ENAM_MOUSE
ID ENAM_MOUSE Reviewed; 1274 AA.
AC O55196;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Enamelin;
DE Flags: Precursor;
GN Name=Enam;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=Swiss Webster; TISSUE=Enamel epithelium;
RX PubMed=11062988; DOI=10.3109/03008209809023911;
RA Hu C.-C., Simmer J.P., Bartlett J.D., Nanci A., Qian Q., Zhang C.,
RA Ryu O.H., Xue J., Fukae M., Uchida T., McDougall M.;
RT "Murine enamelin: cDNA and derived protein sequences.";
RL Connect. Tissue Res. 39:47-61(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
CC -!- FUNCTION: Involved in the mineralization and structural organization of
CC enamel. Involved in the extension of enamel during the secretory stage
CC of dental enamel formation. {ECO:0000250|UniProtKB:O97939}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250|UniProtKB:O97939}.
CC -!- TISSUE SPECIFICITY: Expressed in developing teeth.
CC {ECO:0000269|PubMed:11062988}.
CC -!- PTM: Phosphorylated by FAM20C in vitro. {ECO:0000250|UniProtKB:Q9NRM1}.
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DR EMBL; U82698; AAB94312.1; -; mRNA.
DR CCDS; CCDS19400.1; -.
DR PIR; T37193; T37193.
DR RefSeq; NP_059496.1; NM_017468.3.
DR AlphaFoldDB; O55196; -.
DR BioGRID; 199447; 1.
DR STRING; 10090.ENSMUSP00000031222; -.
DR GlyGen; O55196; 6 sites.
DR iPTMnet; O55196; -.
DR PhosphoSitePlus; O55196; -.
DR PaxDb; O55196; -.
DR PRIDE; O55196; -.
DR Antibodypedia; 24350; 79 antibodies from 15 providers.
DR DNASU; 13801; -.
DR Ensembl; ENSMUST00000031222; ENSMUSP00000031222; ENSMUSG00000029286.
DR GeneID; 13801; -.
DR KEGG; mmu:13801; -.
DR UCSC; uc008xzt.2; mouse.
DR CTD; 10117; -.
DR MGI; MGI:1333772; Enam.
DR VEuPathDB; HostDB:ENSMUSG00000029286; -.
DR eggNOG; ENOG502R69E; Eukaryota.
DR GeneTree; ENSGT00440000037826; -.
DR HOGENOM; CLU_280412_0_0_1; -.
DR InParanoid; O55196; -.
DR OMA; WNSWDHR; -.
DR OrthoDB; 201332at2759; -.
DR PhylomeDB; O55196; -.
DR TreeFam; TF337278; -.
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; 13801; 1 hit in 72 CRISPR screens.
DR PRO; PR:O55196; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; O55196; protein.
DR Bgee; ENSMUSG00000029286; Expressed in molar tooth and 11 other tissues.
DR ExpressionAtlas; O55196; baseline and differential.
DR Genevisible; O55196; MM.
DR GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0030345; F:structural constituent of tooth enamel; IDA:MGI.
DR GO; GO:0036305; P:ameloblast differentiation; IMP:MGI.
DR GO; GO:0097186; P:amelogenesis; IMP:MGI.
DR GO; GO:0031214; P:biomineral tissue development; IEA:UniProtKB-KW.
DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IMP:MGI.
DR GO; GO:0070175; P:positive regulation of enamel mineralization; IMP:MGI.
DR GO; GO:0022604; P:regulation of cell morphogenesis; IMP:MGI.
DR InterPro; IPR015673; Enamelin.
DR PANTHER; PTHR16784; PTHR16784; 2.
DR Pfam; PF15362; Enamelin; 2.
PE 1: Evidence at protein level;
KW Biomineralization; Extracellular matrix; Glycoprotein; Phosphoprotein;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..38
FT /evidence="ECO:0000255"
FT CHAIN 39..1274
FT /note="Enamelin"
FT /id="PRO_0000021175"
FT REGION 103..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 668..700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 712..734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 753..814
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1071..1097
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1109..1128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..187
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..243
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..507
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..577
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..612
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 668..684
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 714..728
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 753..783
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 196
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRM1"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRM1"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 252
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 259
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1066
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1274 AA; 140954 MW; F9DBD1CC9D327143 CRC64;
MLLLQCRNPT SPPKPCGLVP NVKMSLLVFL GLLGVSAAMP FQMPMPRMPG FSSKSEEMMR
YNQFNFMNAP PMMPMGPYGN GMPMPPHMPP QYPPYQMPMW PPPVPNGWQQ PPMPNFPSKT
DQTQETAKPN QTNPQEPQPQ KQPLKEPPNE AARAKDDAQP PQPFPPFGNG LYPYPQPPWP
IPQRGPPTAF GRPKFSNEEG NPYYAFFGYH GFGGRPYYSE EMFEDYEKPK EKDPPKPEDP
PPDDPPPEAS TNSTVPDANA TQSIPEGGND TSPIGNTGPG PNAGNNPTVQ NGVFPPPKVN
VSGQGVPKSQ IPWRPSQPNI YENYPYPNYP SERQWQTTGT QGPRQNGPGY RNPQVERGPQ
WNSFAWEGKQ ATRPGNPTYG KPPSPTSGVN YAGNPVHFGR NLPGPNKPFV GANPASNKPF
VGANPASNKP FVGANPASNK PFVGANPASN KPFVGANPAS NKPYVGANPA SNKPFIGANP
AANKPSIGTN PAANKPSIGT NPAANKPFVR NNVGANKPFV GTNPSSNQPF LRSNQASNKP
FMRSNQASNK PFVGTNVASV GPKQVTVSHN MKTQNPKEKS LGQKERTVTP TKDASNPWRS
AKQYGINNPN YNLPRSEGSM VGPNFNSFDQ QENSYFSKGA SKRVPSPNIQ IQSQNLPKGI
ALEPRRTPFQ SETKKPELKH GTHQPAYPKK IPSPTRKHFP AERNTWNRQK ILPPLKEDYG
RQDENLRHPS YGSRGNIFYH EYTNPYHNEK SQYIKSNPWD KSSPSTMMRP ENPQYTMTSL
DQKETEQYNE EDPIDPNEDE SFPGQSRWGD EEMNFKGNPT VRQYEGEHYA STLAKEYLPY
SLSNPPKPSE DFPYSEFYPW NPQETFPIYN PGPTIAPPVD PRSYYVNNAI GQEESTLFPS
WTSWDHRNQA ERQKESEPYF NRNVWDQSIN LHKSNIPNHP YSTTSPARFP KDPTWFEGEN
LNYDLQITSL SPPEREQLAF PDFLPQSYPT GQNEAHLFHQ SQRGSCCIGG STGHKDNVLA
LQDYTSSYGL PPRKNQETSP VHTESSYIKY ARPNVSPASI LPSQRNISEN KLTAESPNPS
PFGDGVPTVR KNTPYSGKNQ LETGIVAFSE ASSSQPKNTP CLKSDLGGDR RDVLKQFFEG
SQLSERTAGL TPEQLVIGIP DKGSGPDSIQ SEVQGKEGEM QQQRPPTIMK LPCFGSNSKF
HSSTTGPPIN NRRPTLLNGA LSTPTESPNT LVGLATREQL KSINVDKLNA DEHTTLESFQ
GTSPQDQGCL LLQA
