ID DSPP_HUMAN Reviewed; 1301 AA.
AC Q9NZW4; A8MUI0; O95815;
DT 13-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 27-MAR-2024, entry version 167.
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;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10706475; DOI=10.1034/j.1600-0722.2000.00765.x;
RA Gu K., Chang S.R., Ritchie H.H., Clarkson B.H., Rutherford R.B.;
RT "Molecular cloning of a human dentin sialophosphoprotein gene.";
RL Eur. J. Oral Sci. 108:35-42(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 463-1301.
RC TISSUE=Tooth;
RX PubMed=9879917; DOI=10.1046/j.0909-8836..t01-9-.x;
RA Gu K., Chang S.R., Slaven M.S., Clarkson B.H., Rutherford R.B.,
RA Ritchie H.H.;
RT "Human dentin phosphophoryn nucleotide and amino acid sequence.";
RL Eur. J. Oral Sci. 106:1043-1047(1998).
RN [4]
RP INVOLVEMENT IN DGI2.
RX PubMed=11175779; DOI=10.1038/84765;
RA Zhang X., Zhao J., Li C., Gao S., Qiu C., Liu P., Wu G., Qiang B.,
RA Lo W.H.Y., Shen Y.;
RT "DSPP mutation in dentinogenesis imperfecta Shields type II.";
RL Nat. Genet. 27:151-152(2001).
RN [5]
RP INVOLVEMENT IN DGI2; DGI3 AND DTDP2, AND VARIANT DGI3 SER-17.
RX PubMed=18521831; DOI=10.1002/humu.20783;
RA McKnight D.A., Suzanne Hart P., Hart T.C., Hartsfield J.K., Wilson A.,
RA Wright J.T., Fisher L.W.;
RT "A comprehensive analysis of normal variation and disease-causing mutations
RT in the human DSPP gene.";
RL Hum. Mutat. 29:1392-1404(2008).
RN [6]
RP VARIANTS DFNA39/DGI1 THR-17 AND PHE-18.
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 VARIANT DTDP2 ASP-6, AND CHARACTERIZATION OF VARIANT DTDP2 ASP-6.
RX PubMed=12354781; DOI=10.1093/hmg/11.21.2559;
RA Rajpar M.H., Koch M.J., Davies R.M., Mellody K.T., Kielty C.M., Dixon M.J.;
RT "Mutation of the signal peptide region of the bicistronic gene DSPP affects
RT translocation to the endoplasmic reticulum and results in defective dentine
RT biomineralization.";
RL Hum. Mol. Genet. 11:2559-2565(2002).
RN [8]
RP VARIANTS DGI2 VAL-15 AND TRP-68.
RX PubMed=14758537; DOI=10.1007/s00439-004-1084-z;
RA Malmgren B., Lindskog S., Elgadi A., Norgren S.;
RT "Clinical, histopathologic, and genetic investigation in two large families
RT with dentinogenesis imperfecta type II.";
RL Hum. Genet. 114:491-498(2004).
RN [9]
RP VARIANT DGI3 PHE-18.
RX PubMed=15592686; DOI=10.1007/s00439-004-1223-6;
RA Kim J.-W., Hu J.C.-C., Lee J.-I., Moon S.-K., Kim Y.-J., Jang K.-T.,
RA Lee S.-H., Kim C.-C., Hahn S.-H., Simmer J.P.;
RT "Mutational hot spot in the DSPP gene causing dentinogenesis imperfecta
RT type II.";
RL Hum. Genet. 116:186-191(2005).
RN [10]
RP VARIANT TRP-68.
RX PubMed=17033625; DOI=10.1038/ng1868;
RA Lorenz-Depiereux B., Bastepe M., Benet-Pages A., Amyere M.,
RA Wagenstaller J., Mueller-Barth U., Badenhoop K., Kaiser S.M.,
RA Rittmaster R.S., Shlossberg A.H., Olivares J.L., Loris C., Ramos F.J.,
RA Glorieux F., Vikkula M., Jueppner H., Strom T.M.;
RT "DMP1 mutations in autosomal recessive hypophosphatemia implicate a bone
RT matrix protein in the regulation of phosphate homeostasis.";
RL Nat. Genet. 38:1248-1250(2006).
