AMELX_MOUSE
ID AMELX_MOUSE Reviewed; 210 AA.
AC P63277; A2ALX2; A2ALX3; P45559; P70592; Q61293;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Amelogenin, X isoform;
DE AltName: Full=Leucine-rich amelogenin peptide;
DE Short=LRAP;
DE Flags: Precursor;
GN Name=Amelx; Synonyms=Amel;
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 (ISOFORMS 1; 2 AND 3).
RC STRAIN=ICR;
RX PubMed=1445358; DOI=10.1016/0006-291x(92)91366-x;
RA Lau E.C., Simmer J.P., Bringas P. Jr., Hsu D.D.J., Hu C.C.,
RA Zeichner-David M., Thiemann F., Snead M.L., Slavkin H.C., Fincham A.G.;
RT "Alternative splicing of the mouse amelogenin primary RNA transcript
RT contributes to amelogenin heterogeneity.";
RL Biochem. Biophys. Res. Commun. 188:1253-1260(1992).
RN [2]
RP SEQUENCE REVISION TO 4.
RA Oida S., Iimura T., Arai N., Takeda K., Maruoka Y., Terashima T.,
RA Shimokawa H., Sasaki S.;
RL Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 4).
RX PubMed=8988368; DOI=10.3109/10425179609020879;
RA Oida S., Miyazaki H., Iimura T., Suzuki M., Sasaki M., Shimokawa H.;
RT "Molecular structure of the mouse amelogenin genomic DNA.";
RL DNA Seq. 6:307-310(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Head;
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]
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]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 57-210.
RX PubMed=4015654; DOI=10.1016/0006-291x(85)91964-3;
RA Snead M.L., Lau E.C., Zeichner-David M., Fincham A.G., Woo S.L.,
RA Slavkin H.C.;
RT "DNA sequence for cloned cDNA for murine amelogenin reveal the amino acid
RT sequence for enamel-specific protein.";
RL Biochem. Biophys. Res. Commun. 129:812-818(1985).
RN [7]
RP INTERACTION WITH KRT5, AND DEVELOPMENTAL STAGE.
RX PubMed=12657653; DOI=10.1074/jbc.m211184200;
RA Ravindranath R.M., Basilrose R.M. Sr., Ravindranath N.H., Vaitheesvaran B.;
RT "Amelogenin interacts with cytokeratin-5 in ameloblasts during enamel
RT growth.";
RL J. Biol. Chem. 278:20293-20302(2003).
CC -!- FUNCTION: Plays a role in the biomineralization of teeth. Seems to
CC regulate the formation of crystallites during the secretory stage of
CC tooth enamel development. Thought to play a major role in the
CC structural organization and mineralization of developing enamel.
CC -!- SUBUNIT: Interacts with KRT5. {ECO:0000269|PubMed:12657653}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250|UniProtKB:Q99217}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=Additional isoforms seem to exist.;
CC Name=4;
CC IsoId=P63277-4; Sequence=Displayed;
CC Name=1;
CC IsoId=P63277-1, P45559-1;
CC Sequence=VSP_011688;
CC Name=2; Synonyms=LRAP;
CC IsoId=P63277-2, P45559-2;
CC Sequence=VSP_011688, VSP_000230;
CC Name=3;
CC IsoId=P63277-3, P45559-3;
CC Sequence=VSP_011688, VSP_000231;
CC -!- DEVELOPMENTAL STAGE: Expressed in ameloblasts at the periphery of
CC mandibular molars at P1 (PubMed:12657653). At P3 also expressed at the
CC molar incisal region (PubMed:12657653). Expressed at the terminal of
CC Tomes' processes of ameloblasts at the incisal region at P5
CC (PubMed:12657653). {ECO:0000269|PubMed:12657653}.
CC -!- PTM: Several forms are produced by C-terminal processing.
CC -!- PTM: Phosphorylated by FAM20C in vitro. {ECO:0000250|UniProtKB:Q99217}.
CC -!- SIMILARITY: Belongs to the amelogenin family. {ECO:0000305}.
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DR EMBL; D31768; BAA06546.1; -; mRNA.
DR EMBL; D31769; BAA06547.1; -; mRNA.
DR EMBL; D83067; BAA23665.1; -; Genomic_DNA.
DR EMBL; AK029358; BAC26415.1; -; mRNA.
DR EMBL; AL805974; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; M10095; AAA37218.1; -; mRNA.
DR CCDS; CCDS41214.1; -. [P63277-1]
DR CCDS; CCDS81197.1; -. [P63277-3]
DR PIR; I49486; I49486.
DR PIR; PC1148; PC1148.
DR RefSeq; NP_001075447.1; NM_001081978.2.
