MEPE_HUMAN
ID MEPE_HUMAN Reviewed; 525 AA.
AC Q9NQ76; A1A4X9; A8MTA3; D2CFR4; F5H5C5;
DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Matrix extracellular phosphoglycoprotein {ECO:0000303|PubMed:10945470};
DE AltName: Full=Osteoblast/osteocyte factor 45 {ECO:0000250|UniProtKB:Q8K4L6};
DE Short=OF45 {ECO:0000250|UniProtKB:Q8K4L6};
DE AltName: Full=Osteoregulin {ECO:0000303|PubMed:12489176};
DE Flags: Precursor;
GN Name=MEPE;
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 [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Bone;
RX PubMed=10945470; DOI=10.1006/geno.2000.6235;
RA Rowe P.S.N., de Zoysa P.A., Dong R., Wang H.R., White K.E., Econs M.J.,
RA Oudet C.L.;
RT "MEPE, a new gene expressed in bone marrow and tumors causing
RT osteomalacia.";
RL Genomics 67:54-68(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Bone;
RX PubMed=11414762; DOI=10.1006/geno.2001.6553;
RA Argiro L., Desbarats M., Glorieux F.H., Ecarot B.;
RT "Mepe, the gene encoding a tumor-secreted protein in oncogenic
RT hypophosphatemic osteomalacia, is expressed in bone.";
RL Genomics 74:342-351(2001).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 10-101 (ISOFORM 2), AND ALTERNATIVE SPLICING.
RA Wang X., Wang Y.;
RT "A Human MEPE new exon between formerly identified exon 3 and exon 4.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEOLYTIC CLEAVAGE.
RX PubMed=12220505; DOI=10.1016/s0006-291x(02)02125-3;
RA Guo R., Rowe P.S., Liu S., Simpson L.G., Xiao Z.S., Quarles L.D.;
RT "Inhibition of MEPE cleavage by Phex.";
RL Biochem. Biophys. Res. Commun. 297:38-45(2002).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=12489176; DOI=10.1080/03008200290000556;
RA MacDougall M., Simmons D., Gu T.T., Dong J.;
RT "MEPE/OF45, a new dentin/bone matrix protein and candidate gene for dentin
RT diseases mapping to chromosome 4q21.";
RL Connect. Tissue Res. 43:320-330(2002).
RN [9]
RP FUNCTION.
RX PubMed=14962809; DOI=10.1016/j.bone.2003.10.005;
RA Rowe P.S., Kumagai Y., Gutierrez G., Garrett I.R., Blacher R., Rosen D.,
RA Cundy J., Navvab S., Chen D., Drezner M.K., Quarles L.D., Mundy G.R.;
RT "MEPE has the properties of an osteoblastic phosphatonin and minhibin.";
RL Bone 34:303-319(2004).
RN [10]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15108058; DOI=10.1007/s00774-003-0468-9;
RA Nampei A., Hashimoto J., Hayashida K., Tsuboi H., Shi K., Tsuji I.,
RA Miyashita H., Yamada T., Matsukawa N., Matsumoto M., Morimoto S.,
RA Ogihara T., Ochi T., Yoshikawa H.;
RT "Matrix extracellular phosphoglycoprotein (MEPE) is highly expressed in
RT osteocytes in human bone.";
RL J. Bone Miner. Metab. 22:176-184(2004).
RN [11]
RP DOMAIN.
RX PubMed=15040834; DOI=10.1359/jbmr.0301263;
RA Hayashibara T., Hiraga T., Yi B., Nomizu M., Kumagai Y., Nishimura R.,
RA Yoneda T.;
RT "A synthetic peptide fragment of human MEPE stimulates new bone formation
RT in vitro and in vivo.";
RL J. Bone Miner. Res. 19:455-462(2004).
RN [12]
RP TISSUE SPECIFICITY, AND DOMAIN.
RX PubMed=15153459; DOI=10.1177/154405910408300612;
RA Liu H., Li W., Gao C., Kumagai Y., Blacher R.W., DenBesten P.K.;
RT "Dentonin, a fragment of MEPE, enhanced dental pulp stem cell
RT proliferation.";
RL J. Dent. Res. 83:496-499(2004).
RN [13]
RP TISSUE SPECIFICITY.
