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MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
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| Description | RecName: Full=Dentin sialophosphoprotein; Contains: RecName: Full=Dentin phosphoprotein; AltName: Full=Dentin phosphophoryn; Short=DPP; Contains: RecName: Full=Dentin sialoprotein; Short=DSP; Flags: Precursor; |
 |
|
| MyHits synonyms | DSPP_HUMAN , Q9NZW4 , A8MUI0 , O95815 , E0D86B52F5E53D05 |
 Legends: 1, Phosphoserine; by CK1. {ECO:0000255}; 2, Phosphoserine. {ECO:0000250|UniProtKB:Q62598}; 3, N-linked (GlcNAc...) asparagine. {ECO:0000255}; 4, VARIANT Y -> D (in DTDP2; the mutant protein does not translocate into the endoplasmic reticulum; dbSNP:rs121912988). {ECO:0000269|PubMed:12354781}; 5, VARIANT A -> V (in DGI2; dominant negative mutation; results in signal peptide retention; the mutant protein is retained within the rough ER membrane; dbSNP:rs121912989). {ECO:0000269|PubMed:14758537, ECO:0000269|PubMed:22392858}; 6, VARIANT P -> L (in DGI3; the mutant protein is largely retained in the ER). {ECO:0000269|PubMed:23509818}; 7, VARIANT P -> S (in DGI2 AND DGI3; dominant negative mutation; the mutant protein is retained intracellularly). {ECO:0000269|PubMed:17627120, ECO:0000269|PubMed:18521831, ECO:0000269|PubMed:22392858}; 8, VARIANT P -> T (in DFNA39/DGI1; dominant negative mutation; the mutant protein is retained intracellularly; dbSNP:rs121912986). {ECO:0000269|PubMed:11175790, ECO:0000269|PubMed:22392858}; 9, VARIANT V -> D (in DGI2; dominant negative mutation; the mutant protein is retained intracellularly). {ECO:0000269|PubMed:21029264, ECO:0000269|PubMed:22392858}; 10, VARIANT V -> F (in DFNA39/DGI1 and DGI3; dbSNP:rs121912987). {ECO:0000269|PubMed:11175790, ECO:0000269|PubMed:15592686}; 11, VARIANT R -> W (in DGI2; dbSNP:rs36094464). {ECO:0000269|PubMed:14758537, ECO:0000269|PubMed:17033625}; 12, VARIANT D -> N (in dbSNP:rs3750025); 13, CONFLICT D -> DSSDSSS (in Ref. 1; AAF42472). {ECO:0000305}; 14, CONFLICT N -> D (in Ref. 3; AAD16120). {ECO:0000305}; 15, CONFLICT S -> C (in Ref. 3; AAD16120). {ECO:0000305}; 16, CONFLICT G -> S (in Ref. 1; AAF42472). {ECO:0000305}; 17, CONFLICT N -> NSSD (in Ref. 1; AAF42472). {ECO:0000305}; 18, CONFLICT S -> G (in Ref. 1; AAF42472). {ECO:0000305}; 19, CONFLICT S -> G (in Ref. 3; AAD16120). {ECO:0000305}; 20, CONFLICT N -> D (in Ref. 1; AAF42472 and 3; AAD16120). {ECO:0000305}; 21, CONFLICT D -> N (in Ref. 1; AAF42472). {ECO:0000305}; 22, CONFLICT D -> N (in Ref. 3; AAD16120). {ECO:0000305}; 23, CONFLICT D -> G (in Ref. 1; AAF42472). {ECO:0000305}; 24, CONFLICT D -> E (in Ref. 3; AAD16120). {ECO:0000305}; 25, CONFLICT E -> D (in Ref. 1; AAF42472 and 3; AAD16120). {ECO:0000305}; 26, CONFLICT D -> E (in Ref. 1; AAF42472). {ECO:0000305}; 27, CONFLICT E -> D (in Ref. 1; AAF42472). {ECO:0000305}; 28, CONFLICT S -> R (in Ref. 3; AAD16120). {ECO:0000305}; 29, SIGNAL {ECO:0000255}; 30, MOTIF Cell attachment site. {ECO:0000255}; 31, CONFLICT Missing (in Ref. 1; AAF42472). {ECO:0000305}; 32, CONFLICT Missing (in Ref. 1; AAF42472 and 3; AAD16120). {ECO:0000305}.