RN [11]
RP VARIANT DGI2 SER-17.
RX PubMed=17627120; DOI=10.1159/000102682;
RA Hart P.S., Hart T.C.;
RT "Disorders of human dentin.";
RL Cells Tissues Organs 186:70-77(2007).
RN [12]
RP VARIANT DGI2 ASP-18.
RX PubMed=21029264; DOI=10.1111/j.1601-0825.2010.01760.x;
RA Lee S.K., Lee K.E., Hwang Y.H., Kida M., Tsutsumi T., Ariga T., Park J.C.,
RA Kim J.W.;
RT "Identification of the DSPP mutation in a new kindred and phenotype-
RT genotype correlation.";
RL Oral Dis. 17:314-319(2011).
RN [13]
RP CHARACTERIZATION OF VARIANT DFNA39/DGI1 THR-17, AND CHARACTERIZATION OF
RP VARIANTS DGI2 VAL-15; SER-17 AND ASP-18.
RX PubMed=22392858; DOI=10.1002/jbmr.1573;
RA von Marschall Z., Mok S., Phillips M.D., McKnight D.A., Fisher L.W.;
RT "Rough endoplasmic reticulum trafficking errors by different classes of
RT mutant dentin sialophosphoprotein (DSPP) cause dominant negative effects in
RT both dentinogenesis imperfecta and dentin dysplasia by entrapping normal
RT DSPP.";
RL J. Bone Miner. Res. 27:1309-1321(2012).
RN [14]
RP VARIANT DGI3 LEU-17, AND CHARACTERIZATION OF VARIANT DGI3 LEU-17.
RX PubMed=23509818; DOI=10.1155/2013/948181;
RA Lee S.K., Lee K.E., Song S.J., Hyun H.K., Lee S.H., Kim J.W.;
RT "A DSPP mutation causing dentinogenesis imperfecta and characterization of
RT the mutational effect.";
RL Biomed. Res. Int. 2013:948181-948181(2013).
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 -!- TISSUE SPECIFICITY: Expressed in teeth. DPP is synthesized by
CC odontoblast and transiently expressed by pre-ameloblasts.
CC -!- PTM: DSP is glycosylated.
CC -!- DISEASE: Deafness, autosomal dominant, 39, with dentinogenesis
CC imperfecta 1 (DFNA39/DGI1) [MIM:605594]: A disorder characterized by
CC the association of progressive sensorineural high-frequency hearing
CC loss with dentinogenesis imperfecta. {ECO:0000269|PubMed:11175790,
CC ECO:0000269|PubMed:22392858}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Dentinogenesis imperfecta, Shields type 2 (DGI2) [MIM:125490]:
CC A form of dentinogenesis imperfecta, an autosomal dominant dentin
CC disorder characterized by amber-brown, opalescent teeth that fracture
CC and shed their enamel during mastication, thereby exposing the dentin
CC to rapid wear. Radiographically, the crown appears bulbous and pulpal
CC obliteration is common. The pulp chambers are initially larger than
CC normal prior and immediately after tooth eruption, and then
CC progressively close down to become almost obliterated by abnormal
CC dentin formation. Roots are short and thin. Both primary and permanent
CC teeth are affected. DGI2 is not associated with osteogenesis
CC imperfecta. {ECO:0000269|PubMed:11175779, ECO:0000269|PubMed:14758537,
CC ECO:0000269|PubMed:17627120, ECO:0000269|PubMed:21029264,
CC ECO:0000269|PubMed:22392858}. Note=The disease is caused by variants
CC affecting the gene represented in this entry. DSPP defects causing
CC dentin abnormalities act in a dominant negative manner and include
CC missense, splice-site, frameshift mutations. 5' frameshift mutations
CC cause dentin dysplasia while frameshift mutations at the 3' end cause
CC the more severe dentinogenesis imperfecta phenotype (PubMed:18521831,
CC PubMed:22392858).