DR RefSeq; NP_001277300.1; NM_001290371.1. [P63277-3]
DR RefSeq; NP_033796.1; NM_009666.4. [P63277-1]
DR AlphaFoldDB; P63277; -.
DR DIP; DIP-59703N; -.
DR STRING; 10090.ENSMUSP00000065966; -.
DR iPTMnet; P63277; -.
DR PhosphoSitePlus; P63277; -.
DR PRIDE; P63277; -.
DR ProteomicsDB; 296104; -. [P63277-4]
DR Antibodypedia; 23742; 162 antibodies from 21 providers.
DR DNASU; 11704; -.
DR Ensembl; ENSMUST00000112118; ENSMUSP00000107746; ENSMUSG00000031354. [P63277-1]
DR Ensembl; ENSMUST00000112119; ENSMUSP00000107747; ENSMUSG00000031354. [P63277-4]
DR Ensembl; ENSMUST00000112120; ENSMUSP00000107748; ENSMUSG00000031354. [P63277-3]
DR GeneID; 11704; -.
DR KEGG; mmu:11704; -.
DR UCSC; uc009uxs.2; mouse. [P63277-1]
DR UCSC; uc009uxu.1; mouse. [P63277-4]
DR CTD; 265; -.
DR MGI; MGI:88005; Amelx.
DR VEuPathDB; HostDB:ENSMUSG00000031354; -.
DR eggNOG; ENOG502S4XP; Eukaryota.
DR GeneTree; ENSGT00390000009151; -.
DR HOGENOM; CLU_120753_0_0_1; -.
DR InParanoid; P63277; -.
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; 11704; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Amelx; mouse.
DR PRO; PR:P63277; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; P63277; protein.
DR Bgee; ENSMUSG00000031354; Expressed in molar tooth and 26 other tissues.
DR ExpressionAtlas; P63277; baseline and differential.
DR Genevisible; P63277; MM.
DR GO; GO:0005604; C:basement membrane; IDA:MGI.
DR GO; GO:0009986; C:cell surface; IMP:BHF-UCL.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0030139; C:endocytic vesicle; ISO:MGI.
DR GO; GO:0031012; C:extracellular matrix; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; IDA:CAFA.
DR GO; GO:0099080; C:supramolecular complex; IDA:CAFA.
DR GO; GO:0005509; F:calcium ion binding; IDA:CAFA.
DR GO; GO:0008083; F:growth factor activity; IMP:BHF-UCL.
DR GO; GO:0046848; F:hydroxyapatite binding; IDA:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; IDA:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:CAFA.
DR GO; GO:0031402; F:sodium ion binding; IDA:CAFA.
DR GO; GO:0030345; F:structural constituent of tooth enamel; ISO:MGI.
DR GO; GO:0097186; P:amelogenesis; IDA:ARUK-UCL.
DR GO; GO:0007155; P:cell adhesion; IMP:BHF-UCL.
DR GO; GO:0070166; P:enamel mineralization; IDA:ARUK-UCL.
DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEP:BHF-UCL.
DR GO; GO:0042127; P:regulation of cell population proliferation; IMP:BHF-UCL.
DR GO; GO:0007165; P:signal transduction; TAS:BHF-UCL.
DR GO; GO:0034505; P:tooth mineralization; IMP:BHF-UCL.
DR InterPro; IPR004116; Amelogenin.
DR PANTHER; PTHR46794; PTHR46794; 1.
DR PRINTS; PR01757; AMELOGENIN.
DR SMART; SM00818; Amelogenin; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Biomineralization; Extracellular matrix;
KW Phosphoprotein; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000250"
FT CHAIN 17..210
FT /note="Amelogenin, X isoform"
FT /id="PRO_0000001201"
FT REGION 109..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..185
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02817"
FT VAR_SEQ 35..48
FT /note="Missing (in isoform 1, isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_011688"
FT VAR_SEQ 64..184
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_000230"
FT VAR_SEQ 64..87
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_000231"
FT CONFLICT 111
FT /note="P -> A (in Ref. 6; AAA37218)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 210 AA; 23483 MW; EB6ED5D09AA83AFA CRC64;
MGTWILFACL LGAAFAMPLP PHPGSPGYIN LSYEKSHSQA INTDRTALVL TPLKWYQSMI
RQPYPSYGYE PMGGWLHHQI IPVLSQQHPP SHTLQPHHHL PVVPAQQPVA PQQPMMPVPG
HHSMTPTQHH QPNIPPSAQQ PFQQPFQPQA IPPQSHQPMQ PQSPLHPMQP LAPQPPLPPL
FSMQPLSPIL PELPLEAWPA TDKTKREEVD
