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}.
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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   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.
DR   Genevisible; Q9NZW4; HS.
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
//