CC -!- DISEASE: Dentinogenesis imperfecta, Shields type 3 (DGI3) [MIM:125500]:
CC A form of dentinogenesis imperfecta, an autosomal dominant dentin
CC disorder characterized by amber-brown, opalescent teeth that fracture
CC and shed their enamel during mastication, thereby exposing the dentin
CC to rapid wear. Radiographically, the crown appears bulbous and pulpal
CC obliteration is common. The pulp chambers are initially larger than
CC normal prior and immediately after tooth eruption, and then
CC progressively close down to become almost obliterated by abnormal
CC dentin formation. Roots are short and thin. Both primary and permanent
CC teeth are affected. DGI3 teeth typically manifest multiple periapical
CC radiolucencies. DGI3 is not associated with osteogenesis imperfecta.
CC {ECO:0000269|PubMed:15592686, ECO:0000269|PubMed:18521831,
CC ECO:0000269|PubMed:23509818}. Note=The disease is caused by variants
CC affecting the gene represented in this entry. DSPP defects causing
CC dentin abnormalities act in a dominant negative manner and include
CC missense, splice-site, frameshift mutations. 5' frameshift mutations
CC cause dentin dysplasia while frameshift mutations at the 3' end cause
CC the more severe dentinogenesis imperfecta phenotype (PubMed:18521831,
CC PubMed:22392858).
CC -!- DISEASE: Dentin dysplasia 2 (DTDP2) [MIM:125420]: A dental defect in
CC which the deciduous teeth are opalescent. The permanent teeth are of
CC normal shape, form, and color in most cases. The root length is normal.
CC On radiographs, the pulp chambers of permanent teeth are obliterated,
CC have a thistle-tube deformity and contain pulp stones.
CC {ECO:0000269|PubMed:12354781, ECO:0000269|PubMed:18521831}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry. DSPP defects causing dentin abnormalities act in a dominant
CC negative manner and include missense, splice-site, frameshift
CC mutations. 5' frameshift mutations cause dentin dysplasia while
CC frameshift mutations at the 3' end cause the more severe dentinogenesis
CC imperfecta phenotype (PubMed:18521831, PubMed:22392858).
CC {ECO:0000269|PubMed:18521831, ECO:0000269|PubMed:22392858}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF163151; AAF42472.1; -; Genomic_DNA.
DR EMBL; AC093895; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF094508; AAD16120.1; -; mRNA.
DR CCDS; CCDS43248.1; -.
DR RefSeq; NP_055023.2; NM_014208.3.
DR AlphaFoldDB; Q9NZW4; -.
DR BioGRID; 108168; 3.
DR STRING; 9606.ENSP00000498766; -.
DR GlyCosmos; Q9NZW4; 12 sites, No reported glycans.
DR GlyGen; Q9NZW4; 12 sites.
DR iPTMnet; Q9NZW4; -.
DR PhosphoSitePlus; Q9NZW4; -.
DR BioMuta; DSPP; -.
DR DMDM; 215273974; -.
DR MassIVE; Q9NZW4; -.
DR PaxDb; 9606-ENSP00000382213; -.
DR PeptideAtlas; Q9NZW4; -.
DR Antibodypedia; 51372; 115 antibodies from 16 providers.
DR DNASU; 1834; -.
DR Ensembl; ENST00000651931.1; ENSP00000498766.1; ENSG00000152591.15.
DR GeneID; 1834; -.
DR KEGG; hsa:1834; -.
DR MANE-Select; ENST00000651931.1; ENSP00000498766.1; NM_014208.3; NP_055023.2.
DR UCSC; uc003hqu.3; human.
DR AGR; HGNC:3054; -.
DR CTD; 1834; -.
DR DisGeNET; 1834; -.
DR GeneCards; DSPP; -.
DR HGNC; HGNC:3054; DSPP.
DR HPA; ENSG00000152591; Not detected.
DR MalaCards; DSPP; -.
DR MIM; 125420; phenotype.
DR MIM; 125485; gene.
DR MIM; 125490; phenotype.
DR MIM; 125500; phenotype.
DR MIM; 605594; phenotype.
DR neXtProt; NX_Q9NZW4; -.