| |
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 10-MAY-2017, entry version 128.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA 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.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA 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.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 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
RT mutations 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.,
RA Yang J., Shi Y., Hu L., Han B., Wang Z., Huang W., Liu J., Chen Z.,
RA Zhao G., Kong X.;
RT "Dentinogenesis imperfecta 1 with or without progressive hearing loss
RT is 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.,
RA Dixon M.J.;
RT "Mutation of the signal peptide region of the bicistronic gene DSPP
RT affects translocation to the endoplasmic reticulum and results in
RT defective dentine 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
RT families 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
RT imperfecta 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
RT bone 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.,
RA Park J.C., 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
RP OF 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
RT of mutant dentin sialophosphoprotein (DSPP) cause dominant negative
RT effects in both dentinogenesis imperfecta and dentin dysplasia by
RT entrapping normal 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
RT characterization of the mutational effect.";
RL Biomed. Res. Int. 2013:948181-948181(2013).
CC -!- FUNCTION: DSP may be an important factor in dentinogenesis. DPP
CC may bind high amount of calcium and facilitate initial
CC mineralization of dentin matrix collagen as well as regulate the
CC size and shape of the 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
CC by the association of progressive sensorineural high-frequency
CC hearing loss with dentinogenesis imperfecta.
CC {ECO:0000269|PubMed:11175790, ECO:0000269|PubMed:22392858}.
CC Note=The disease is caused by mutations affecting the gene
CC represented in this entry.
CC -!- DISEASE: Dentinogenesis imperfecta, Shields type 2 (DGI2)
CC [MIM:125490]: A form of dentinogenesis imperfecta, an autosomal
CC dominant dentin disorder characterized by amber-brown, opalescent
CC teeth that fracture and shed their enamel during mastication,
CC thereby exposing the dentin to rapid wear. Radiographically, the
CC crown appears bulbous and pulpal obliteration is common. The pulp
CC chambers are initially larger than normal prior and immediately
CC after tooth eruption, and then progressively close down to become
CC almost obliterated by abnormal dentin formation. Roots are short
CC and thin. Both primary and permanent teeth are affected. DGI2 is
CC not associated with osteogenesis imperfecta.
CC {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
CC mutations affecting the gene represented in this entry. DSPP
CC defects causing dentin abnormalities act in a dominant negative
CC manner and include missense, splice-site, frameshift mutations. 5'
CC frameshift mutations cause dentin dysplasia while frameshift
CC mutations at the 3' end cause the more severe dentinogenesis
CC imperfecta phenotype (PubMed:18521831 and PubMed:22392858).
CC -!- DISEASE: Dentinogenesis imperfecta, Shields type 3 (DGI3)
CC [MIM:125500]: A form of dentinogenesis imperfecta, an autosomal
CC dominant dentin disorder characterized by amber-brown, opalescent
CC teeth that fracture and shed their enamel during mastication,
CC thereby exposing the dentin to rapid wear. Radiographically, the
CC crown appears bulbous and pulpal obliteration is common. The pulp
CC chambers are initially larger than normal prior and immediately
CC after tooth eruption, and then progressively close down to become
CC almost obliterated by abnormal dentin formation. Roots are short
CC and thin. Both primary and permanent teeth are affected. DGI3
CC teeth typically manifest multiple periapical radiolucencies. DGI3
CC 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
CC mutations affecting the gene represented in this entry. DSPP
CC defects causing dentin abnormalities act in a dominant negative
CC manner and include missense, splice-site, frameshift mutations. 5'
CC frameshift mutations cause dentin dysplasia while frameshift
CC mutations at the 3' end cause the more severe dentinogenesis
CC imperfecta phenotype (PubMed:18521831 and PubMed:22392858).
CC -!- DISEASE: Dentin dysplasia 2 (DTDP2) [MIM:125420]: A dental defect
CC in which the deciduous teeth are opalescent. The permanent teeth
CC are of normal shape, form, and color in most cases. The root
CC length is normal. On radiographs, the pulp chambers of permanent
CC teeth are obliterated, have a thistle-tube deformity and contain
CC pulp stones. {ECO:0000269|PubMed:12354781,
CC ECO:0000269|PubMed:18521831}. Note=The disease is caused by
CC mutations affecting the gene represented in this entry. DSPP
CC defects causing dentin abnormalities act in a dominant negative
CC manner and include missense, splice-site, frameshift mutations. 5'
CC frameshift mutations cause dentin dysplasia while frameshift
CC 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 UniGene; Hs.678914; -.