RX PubMed=15329369; DOI=10.1177/154405910408300902;
RA Ogbureke K.U., Fisher L.W.;
RT "Expression of SIBLINGs and their partner MMPs in salivary glands.";
RL J. Dent. Res. 83:664-670(2004).
RN [14]
RP INTERACTION WITH PHEX, AND DOMAIN.
RX PubMed=15664000; DOI=10.1016/j.bone.2004.09.015;
RA Rowe P.S., Garrett I.R., Schwarz P.M., Carnes D.L., Lafer E.M., Mundy G.R.,
RA Gutierrez G.E.;
RT "Surface plasmon resonance (SPR) confirms that MEPE binds to PHEX via the
RT MEPE-ASARM motif: a model for impaired mineralization in X-linked rickets
RT (HYP).";
RL Bone 36:33-46(2005).
RN [15]
RP FUNCTION, INTERACTION WITH PHEX, AND DOMAIN.
RX PubMed=18162525; DOI=10.1210/en.2007-1205;
RA Martin A., David V., Laurence J.S., Schwarz P.M., Lafer E.M., Hedge A.M.,
RA Rowe P.S.;
RT "Degradation of MEPE, DMP1, and release of SIBLING ASARM-peptides
RT (minhibins): ASARM-peptide(s) are directly responsible for defective
RT mineralization in HYP.";
RL Endocrinology 149:1757-1772(2008).
RN [16]
RP DOMAIN.
RX PubMed=18597632; DOI=10.1359/jbmr.080601;
RA Addison W.N., Nakano Y., Loisel T., Crine P., McKee M.D.;
RT "MEPE-ASARM peptides control extracellular matrix mineralization by binding
RT to hydroxyapatite: an inhibition regulated by PHEX cleavage of ASARM.";
RL J. Bone Miner. Res. 23:1638-1649(2008).
RN [17]
RP TISSUE SPECIFICITY.
RX PubMed=18547474; DOI=10.1177/039463200802100207;
RA Tete S., Nargi E., Mastrangelo F., Zizzari V., D'Apolito G., Traini T.,
RA Costanzo G., Dadorante V., D'Alimonte I., Caputi S., Caciagli F.,
RA Ciccarelli R.;
RT "Changes in matrix extracellular phosphoglycoprotein expression before and
RT during in vitro osteogenic differentiation of human dental papilla
RT mesenchymal cells.";
RL Int. J. Immunopathol. Pharmacol. 21:309-318(2008).
RN [18]
RP FUNCTION.
RX PubMed=19005008; DOI=10.1681/asn.2008030315;
RA Marks J., Churchill L.J., Debnam E.S., Unwin R.J.;
RT "Matrix extracellular phosphoglycoprotein inhibits phosphate transport.";
RL J. Am. Soc. Nephrol. 19:2313-2320(2008).
RN [19]
RP FUNCTION, DOMAIN, AND PHOSPHORYLATION.
RX PubMed=19998030; DOI=10.1007/s00223-009-9313-z;
RA Boskey A.L., Chiang P., Fermanis A., Brown J., Taleb H., David V.,
RA Rowe P.S.;
RT "MEPE's diverse effects on mineralization.";
RL Calcif. Tissue Int. 86:42-46(2010).
RN [20]
RP FUNCTION, TISSUE SPECIFICITY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=20581062; DOI=10.2353/ajpath.2010.091231;
RA Boukpessi T., Gaucher C., Leger T., Salmon B., Le Faouder J., Willig C.,
RA Rowe P.S., Garabedian M., Meilhac O., Chaussain C.;
RT "Abnormal presence of the matrix extracellular phosphoglycoprotein-derived
RT acidic serine- and aspartate-rich motif peptide in human hypophosphatemic
RT dentin.";
RL Am. J. Pathol. 177:803-812(2010).
RN [21]
RP FUNCTION, AND DOMAIN.
RX PubMed=22766095; DOI=10.1016/j.bone.2012.06.022;
RA Staines K.A., Mackenzie N.C., Clarkin C.E., Zelenchuk L., Rowe P.S.,
RA MacRae V.E., Farquharson C.;
RT "MEPE is a novel regulator of growth plate cartilage mineralization.";
RL Bone 51:418-430(2012).