DR OpenTargets; ENSG00000152591; -.
DR Orphanet; 99789; Dentin dysplasia type I.
DR Orphanet; 99791; Dentin dysplasia type II.
DR Orphanet; 166260; Dentinogenesis imperfecta type 2.
DR Orphanet; 166265; Dentinogenesis imperfecta type 3.
DR PharmGKB; PA27507; -.
DR VEuPathDB; HostDB:ENSG00000152591; -.
DR eggNOG; ENOG502S0YS; Eukaryota.
DR GeneTree; ENSGT00730000111489; -.
DR HOGENOM; CLU_006339_0_0_1; -.
DR InParanoid; Q9NZW4; -.
DR OMA; ITYFCIW; -.
DR OrthoDB; 4642537at2759; -.
DR PhylomeDB; Q9NZW4; -.
DR TreeFam; TF318563; -.
DR PathwayCommons; Q9NZW4; -.
DR Reactome; R-HSA-3000178; ECM proteoglycans.
DR SignaLink; Q9NZW4; -.
DR SIGNOR; Q9NZW4; -.
DR BioGRID-ORCS; 1834; 7 hits in 1132 CRISPR screens.
DR GeneWiki; Dentin_sialophosphoprotein_(gene); -.
DR GenomeRNAi; 1834; -.
DR Pharos; Q9NZW4; Tbio.
DR PRO; PR:Q9NZW4; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q9NZW4; Protein.
DR Bgee; ENSG00000152591; Expressed in buccal mucosa cell and 66 other cell types or tissues.
DR Genevisible; Q9NZW4; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0031012; C:extracellular matrix; TAS:ProtInc.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; TAS:ProtInc.
DR GO; GO:0005518; F:collagen binding; IBA:GO_Central.
DR GO; GO:0005201; F:extracellular matrix structural constituent; TAS:ProtInc.
DR GO; GO:0031214; P:biomineral tissue development; IEA:UniProtKB-KW.
DR GO; GO:0097187; P:dentinogenesis; IBA:GO_Central.
DR GO; GO:0071895; P:odontoblast differentiation; IBA:GO_Central.
DR GO; GO:1901329; P:regulation of odontoblast differentiation; ISS:UniProtKB.
DR PANTHER; PTHR47819; DENTIN SIALOPHOSPHOPROTEIN; 1.
DR PANTHER; PTHR47819:SF1; DENTIN SIALOPHOSPHOPROTEIN; 1.
PE 1: Evidence at protein level;
KW Biomineralization; Calcium; Deafness; Disease variant;
KW Extracellular matrix; Glycoprotein; Phosphoprotein; Reference proteome;
KW Secreted; Sialic acid; Signal.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT CHAIN 16..1301
FT /note="Dentin sialophosphoprotein"
FT /id="PRO_0000021120"
FT CHAIN 16..462
FT /note="Dentin sialoprotein"
FT /id="PRO_0000021121"
FT CHAIN 463..1301
FT /note="Dentin phosphoprotein"
FT /id="PRO_0000021122"
FT REGION 55..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 146..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..1301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 488..490
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT COMPBIAS 59..81
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..268
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..328
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..373
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..406
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..449
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..500
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..515
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..536
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 537..551
