MEPE_MOUSE
ID MEPE_MOUSE Reviewed; 441 AA.
AC Q8K4L6; D6C6N6; Q3TYZ5; Q924I1;
DT 12-SEP-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Matrix extracellular phosphoglycoprotein {ECO:0000303|PubMed:11414762};
DE AltName: Full=Osteoblast/osteocyte factor 45 {ECO:0000303|PubMed:12421822};
DE Short=OF45 {ECO:0000303|PubMed:12421822};
DE AltName: Full=Osteoregulin {ECO:0000250|UniProtKB:Q9ES02};
DE Flags: Precursor;
GN Name=Mepe {ECO:0000312|MGI:MGI:2137384};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000312|EMBL:AAM87687.1};
RN [1] {ECO:0000312|EMBL:AAK70342.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAK70342.1};
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 [2] {ECO:0000312|EMBL:AAM87687.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12421822; DOI=10.1074/jbc.m203250200;
RA Gowen L.C., Petersen D.N., Mansolf A.L., Qi H., Stock J.L., Tkalcevic G.T.,
RA Simmons H.A., Crawford D.T., Chidsey-Frink K.L., Ke H.Z., McNeish J.D.,
RA Brown T.A.;
RT "Targeted disruption of the osteoblast/osteocyte factor 45 gene (OF45)
RT results in increased bone formation and bone mass.";
RL J. Biol. Chem. 278:1998-2007(2003).
RN [3] {ECO:0000312|EMBL:ACS37545.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=19924383; DOI=10.1007/s00018-009-0185-1;
RA Bardet C., Delgado S., Sire J.Y.;
RT "MEPE evolution in mammals reveals regions and residues of prime functional
RT importance.";
RL Cell. Mol. Life Sci. 67:305-320(2010).
RN [4] {ECO:0000312|EMBL:BAE34415.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE34415.1};
RC TISSUE=Inner ear {ECO:0000312|EMBL:BAE34415.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5] {ECO:0000312|EMBL:AAM87687.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [6] {ECO:0000312|EMBL:AAI19163.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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] {ECO:0000305}
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=15221418; DOI=10.1007/s00418-004-0653-5;
RA Lu C., Huang S., Miclau T., Helms J.A., Colnot C.;
RT "Mepe is expressed during skeletal development and regeneration.";
RL Histochem. Cell Biol. 121:493-499(2004).
RN [8] {ECO:0000305}
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 [9] {ECO:0000305}
RP FUNCTION, PHOSPHORYLATION, AND DISRUPTION PHENOTYPE.
RX PubMed=15843468; DOI=10.1681/asn.2004121060;
RA Liu S., Brown T.A., Zhou J., Xiao Z.S., Awad H., Guilak F., Quarles L.D.;
RT "Role of matrix extracellular phosphoglycoprotein in the pathogenesis of X-
RT linked hypophosphatemia.";
RL J. Am. Soc. Nephrol. 16:1645-1653(2005).
RN [10] {ECO:0000305}
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND PHOSPHORYLATION.
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 [11] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, AND PHOSPHORYLATION.
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 [12] {ECO:0000305}
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=22042093; DOI=10.1007/s10735-011-9368-9;
RA Hou C., Liu Z.X., Tang K.L., Wang M.G., Sun J., Wang J., Li S.;
RT "Developmental changes and regional localization of Dspp, Mepe, Mimecan and
RT Versican in postnatal developing mouse teeth.";
RL J. Mol. Histol. 43:9-16(2012).
RN [13] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DOMAIN, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=26051469; DOI=10.1016/j.bone.2015.05.030;
RA Zelenchuk L.V., Hedge A.M., Rowe P.S.;
RT "Age dependent regulation of bone-mass and renal function by the MEPE
RT ASARM-motif.";
RL Bone 79:131-142(2015).
RN [14] {ECO:0000305}
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=26428891; DOI=10.4081/ejh.2015.2553;
RA Fujikawa K., Yokohama-Tamaki T., Morita T., Baba O., Qin C., Shibata S.;
RT "An in situ hybridization study of perlecan, DMP1, and MEPE in developing
RT condylar cartilage of the fetal mouse mandible and limb bud cartilage.";
RL Eur. J. Histochem. 59:2553-2553(2015).