RN [22]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=22341070; DOI=10.1016/j.joen.2011.10.015;
RA Wei X., Liu L., Zhou X., Zhang F., Ling J.;
RT "The effect of matrix extracellular phosphoglycoprotein and its downstream
RT osteogenesis-related gene expression on the proliferation and
RT differentiation of human dental pulp cells.";
RL J. Endod. 38:330-338(2012).
RN [23]
RP PHOSPHORYLATION BY FAM20C.
RX PubMed=22582013; DOI=10.1126/science.1217817;
RA Tagliabracci V.S., Engel J.L., Wen J., Wiley S.E., Worby C.A., Kinch L.N.,
RA Xiao J., Grishin N.V., Dixon J.E.;
RT "Secreted kinase phosphorylates extracellular proteins that regulate
RT biomineralization.";
RL Science 336:1150-1153(2012).
CC -!- FUNCTION: Promotes renal phosphate excretion and inhibits intestinal
CC phosphate absorption (PubMed:14962809, PubMed:19005008). Promotes bone
CC mineralization by osteoblasts and cartilage mineralization by
CC chondrocytes (PubMed:18162525, PubMed:19998030, PubMed:22766095).
CC Regulates the mineralization of the extracellular matrix of the
CC craniofacial complex, such as teeth, bone and cartilage (By
CC similarity). Promotes dental pulp stem cell proliferation and
CC differentiation (PubMed:22341070). {ECO:0000250|UniProtKB:Q8K4L6,
CC ECO:0000269|PubMed:14962809, ECO:0000269|PubMed:18162525,
CC ECO:0000269|PubMed:19005008, ECO:0000269|PubMed:19998030,
CC ECO:0000269|PubMed:22341070, ECO:0000269|PubMed:22766095}.
CC -!- SUBUNIT: Interacts (via the ASARM motif) with PHEX; the interaction is
CC zinc-dependent. {ECO:0000269|PubMed:15664000,
CC ECO:0000269|PubMed:18162525}.
CC -!- INTERACTION:
CC Q9NQ76; P16333: NCK1; NbExp=3; IntAct=EBI-1753293, EBI-389883;
CC Q9NQ76; P78562: PHEX; NbExp=2; IntAct=EBI-1753293, EBI-2827676;
CC Q9NQ76; Q2QGD7: ZXDC; NbExp=3; IntAct=EBI-1753293, EBI-1538838;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000269|PubMed:11414762, ECO:0000269|PubMed:15108058}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9NQ76-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NQ76-2; Sequence=VSP_043986;
CC Name=3;
CC IsoId=Q9NQ76-3; Sequence=VSP_046892;
CC -!- TISSUE SPECIFICITY: Expressed by osteoblasts (PubMed:10945470,
CC PubMed:11414762, PubMed:15108058). Expressed by stem cells in dental
CC pulp (PubMed:15153459). Expressed by mesenchymal cells in dental
CC papilla and dental pulp (PubMed:18547474, PubMed:22341070). Expressed
CC in teeth, specifically in decidious dentin (PubMed:20581062). Expressed
CC in ondotoblasts (PubMed:12489176). Expressed in salivary glands
CC (PubMed:15329369). Secreted from oncogenic hypophosphatemic tumors
CC (PubMed:11414762). {ECO:0000269|PubMed:10945470,
CC ECO:0000269|PubMed:11414762, ECO:0000269|PubMed:12489176,
CC ECO:0000269|PubMed:15108058, ECO:0000269|PubMed:15153459,
CC ECO:0000269|PubMed:15329369, ECO:0000269|PubMed:18547474,
CC ECO:0000269|PubMed:20581062, ECO:0000269|PubMed:22341070}.
CC -!- DOMAIN: The acidic serine aspartate-rich MEPE-associated (ASARM) motif
CC is sufficient when phosphorylated to inhibit bone mineralization by
CC osteoblasts and cartilage mineralization by chondrocytes by binding
CC hydroxyapatite crystals during the mineralization stage
CC (PubMed:15664000, PubMed:18162525, PubMed:18597632, PubMed:19998030,
CC PubMed:22766095). It can also inhibit dentin mineralization
CC (PubMed:20581062). {ECO:0000269|PubMed:15664000,
CC ECO:0000269|PubMed:18162525, ECO:0000269|PubMed:18597632,
CC ECO:0000269|PubMed:19998030, ECO:0000269|PubMed:20581062,
CC ECO:0000269|PubMed:22766095}.