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..584
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..615
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..639
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..1288
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 259
FT /note="Phosphoserine; by CK1"
FT /evidence="ECO:0000255"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62598"
FT CARBOHYD 41
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 49
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 81
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 150
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 191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 209
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 336
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 387
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 6
FT /note="Y -> D (in DTDP2; the mutant protein does not
FT translocate into the endoplasmic reticulum;
FT dbSNP:rs121912988)"
FT /evidence="ECO:0000269|PubMed:12354781"
FT /id="VAR_036861"
FT VARIANT 15
FT /note="A -> V (in DGI2; dominant negative mutation; results
FT in signal peptide retention; the mutant protein is retained
FT within the rough ER membrane; dbSNP:rs121912989)"
FT /evidence="ECO:0000269|PubMed:14758537,
FT ECO:0000269|PubMed:22392858"
FT /id="VAR_036862"
FT VARIANT 17
FT /note="P -> L (in DGI3; the mutant protein is largely
FT retained in the ER)"
FT /evidence="ECO:0000269|PubMed:23509818"
FT /id="VAR_070252"
FT VARIANT 17
FT /note="P -> S (in DGI2 and DGI3; dominant negative
FT mutation; the mutant protein is retained intracellularly;
FT dbSNP:rs121912986)"
FT /evidence="ECO:0000269|PubMed:17627120,
FT ECO:0000269|PubMed:18521831, ECO:0000269|PubMed:22392858"
FT /id="VAR_054443"
FT VARIANT 17
FT /note="P -> T (in DFNA39/DGI1; dominant negative mutation;
FT the mutant protein is retained intracellularly;
FT dbSNP:rs121912986)"
FT /evidence="ECO:0000269|PubMed:11175790,
FT ECO:0000269|PubMed:22392858"
FT /id="VAR_012280"
FT VARIANT 18
FT /note="V -> D (in DGI2; dominant negative mutation; the
FT mutant protein is retained intracellularly)"
FT /evidence="ECO:0000269|PubMed:21029264,
FT ECO:0000269|PubMed:22392858"
FT /id="VAR_070253"
FT VARIANT 18
FT /note="V -> F (in DFNA39/DGI1 and DGI3; dbSNP:rs121912987)"
FT /evidence="ECO:0000269|PubMed:11175790,
FT ECO:0000269|PubMed:15592686"
FT /id="VAR_012281"
FT VARIANT 68
FT /note="R -> W (in DGI2; dbSNP:rs36094464)"
FT /evidence="ECO:0000269|PubMed:14758537,
FT ECO:0000269|PubMed:17033625"
FT /id="VAR_030661"
FT VARIANT 243
FT /note="D -> N (in dbSNP:rs3750025)"
FT /id="VAR_047551"
FT CONFLICT 673
FT /note="D -> DSSDSSS (in Ref. 1; AAF42472)"
FT /evidence="ECO:0000305"
FT CONFLICT 734..739
FT /note="Missing (in Ref. 1; AAF42472)"
FT /evidence="ECO:0000305"
FT CONFLICT 799
FT /note="N -> D (in Ref. 3; AAD16120)"
FT /evidence="ECO:0000305"
FT CONFLICT 836
FT /note="S -> C (in Ref. 3; AAD16120)"
FT /evidence="ECO:0000305"