RN [15] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=26927967; DOI=10.1369/0022155416635569;
RA Gullard A., Gluhak-Heinrich J., Papagerakis S., Sohn P., Unterbrink A.,
RA Chen S., MacDougall M.;
RT "MEPE Localization in the Craniofacial Complex and Function in Tooth Dentin
RT Formation.";
RL J. Histochem. Cytochem. 64:224-236(2016).
CC -!- FUNCTION: Regulates renal phosphate and uric acid excretion
CC (PubMed:26051469). Regulates bone mineralization by osteoblasts and
CC cartilage mineralization by chondrocytes (PubMed:11414762,
CC PubMed:12421822, PubMed:15843468, PubMed:22766095). Regulates the
CC mineralization of the extracellular matrix of the craniofacial complex,
CC such as teeth, bone and cartilage (PubMed:26927967). Increases dental
CC pulp stem cell proliferation (By similarity).
CC {ECO:0000250|UniProtKB:Q9NQ76, ECO:0000269|PubMed:11414762,
CC ECO:0000269|PubMed:12421822, ECO:0000269|PubMed:15843468,
CC ECO:0000269|PubMed:22766095, ECO:0000269|PubMed:26051469,
CC ECO:0000269|PubMed:26927967}.
CC -!- SUBUNIT: Interacts (via ASARM motif) with PHEX; the interaction is
CC zinc-dependent. {ECO:0000250|UniProtKB:Q9NQ76}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000269|PubMed:12421822, ECO:0000269|PubMed:18597632,
CC ECO:0000269|PubMed:26051469}.
CC -!- TISSUE SPECIFICITY: Expressed in osteocytes (at protein level)
CC (PubMed:12421822, PubMed:15221418). Expressed by chondrocytes,
CC specifically in the hypertrophic zone of the bone growth plate (at
CC protein level) (PubMed:22766095). Expressed in osteoblasts in bone (at
CC protein level) (PubMed:11414762, PubMed:15221418, PubMed:18597632).
CC Expressed by osteoblasts within the metaphysis (at protein level)
CC (PubMed:15221418, PubMed:22766095). Expressed at low levels in white
CC fat, brown fat, testes, brain and aorta (PubMed:12421822). Expressed in
CC the craniofacial complex (at protein level) (PubMed:26927967).
CC Expressed in odontoblasts, ameloblasts and in predentin during tooth
CC development (at protein level) (PubMed:22042093). Expressed in the
CC kidney (at protein level) (PubMed:26051469). Expressed in osteocytes in
CC mandibular condylar cartilage and tibial cartilage (at protein level)
CC (PubMed:26428891). Expressed in salivary glands (PubMed:15329369).
CC {ECO:0000269|PubMed:11414762, ECO:0000269|PubMed:12421822,
CC ECO:0000269|PubMed:15329369, ECO:0000269|PubMed:18597632,
CC ECO:0000269|PubMed:22042093, ECO:0000269|PubMed:22766095,
CC ECO:0000269|PubMed:26051469, ECO:0000269|PubMed:26428891,
CC ECO:0000269|PubMed:26927967}.
CC -!- DEVELOPMENTAL STAGE: Detected at 16 days post coitum (dpc) in both
CC epithelial and mesenchymal components of the tooth organ
CC (PubMed:26927967). Also detected at 16 dpc and 18 dpc in mandibular
CC bone osteocytes (PubMed:26428891). Detected at 15 dpc in the bone
CC collar (PubMed:26428891). Detected at 13 dpc in the cartilage matrix
CC (PubMed:26428891). Detected at postnatal day 3 in odontoblasts and
CC ameloblasts (PubMed:22042093). At postnatal day 5, expression is
CC decreased in dental papilla cells, but increased in the predentin
CC (PubMed:22042093). By postnatal day 9, is only detected in the
CC predentin (PubMed:22042093). Detected at postnatal day 2 in
CC osteoblasts, the calcified cartilage cores in primary metaphyseal bone
CC and in osterocytes embedded in cortical bone matrix (PubMed:15221418).
CC At postnatal day 84 expression is detected in the osteocytes of
CC cortical and trabecular bone (PubMed:15221418).
CC {ECO:0000269|PubMed:15221418, ECO:0000269|PubMed:22042093,
CC ECO:0000269|PubMed:26428891, ECO:0000269|PubMed:26927967}.