DR ProteinModelPortal; Q9NZW4; -.
DR STRING; 9606.ENSP00000282478; -.
DR iPTMnet; Q9NZW4; -.
DR PhosphoSitePlus; Q9NZW4; -.
DR BioMuta; DSPP; -.
DR DMDM; 215273974; -.
DR EPD; Q9NZW4; -.
DR PaxDb; Q9NZW4; -.
DR PRIDE; Q9NZW4; -.
DR Ensembl; ENST00000282478; ENSP00000282478; ENSG00000152591.
DR Ensembl; ENST00000399271; ENSP00000382213; ENSG00000152591.
DR GeneID; 1834; -.
DR KEGG; hsa:1834; -.
DR UCSC; uc003hqu.3; human.
DR CTD; 1834; -.
DR DisGeNET; 1834; -.
DR GeneCards; DSPP; -.
DR HGNC; HGNC:3054; DSPP.
DR HPA; HPA036230; -.
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 eggNOG; ENOG410JAJ8; Eukaryota.
DR eggNOG; ENOG4111CIV; LUCA.
DR GeneTree; ENSGT00730000111489; -.
DR HOVERGEN; HBG098252; -.
DR InParanoid; Q9NZW4; -.
DR OMA; GNEGNED; -.
DR OrthoDB; EOG091G0DJR; -.
DR PhylomeDB; Q9NZW4; -.
DR TreeFam; TF318563; -.
DR Reactome; R-HSA-3000178; ECM proteoglycans.
DR GeneWiki; Dentin_sialophosphoprotein_(gene); -.
DR GenomeRNAi; 1834; -.
DR PMAP-CutDB; A8MUI0; -.
DR PRO; PR:Q9NZW4; -.
DR Proteomes; UP000005640; Chromosome 4.
DR Bgee; ENSG00000152591; -.
DR CleanEx; HS_DSPP; -.
DR Genevisible; Q9NZW4; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005578; C:proteinaceous extracellular matrix; TAS:ProtInc.
DR GO; GO:0005509; F:calcium ion binding; TAS:ProtInc.
DR GO; GO:0005518; F:collagen binding; TAS:ProtInc.
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:0030198; P:extracellular matrix organization; TAS:Reactome.
DR GO; GO:0007275; P:multicellular organism development; TAS:ProtInc.
DR GO; GO:0001503; P:ossification; TAS:ProtInc.
DR GO; GO:0001501; P:skeletal system development; TAS:ProtInc.
PE 1: Evidence at protein level;
KW Biomineralization; Calcium; Complete proteome; Deafness;
KW Disease mutation; Extracellular matrix; Glycoprotein; Phosphoprotein;
KW Polymorphism; Reference proteome; Secreted; Sialic acid; Signal.
FT SIGNAL 1 15 {ECO:0000255}.
FT CHAIN 16 1301 Dentin sialophosphoprotein.
FT /FTId=PRO_0000021120.
FT CHAIN 16 462 Dentin sialoprotein.
FT /FTId=PRO_0000021121.
FT CHAIN 463 1301 Dentin phosphoprotein.
FT /FTId=PRO_0000021122.
FT MOTIF 488 490 Cell attachment site. {ECO:0000255}.
FT COMPBIAS 439 1301 Asp/Ser-rich.
FT MOD_RES 259 259 Phosphoserine; by CK1. {ECO:0000255}.
FT MOD_RES 301 301 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q62598}.
FT CARBOHYD 41 41 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 49 49 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 81 81 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 130 130 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 150 150 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 190 190 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 191 191 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 209 209 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 222 222 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 275 275 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 336 336 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 387 387 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT VARIANT 6 6 Y -> D (in DTDP2; the mutant protein does
FT not translocate into the endoplasmic
FT reticulum; dbSNP:rs121912988).
FT {ECO:0000269|PubMed:12354781}.
FT /FTId=VAR_036861.
FT VARIANT 15 15 A -> V (in DGI2; dominant negative
FT mutation; results in signal peptide
FT retention; the mutant protein is retained
FT within the rough ER membrane;
FT dbSNP:rs121912989).
FT {ECO:0000269|PubMed:14758537,
FT ECO:0000269|PubMed:22392858}.
FT /FTId=VAR_036862.