FT CONFLICT 850
FT /note="G -> S (in Ref. 1; AAF42472)"
FT /evidence="ECO:0000305"
FT CONFLICT 875
FT /note="N -> NSSD (in Ref. 1; AAF42472)"
FT /evidence="ECO:0000305"
FT CONFLICT 960
FT /note="S -> G (in Ref. 1; AAF42472)"
FT /evidence="ECO:0000305"
FT CONFLICT 1002
FT /note="N -> D (in Ref. 3; AAD16120)"
FT /evidence="ECO:0000305"
FT CONFLICT 1022
FT /note="S -> G (in Ref. 3; AAD16120)"
FT /evidence="ECO:0000305"
FT CONFLICT 1029
FT /note="N -> D (in Ref. 1; AAF42472 and 3; AAD16120)"
FT /evidence="ECO:0000305"
FT CONFLICT 1044
FT /note="D -> N (in Ref. 1; AAF42472)"
FT /evidence="ECO:0000305"
FT CONFLICT 1050
FT /note="D -> N (in Ref. 3; AAD16120)"
FT /evidence="ECO:0000305"
FT CONFLICT 1056
FT /note="N -> D (in Ref. 1; AAF42472 and 3; AAD16120)"
FT /evidence="ECO:0000305"
FT CONFLICT 1062
FT /note="D -> G (in Ref. 1; AAF42472)"
FT /evidence="ECO:0000305"
FT CONFLICT 1077
FT /note="D -> E (in Ref. 3; AAD16120)"
FT /evidence="ECO:0000305"
FT CONFLICT 1083
FT /note="E -> D (in Ref. 1; AAF42472 and 3; AAD16120)"
FT /evidence="ECO:0000305"
FT CONFLICT 1090..1140
FT /note="Missing (in Ref. 1; AAF42472 and 3; AAD16120)"
FT /evidence="ECO:0000305"
FT CONFLICT 1143
FT /note="D -> E (in Ref. 1; AAF42472)"
FT /evidence="ECO:0000305"
FT CONFLICT 1149
FT /note="E -> D (in Ref. 1; AAF42472)"
FT /evidence="ECO:0000305"
FT CONFLICT 1152
FT /note="D -> N (in Ref. 3; AAD16120)"
FT /evidence="ECO:0000305"
FT CONFLICT 1180
FT /note="S -> R (in Ref. 3; AAD16120)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1301 AA; 131151 MW; E0D86B52F5E53D05 CRC64;
MKIITYFCIW AVAWAIPVPQ SKPLERHVEK SMNLHLLARS NVSVQDELNA SGTIKESGVL
VHEGDRGRQE NTQDGHKGEG NGSKWAEVGG KSFSTYSTLA NEEGNIEGWN GDTGKAETYG
HDGIHGKEEN ITANGIQGQV SIIDNAGATN RSNTNGNTDK NTQNGDVGDA GHNEDVAVVQ
EDGPQVAGSN NSTDNEDEII ENSCRNEGNT SEITPQINSK RNGTKEAEVT PGTGEDAGLD
NSDGSPSGNG ADEDEDEGSG DDEDEEAGNG KDSSNNSKGQ EGQDHGKEDD HDSSIGQNSD
SKEYYDPEGK EDPHNEVDGD KTSKSEENSA GIPEDNGSQR IEDTQKLNHR ESKRVENRIT
KESETHAVGK SQDKGIEIKG PSSGNRNITK EVGKGNEGKE DKGQHGMILG KGNVKTQGEV
VNIEGPGQKS EPGNKVGHSN TGSDSNSDGY DSYDFDDKSM QGDDPNSSDE SNGNDDANSE
SDNNSSSRGD ASYNSDESKD NGNGSDSKGA EDDDSDSTSD TNNSDSNGNG NNGNDDNDKS
DSGKGKSDSS DSDSSDSSNS SDSSDSSDSD SSDSNSSSDS DSSDSDSSDS SDSDSSDSSN
SSDSSDSSDS SDSSDSSDSS DSKSDSSKSE SDSSDSDSKS DSSDSNSSDS SDNSDSSDSS
NSSNSSDSSD SSDSSDSSSS SDSSNSSDSS DSSDSSNSSE SSDSSDSSDS DSSDSSDSSN
SNSSDSDSSN SSDSSDSSNS SDSSDSSDSS NSSDSSDSSD SSNSSDSSDS SDSSDSSDSS
NSSDSNDSSN SSDSSDSSNS SDSSNSSDSS DSSDSSDSDS SNSSDSSNSS DSSDSSNSSD
SSDSSDSSDG SDSDSSNRSD SSNSSDSSDS SDSSNSSDSS DSSDSNESSN SSDSSDSSNS
SDSDSSDSSN SSDSSDSSNS SDSSESSNSS DNSNSSDSSN SSDSSDSSDS SNSSDSSNSS
DSSNSSDSSD SNSSDSSDSS NSSDSSDSSD SSDSSDSSDS SNSSDSSDSS DSSDSSNSSD
SSNSSDSSNS SDSSDSSDSS DSSDSSDSSD SSDSSNSSDS SDSSDSSDSS DSSDSSDSSD
SSESSDSSDS SNSSDSSDSS DSSDSSDSSD SSDSSDSSDS SNSSDSSDSS DSSDSSDSSN
SSDSSDSSES SDSSDSSDSS DSSDSSDSSD SSDSSDSSNS SDSSDSSDSS DSSDSSDSSD
SSDSSDSSDS SDSSDSSDSS DSSDSSDSSD SNESSDSSDS SDSSDSSNSS DSSDSSDSSD
STSDSNDESD SQSKSGNGNN NGSDSDSDSE GSDSNHSTSD D
//