CC -!- INDUCTION: Induced by ascorbate and beta-glycerophosphate
CC (PubMed:11414762, PubMed:12421822). Induced expression during bone
CC fracture healing, with low levels of expression being detected in
CC fibroblast-like cells at 6 days post-fracture, and increased expression
CC at 10 days post-fracture in late hypertrophic chondrocytes. At 14 days
CC post-fracture, expression is detected in osteocytes, osteoblasts, and
CC hypertrophic chondrocytes. By 28 days post-fracture, expression was
CC highest in osteocytes and lower in osteoblasts (PubMed:15221418). Down-
CC regulated by 1-alpha-25-dihydroxyvitamin D3 (calcitriol)
CC (PubMed:11414762). {ECO:0000269|PubMed:11414762,
CC ECO:0000269|PubMed:12421822, ECO:0000269|PubMed:15221418}.
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:15843468, PubMed:22766095, PubMed:26051469). It can also
CC inhibit dentin mineralization (By similarity).
CC {ECO:0000250|UniProtKB:Q9NQ76, ECO:0000269|PubMed:15843468,
CC ECO:0000269|PubMed:22766095, ECO:0000269|PubMed:26051469}.
CC -!- DOMAIN: The dentonin region is sufficient to promote dental pulp stem
CC cell proliferation. It can also stimulate bone formation, osteoblast
CC differentiation, and activate integrin signaling pathways.
CC {ECO:0000250|UniProtKB:Q9NQ76}.
CC -!- PTM: Phosphorylated on serine residues in the ASARM motif; the
CC phosphorylation is important for the inhibition of bone mineralization.
CC {ECO:0000269|PubMed:15843468, ECO:0000269|PubMed:18597632,
CC ECO:0000269|PubMed:22766095}.
CC -!- PTM: Cleaved by CTSB/cathepsin B; the cleavage is blocked by
CC metalloprotease PHEX. {ECO:0000250|UniProtKB:Q9NQ76}.
CC -!- DISRUPTION PHENOTYPE: Mutant mice exhibit increased cancellous bone
CC mass and no loss of trabecular bone characteristics (PubMed:12421822,
CC PubMed:26051469). They also exhibit decreased biomechanical strength in
CC their bones and increased skeletal mineralization (PubMed:15843468). In
CC craniofacial complex development, mutant mice also exhibit
CC hypermineralization in predentin, dentin and enamel of teeth and
CC decreased expression of AMBN, ENAM, IBSP, DMP1, DSPP and SPP1
CC (PubMed:26927967). Mutant mice also exhibit hyperphostatemia and
CC increased expression of SLC34A1/NPT2a, SLC34A3/NPT2c and VEGF in the
CC kidney (PubMed:26051469). Hyperuricemia and reduced fractional
CC excretion of uric acid was also exhibited (PubMed:26051469). As mutant
CC mice age, bone mineral density and content is increased
CC (PubMed:26051469). {ECO:0000269|PubMed:12421822,
CC ECO:0000269|PubMed:15843468, ECO:0000269|PubMed:26051469,
CC ECO:0000269|PubMed:26927967}.
CC -!- MISCELLANEOUS: It has been proposed that MEPE is cleaved and generate 2
CC peptides dentonin and ASARM peptide. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the PF07175/osteoregulin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI19163.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAK70342.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=ACS37545.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF314964; AAK70342.1; ALT_INIT; mRNA.
DR EMBL; AF298661; AAM87687.1; -; mRNA.
DR EMBL; AC122775; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK158231; BAE34415.1; -; mRNA.
DR EMBL; FJ999695; ACS37545.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC119162; AAI19163.1; ALT_INIT; mRNA.
DR CCDS; CCDS51578.1; -.
DR RefSeq; NP_444402.2; NM_053172.2.
DR AlphaFoldDB; Q8K4L6; -.
DR STRING; 10090.ENSMUSP00000065200; -.
DR GlyGen; Q8K4L6; 1 site.
DR iPTMnet; Q8K4L6; -.
DR PhosphoSitePlus; Q8K4L6; -.
DR PaxDb; Q8K4L6; -.
DR PRIDE; Q8K4L6; -.
DR ProteomicsDB; 341483; -.
DR Antibodypedia; 44860; 178 antibodies from 27 providers.
DR Ensembl; ENSMUST00000066207; ENSMUSP00000065200; ENSMUSG00000053863.
DR GeneID; 94111; -.
DR KEGG; mmu:94111; -.
DR UCSC; uc008ykh.2; mouse.
DR CTD; 56955; -.
DR MGI; MGI:2137384; Mepe.
