; Extracellular matrix; Glycoprotein;
KW Phosphoprotein; Reference proteome; Secreted; Sialic acid; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000269|PubMed:8106414"
FT CHAIN 18..687
FT /note="Dentin sialophosphoprotein"
FT /id="PRO_0000021126"
FT CHAIN 18..447
FT /note="Dentin sialoprotein"
FT /id="PRO_0000021127"
FT CHAIN 448..687
FT /note="Dentin phosphoprotein"
FT /id="PRO_0000021128"
FT REGION 54..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 146..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..223
FT /note="Polar 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..304
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..413
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..434
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..488
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 503..517
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..549
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..599
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..614
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..639
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..654
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 57
FT /note="Phosphothreonine; by CK2"
FT /evidence="ECO:0000255"
FT MOD_RES 226
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000255"
FT MOD_RES 253
FT /note="Phosphoserine; by CK1"
FT /evidence="ECO:0000255"
FT MOD_RES 278
FT /note="Phosphoserine; by CK1"
FT /evidence="ECO:0000255"
FT MOD_RES 292
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:11042175"
FT MOD_RES 298
FT /note="Phosphoserine; by CK1"
FT /evidence="ECO:0000269|PubMed:11042175"
FT MOD_RES 315
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000255"
FT MOD_RES 319
FT /note="Phosphothreonine; by CK2"
FT /evidence="ECO:0000255"
FT MOD_RES 329
FT /note="Phosphothreonine; by CK2"
FT /evidence="ECO:0000255"
FT MOD_RES 337
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000255"
FT MOD_RES 345
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000255"
FT MOD_RES 366
FT /note="Phosphoserine; by CK1"
FT /evidence="ECO:0000255"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 312
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 369
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 567..635
FT /note="Missing (in isoform DPP-2)"
FT /evidence="ECO:0000303|PubMed:10978503"
FT /id="VSP_003855"
FT CONFLICT 74
FT /note="N -> D (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 564
FT /note="S -> T (in Ref. 3; AAC52774)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 687 AA; 70179 MW; 9A845EED6AA31B63 CRC64;
MKTKIIIYIC IWATAWAIPV PQLVPLERDI VEKSADVPFL AHPGTAAQNE LHINNATNDD
SPKGSELGRQ VHSNGGYERD RNGSESIAVG GKSSPTQPIL ANAQGNSAKE REDVETYGHD
GIHAGGENST ANGIRGQVGI AENAEEAKES KVHGQPHQDT KTGLASDTSQ NGDATLVQEN
EPQVAGSKNS TNHEVGTHGS GVAAQETTPQ REGEGSENQG AEVTPSIGEG AGLDNTEGSP
SGNGIEEDED TGSGDGVGAD AGDGRESHDG TEGHEGQSSG GNNDNRGQGS VSTEDDDSKE
QEGSPNGRGG DNTSSSEETG IEEGDGTQTT QDNQNLSPTE GGIISQAEAC PSGQSQNQGL
ETEGSSTGNK SSITKESGKL SGSKDSNGHH GMELDKRNSP KQGESDKPQG AAEKSDTHNN
MGHSRIGSSS NSDGHDSYDF DDESMQGDDP NSSDESNGSD GSDDANSESA IENGNHGDAS
YTSDESSDNG SDSDSHAGED DSSDDTSDTD DSDSNGDDDS ESKDKDESDN SNHDNDSDSE
SKSDSSDSDS DSSDSSDSSD SSDSSETSDS SDSSDTSDSS DSSDSSDSSN SSDTSDSSDS
SDGDSSDGDS SDSDSSDSDS SNSSDSDSSD SSDSSSSDSS DSDSDSKDST SDSSDDNSKS
GNGNSDSDSD SDSDSEGSDS NHSTSDD