CC -!- DOMAIN: The dentonin region is sufficient to promote dental pulp stem
CC cell proliferation (PubMed:15153459). It can also stimulate bone
CC formation, osteoblast differentiation, and activate integrin signaling
CC pathways (PubMed:15040834). {ECO:0000269|PubMed:15040834,
CC ECO:0000269|PubMed:15153459}.
CC -!- PTM: Phosphorylated on serine residues in the ASARM motif (in vitro) by
CC FAM20C; the phosphorylation is important for the inhibition of bone
CC mineralization (PubMed:19998030, PubMed:22582013).
CC {ECO:0000269|PubMed:19998030, ECO:0000269|PubMed:22582013}.
CC -!- PTM: Cleaved by CTSB/cathepsin B; the cleavage is blocked by
CC metalloprotease PHEX. {ECO:0000269|PubMed:12220505}.
CC -!- SIMILARITY: Belongs to the PF07175/osteoregulin family. {ECO:0000305}.
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DR EMBL; AJ276396; CAB97250.1; -; mRNA.
DR EMBL; AF325916; AAK70343.1; -; mRNA.
DR EMBL; AC093768; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471057; EAX06001.1; -; Genomic_DNA.
DR EMBL; CH471057; EAX06002.1; -; Genomic_DNA.
DR EMBL; BC128158; AAI28159.1; -; mRNA.
DR EMBL; DQ854717; ABI64294.1; -; mRNA.
DR CCDS; CCDS3625.1; -. [Q9NQ76-1]
DR CCDS; CCDS54776.1; -. [Q9NQ76-3]
DR CCDS; CCDS77940.1; -. [Q9NQ76-2]
DR RefSeq; NP_001171623.1; NM_001184694.2. [Q9NQ76-1]
DR RefSeq; NP_001171624.1; NM_001184695.1. [Q9NQ76-3]
DR RefSeq; NP_001171625.1; NM_001184696.1. [Q9NQ76-3]
DR RefSeq; NP_001171626.1; NM_001184697.1. [Q9NQ76-3]
DR RefSeq; NP_001278112.1; NM_001291183.1. [Q9NQ76-2]
DR RefSeq; NP_064588.1; NM_020203.3. [Q9NQ76-1]
DR RefSeq; XP_006714341.1; XM_006714278.2. [Q9NQ76-2]
DR AlphaFoldDB; Q9NQ76; -.
DR BioGRID; 121279; 46.
DR IntAct; Q9NQ76; 15.
DR STRING; 9606.ENSP00000416984; -.
DR GlyGen; Q9NQ76; 2 sites.
DR iPTMnet; Q9NQ76; -.
DR PhosphoSitePlus; Q9NQ76; -.
DR BioMuta; MEPE; -.
DR DMDM; 33112396; -.
DR EPD; Q9NQ76; -.
DR MassIVE; Q9NQ76; -.
DR PaxDb; Q9NQ76; -.
DR PeptideAtlas; Q9NQ76; -.
DR PRIDE; Q9NQ76; -.
DR ProteomicsDB; 26838; -.
DR ProteomicsDB; 82096; -. [Q9NQ76-1]
DR ProteomicsDB; 82097; -. [Q9NQ76-2]
DR Antibodypedia; 44860; 178 antibodies from 27 providers.
DR DNASU; 56955; -.
DR Ensembl; ENST00000361056.4; ENSP00000354341.3; ENSG00000152595.17. [Q9NQ76-1]
DR Ensembl; ENST00000395102.8; ENSP00000378534.4; ENSG00000152595.17. [Q9NQ76-2]
DR Ensembl; ENST00000424957.8; ENSP00000416984.3; ENSG00000152595.17. [Q9NQ76-1]
DR GeneID; 56955; -.
DR KEGG; hsa:56955; -.
DR MANE-Select; ENST00000361056.4; ENSP00000354341.3; NM_020203.6; NP_064588.1.
DR UCSC; uc003hqy.4; human. [Q9NQ76-1]
DR CTD; 56955; -.
DR DisGeNET; 56955; -.
DR GeneCards; MEPE; -.
