AMELX_RAT
ID AMELX_RAT Reviewed; 210 AA.
AC P63278; P45559; Q62945; Q63640; Q78E56;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Amelogenin, X isoform;
DE AltName: Full=Leucine-rich amelogenin peptide;
DE Short=LRAP;
DE Flags: Precursor;
GN Name=Amelx; Synonyms=Amel, Amgx;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Enamel organ;
RX PubMed=8297387; DOI=10.1006/bbrc.1994.1109;
RA Bonass W.A., Robinson P.A., Kirkham J., Shore R.C., Robinson C.;
RT "Molecular cloning and DNA sequence of rat amelogenin and a comparative
RT analysis of mammalian amelogenin protein sequence divergence.";
RL Biochem. Biophys. Res. Commun. 198:755-763(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=Wistar; TISSUE=Enamel organ;
RX PubMed=7948026; DOI=10.1016/0167-4781(94)90228-3;
RA Bonass W.A., Kirkham J., Brookes S.J., Shore R.C., Robinson C.;
RT "Isolation and characterisation of an alternatively-spliced rat amelogenin
RT cDNA: LRAP -- a highly conserved, functional alternatively-spliced
RT amelogenin?";
RL Biochim. Biophys. Acta 1219:690-692(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
RA Bonass W.A.;
RT "Rat amelogenin cDNA containing exon 4.";
RL Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 5 AND 6).
RC TISSUE=Tooth enamel;
RX PubMed=8600184; DOI=10.1177/00220345950740121101;
RA Li R., Li W., DenBesten P.K.;
RT "Alternative splicing of amelogenin mRNA from rat incisor ameloblasts.";
RL J. Dent. Res. 74:1880-1885(1995).
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:0000250|UniProtKB:P63277}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250|UniProtKB:Q99217}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Comment=Additional isoforms seem to exist.;
CC Name=4;
CC IsoId=P63278-4; Sequence=Displayed;
CC Name=1;
CC IsoId=P63278-1, P45559-1;
CC Sequence=VSP_011689;
CC Name=2; Synonyms=LRAP;
CC IsoId=P63278-2, P45559-2;
CC Sequence=VSP_011689, VSP_011690;
CC Name=3;
CC IsoId=P63278-3, P45559-3;
CC Sequence=VSP_011689, VSP_011691;
CC Name=5;
CC IsoId=P63278-5; Sequence=VSP_011689, VSP_011692;
CC Name=6;
CC IsoId=P63278-6; Sequence=VSP_011689, VSP_011691, VSP_011692;
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; U01245; AAA20491.1; -; mRNA.
DR EMBL; U07054; AAA61964.1; -; mRNA.
DR EMBL; U67130; AAB06753.1; -; mRNA.
DR EMBL; U51195; AAB02691.1; -; mRNA.
DR EMBL; U60562; AAB03481.1; -; mRNA.
DR PIR; JC2391; JC2391.
DR RefSeq; NP_001258002.1; NM_001271073.1. [P63278-6]
DR RefSeq; NP_001258003.1; NM_001271074.1. [P63278-5]
DR RefSeq; NP_001258004.1; NM_001271075.1.
DR RefSeq; NP_001258005.1; NM_001271076.1.
DR RefSeq; NP_001258006.1; NM_001271077.1. [P63278-1]
DR RefSeq; NP_001258007.1; NM_001271078.1. [P63278-2]
DR RefSeq; NP_062027.1; NM_019154.1. [P63278-4]
DR AlphaFoldDB; P63278; -.
DR IntAct; P63278; 65.
DR STRING; 10116.ENSRNOP00000048382; -.
DR PhosphoSitePlus; P63278; -.
DR PRIDE; P63278; -.
DR Ensembl; ENSRNOT00000052176; ENSRNOP00000048382; ENSRNOG00000003965. [P63278-5]
DR Ensembl; ENSRNOT00000078843; ENSRNOP00000069787; ENSRNOG00000003965. [P63278-4]
DR GeneID; 29160; -.
DR KEGG; rno:29160; -.
DR CTD; 265; -.
DR RGD; 2107; Amelx.
DR eggNOG; ENOG502S4XP; Eukaryota.
DR GeneTree; ENSGT00390000009151; -.
DR InParanoid; P63278; -.
DR OMA; IPIMAAQ; -.
DR OrthoDB; 1509730at2759; -.
DR PhylomeDB; P63278; -.
DR TreeFam; TF337092; -.
DR Reactome; R-RNO-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-RNO-8957275; Post-translational protein phosphorylation.
DR PRO; PR:P63278; -.
DR Proteomes; UP000002494; Chromosome X.
DR Bgee; ENSRNOG00000003965; Expressed in skeletal muscle tissue and 2 other tissues.
DR ExpressionAtlas; P63278; baseline and differential.
DR Genevisible; P63278; RN.
DR GO; GO:0005604; C:basement membrane; ISO:RGD.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0030139; C:endocytic vesicle; IDA:RGD.
DR GO; GO:0031012; C:extracellular matrix; IDA:RGD.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0099080; C:supramolecular complex; ISO:RGD.
DR GO; GO:0005509; F:calcium ion binding; ISO:RGD.
DR GO; GO:0008083; F:growth factor activity; ISO:RGD.
DR GO; GO:0046848; F:hydroxyapatite binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; IDA:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0031402; F:sodium ion binding; ISO:RGD.
DR GO; GO:0030345; F:structural constituent of tooth enamel; IDA:RGD.
DR GO; GO:0097186; P:amelogenesis; ISO:RGD.
DR GO; GO:0007155; P:cell adhesion; ISO:RGD.
DR GO; GO:0070166; P:enamel mineralization; ISO:RGD.
DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; ISO:RGD.
DR GO; GO:0042127; P:regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0051592; P:response to calcium ion; IEP:RGD.
DR GO; GO:0007584; P:response to nutrient; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0034505; P:tooth mineralization; ISO:RGD.
DR InterPro; IPR004116; Amelogenin.
DR PANTHER; PTHR46794; PTHR46794; 1.
DR PRINTS; PR01757; AMELOGENIN.
DR SMART; SM00818; Amelogenin; 1.
PE 2: Evidence at transcript 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_0000001202"
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, isoform 3, isoform
FT 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:7948026,
FT ECO:0000303|PubMed:8600184"
FT /id="VSP_011689"
FT VAR_SEQ 64..184
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_011690"
FT VAR_SEQ 64..87
FT /note="Missing (in isoform 3 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:8600184"
FT /id="VSP_011691"
FT VAR_SEQ 210
FT /note="D -> AFSPMKWYQGTARHPLNMETTTEK (in isoform 5 and
FT isoform 6)"
FT /evidence="ECO:0000303|PubMed:8600184"
FT /id="VSP_011692"
FT CONFLICT 64
FT /note="Y -> H (in Ref. 4; AAB02691)"
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