FT VARIANT 17 17 P -> L (in DGI3; the mutant protein is
FT largely retained in the ER).
FT {ECO:0000269|PubMed:23509818}.
FT /FTId=VAR_070252.
FT VARIANT 17 17 P -> S (in DGI2 AND DGI3; dominant
FT negative mutation; the mutant protein is
FT retained intracellularly).
FT {ECO:0000269|PubMed:17627120,
FT ECO:0000269|PubMed:18521831,
FT ECO:0000269|PubMed:22392858}.
FT /FTId=VAR_054443.
FT VARIANT 17 17 P -> T (in DFNA39/DGI1; dominant negative
FT mutation; the mutant protein is retained
FT intracellularly; dbSNP:rs121912986).
FT {ECO:0000269|PubMed:11175790,
FT ECO:0000269|PubMed:22392858}.
FT /FTId=VAR_012280.
FT VARIANT 18 18 V -> D (in DGI2; dominant negative
FT mutation; the mutant protein is retained
FT intracellularly).
FT {ECO:0000269|PubMed:21029264,
FT ECO:0000269|PubMed:22392858}.
FT /FTId=VAR_070253.
FT VARIANT 18 18 V -> F (in DFNA39/DGI1 and DGI3;
FT dbSNP:rs121912987).
FT {ECO:0000269|PubMed:11175790,
FT ECO:0000269|PubMed:15592686}.
FT /FTId=VAR_012281.
FT VARIANT 68 68 R -> W (in DGI2; dbSNP:rs36094464).
FT {ECO:0000269|PubMed:14758537,
FT ECO:0000269|PubMed:17033625}.
FT /FTId=VAR_030661.
FT VARIANT 243 243 D -> N (in dbSNP:rs3750025).
FT /FTId=VAR_047551.
FT CONFLICT 673 673 D -> DSSDSSS (in Ref. 1; AAF42472).
FT {ECO:0000305}.
FT CONFLICT 734 739 Missing (in Ref. 1; AAF42472).
FT {ECO:0000305}.
FT CONFLICT 799 799 N -> D (in Ref. 3; AAD16120).
FT {ECO:0000305}.
FT CONFLICT 836 836 S -> C (in Ref. 3; AAD16120).
FT {ECO:0000305}.
FT CONFLICT 850 850 G -> S (in Ref. 1; AAF42472).
FT {ECO:0000305}.
FT CONFLICT 875 875 N -> NSSD (in Ref. 1; AAF42472).
FT {ECO:0000305}.
FT CONFLICT 960 960 S -> G (in Ref. 1; AAF42472).
FT {ECO:0000305}.
FT CONFLICT 1002 1002 N -> D (in Ref. 3; AAD16120).
FT {ECO:0000305}.
FT CONFLICT 1022 1022 S -> G (in Ref. 3; AAD16120).
FT {ECO:0000305}.
FT CONFLICT 1029 1029 N -> D (in Ref. 1; AAF42472 and 3;
FT AAD16120). {ECO:0000305}.
FT CONFLICT 1044 1044 D -> N (in Ref. 1; AAF42472).
FT {ECO:0000305}.
FT CONFLICT 1050 1050 D -> N (in Ref. 3; AAD16120).
FT {ECO:0000305}.
FT CONFLICT 1056 1056 N -> D (in Ref. 1; AAF42472 and 3;
FT AAD16120). {ECO:0000305}.
FT CONFLICT 1062 1062 D -> G (in Ref. 1; AAF42472).
FT {ECO:0000305}.
FT CONFLICT 1077 1077 D -> E (in Ref. 3; AAD16120).
FT {ECO:0000305}.
FT CONFLICT 1083 1083 E -> D (in Ref. 1; AAF42472 and 3;
FT AAD16120). {ECO:0000305}.
FT CONFLICT 1090 1140 Missing (in Ref. 1; AAF42472 and 3;
FT AAD16120). {ECO:0000305}.
FT CONFLICT 1143 1143 D -> E (in Ref. 1; AAF42472).
FT {ECO:0000305}.
FT CONFLICT 1149 1149 E -> D (in Ref. 1; AAF42472).
FT {ECO:0000305}.
FT CONFLICT 1152 1152 D -> N (in Ref. 3; AAD16120).
FT {ECO:0000305}.
FT CONFLICT 1180 1180 S -> R (in Ref. 3; AAD16120).
FT {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
//
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