DR VEuPathDB; HostDB:ENSMUSG00000053863; -.
DR eggNOG; ENOG502SW2S; Eukaryota.
DR GeneTree; ENSGT00390000010702; -.
DR HOGENOM; CLU_039303_0_0_1; -.
DR InParanoid; Q8K4L6; -.
DR OMA; HEKHGYY; -.
DR OrthoDB; 962767at2759; -.
DR PhylomeDB; Q8K4L6; -.
DR TreeFam; TF338655; -.
DR Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
DR BioGRID-ORCS; 94111; 2 hits in 72 CRISPR screens.
DR PRO; PR:Q8K4L6; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8K4L6; protein.
DR Bgee; ENSMUSG00000053863; Expressed in hindlimb long bone and 9 other tissues.
DR GO; GO:0031012; C:extracellular matrix; ISO:MGI.
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:0031214; P:biomineral tissue development; IBA:GO_Central.
DR GO; GO:0030282; P:bone mineralization; IMP:MGI.
DR GO; GO:0030502; P:negative regulation of bone mineralization; IDA:MGI.
DR GO; GO:0001501; P:skeletal system development; TAS:MGI.
DR InterPro; IPR009837; MEPE.
DR PANTHER; PTHR16510; PTHR16510; 1.
DR Pfam; PF07175; Osteoregulin; 1.
PE 1: Evidence at protein level;
KW Biomineralization; Extracellular matrix; Glycoprotein; Phosphoprotein;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..441
FT /note="Matrix extracellular phosphoglycoprotein"
FT /evidence="ECO:0000255"
FT /id="PRO_5014107441"
FT REGION 137..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 178..200
FT /note="Dentonin"
FT /evidence="ECO:0000250|UniProtKB:Q9NQ76"
FT REGION 424..441
FT /note="ASARM motif; interaction with PHEX"
FT /evidence="ECO:0000269|PubMed:18597632"
FT MOTIF 183..185
FT /note="Cell attachment site"
FT /evidence="ECO:0000250|UniProtKB:Q9NQ76"
FT COMPBIAS 345..362
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..409
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..441
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 2
FT /note="T -> M (in Ref. 4; BAE34415)"
FT /evidence="ECO:0000305"
FT CONFLICT 14
FT /note="V -> A (in Ref. 4; BAE34415)"
FT /evidence="ECO:0000305"
FT CONFLICT 81
FT /note="R -> G (in Ref. 4; BAE34415)"
FT /evidence="ECO:0000305"
FT CONFLICT 120
FT /note="A -> V (in Ref. 4; BAE34415)"
FT /evidence="ECO:0000305"
FT CONFLICT 132
FT /note="S -> T (in Ref. 4; BAE34415)"
FT /evidence="ECO:0000305"
FT CONFLICT 219
FT /note="L -> V (in Ref. 4; BAE34415)"
FT /evidence="ECO:0000305"
FT CONFLICT 293
FT /note="N -> D (in Ref. 4; BAE34415)"
FT /evidence="ECO:0000305"
FT CONFLICT 340
FT /note="S -> A (in Ref. 4; BAE34415)"
FT /evidence="ECO:0000305"
FT CONFLICT 414
FT /note="N -> H (in Ref. 4; BAE34415)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 441 AA; 46872 MW; AA1947BFE9F2E300 CRC64;
MTPEGLMKMQ AVSVGLLLFS MTWAAPMPNE DRSSCGNQDS IHKDLAASVY PDPTVDEGTE
DGQGALLHPP GQDRYGAALL RNITQPVKSL VTGAELRREG NQEKRPQSVL SVIPADVNDA
KVSLKDIKNQ ESYLLTQSSP VKSKHTKHTR QTRRSTHYLT HLPQIKKTPS DLEGSGSPDL
LVRGDNDVPP FSGDGQHFMH IPGKGGAGSG PESSTSRPLS GSSKAEVIDP HMSGLGSNEI
PGREGHGGSA YATRDKAAQG AGSAGGSLVG GSNEITGSTN FRELPGKEGN RINAGSQNAH
QGKVEFHYPQ VASREKVKGG VEHAGRAGYN EIPKSSKGSS SKDAEESKGN QLTLTASQRF
PGKGKSQGPA LPSHSLSNEV KSEENHYVFH GQNNLTPNKG MSQRRGSWPS RRPNSHRRAS
TRQRDSSESS SSGSSSESHG D