DR HGNC; HGNC:13361; MEPE.
DR HPA; ENSG00000152595; Tissue enriched (brain).
DR MIM; 605912; gene.
DR neXtProt; NX_Q9NQ76; -.
DR OpenTargets; ENSG00000152595; -.
DR PharmGKB; PA30755; -.
DR VEuPathDB; HostDB:ENSG00000152595; -.
DR eggNOG; ENOG502SW2S; Eukaryota.
DR GeneTree; ENSGT00390000010702; -.
DR HOGENOM; CLU_039303_0_0_1; -.
DR InParanoid; Q9NQ76; -.
DR OMA; HEKHGYY; -.
DR OrthoDB; 962767at2759; -.
DR PhylomeDB; Q9NQ76; -.
DR TreeFam; TF338655; -.
DR PathwayCommons; Q9NQ76; -.
DR Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
DR SignaLink; Q9NQ76; -.
DR BioGRID-ORCS; 56955; 22 hits in 1058 CRISPR screens.
DR GeneWiki; MEPE; -.
DR GenomeRNAi; 56955; -.
DR Pharos; Q9NQ76; Tbio.
DR PRO; PR:Q9NQ76; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q9NQ76; protein.
DR Bgee; ENSG00000152595; Expressed in tibia and 43 other tissues.
DR ExpressionAtlas; Q9NQ76; baseline and differential.
DR Genevisible; Q9NQ76; HS.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:1990430; F:extracellular matrix protein binding; IBA:GO_Central.
DR GO; GO:0005201; F:extracellular matrix structural constituent; TAS:ProtInc.
DR GO; GO:0031214; P:biomineral tissue development; IBA:GO_Central.
DR GO; GO:0001501; P:skeletal system development; TAS:ProtInc.
DR InterPro; IPR009837; MEPE.
DR PANTHER; PTHR16510; PTHR16510; 1.
DR Pfam; PF07175; Osteoregulin; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Biomineralization; Extracellular matrix;
KW Glycoprotein; Phosphoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..525
FT /note="Matrix extracellular phosphoglycoprotein"
FT /id="PRO_0000021668"
FT REGION 24..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 242..264
FT /note="Dentonin"
FT /evidence="ECO:0000305|PubMed:15040834,
FT ECO:0000305|PubMed:15153459"
FT REGION 507..525
FT /note="ASARM motif; interaction with PHEX"
FT /evidence="ECO:0000305|PubMed:22766095"
FT MOTIF 247..249
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT COMPBIAS 29..76
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..202
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..307
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..389
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..498
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 477
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 478
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..113
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_046892"
FT VAR_SEQ 36
FT /note="R -> RITYKGHYEKHGHYVFKCVYMSPEKKNQTDVK (in isoform
FT 2)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_043986"
FT VARIANT 330
FT /note="V -> I (in dbSNP:rs17013285)"
FT /id="VAR_034094"
SQ SEQUENCE 525 AA; 58419 MW; 0977CA6E871CA9E5 CRC64;
MRVFCVGLLL FSVTWAAPTF QPQTEKTKQS CVEEQRQEEK NKDNIGFHHL GKRINQELSS
KENIVQERKK DLSLSEASEN KGSSKSQNYF TNRQRLNKEY SISNKENTHN GLRMSIYPKS
TGNKGFEDGD DAISKLHDQE EYGAALIRNN MQHIMGPVTA IKLLGEENKE NTPRNVLNII
PASMNYAKAH SKDKKKPQRD SQAQKSPVKS KSTHRIQHNI DYLKHLSKVK KIPSDFEGSG
YTDLQERGDN DISPFSGDGQ PFKDIPGKGE ATGPDLEGKD IQTGFAGPSE AESTHLDTKK
PGYNEIPERE ENGGNTIGTR DETAKEADAV DVSLVEGSND IMGSTNFKEL PGREGNRVDA
GSQNAHQGKV EFHYPPAPSK EKRKEGSSDA AESTNYNEIP KNGKGSTRKG VDHSNRNQAT
LNEKQRFPSK GKSQGLPIPS RGLDNEIKNE MDSFNGPSHE NIITHGRKYH YVPHRQNNST
RNKGMPQGKG SWGRQPHSNR RFSSRRRDDS SESSDSGSSS ESDGD
