AMELX_BOVIN
ID AMELX_BOVIN Reviewed; 213 AA.
AC P02817;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Amelogenin, X isoform;
DE AltName: Full=Class I amelogenin;
DE Flags: Precursor;
GN Name=AMELX;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RX PubMed=1989679; DOI=10.1021/bi00218a028;
RA Gibson C., Golub E., Herold R., Risser M., Ding W., Shimokawa H., Young M.,
RA Termine J., Rosenbloom J.;
RT "Structure and expression of the bovine amelogenin gene.";
RL Biochemistry 30:1075-1079(1991).
RN [2]
RP PRELIMINARY PROTEIN SEQUENCE OF 17-201.
RX PubMed=6732825; DOI=10.1016/0006-291x(84)90223-7;
RA Takagi T., Suzuki M., Baba T., Minegishi K., Sasaki S.;
RT "Complete amino acid sequence of amelogenin in developing bovine enamel.";
RL Biochem. Biophys. Res. Commun. 121:592-597(1984).
RN [3]
RP ALTERNATIVE SPLICING (ISOFORM 2).
RC TISSUE=Tooth;
RX PubMed=1996994; DOI=10.1016/0006-291x(91)91564-s;
RA Gibson C.W., Golub E., Ding W., Shimokawa H., Young M., Termine J.,
RA Rosenbloom J.;
RT "Identification of the leucine-rich amelogenin peptide (LRAP) as the
RT translation product of an alternatively spliced transcript.";
RL Biochem. Biophys. Res. Commun. 174:1306-1312(1991).
RN [4]
RP PROTEIN SEQUENCE OF 17-49 AND 188-213, AND PHOSPHORYLATION AT SER-32.
RX PubMed=8250931; DOI=10.1006/bbrc.1993.2468;
RA Fincham A.G., Moradian-Oldak J.;
RT "Amelogenin post-translational modifications: carboxy-terminal processing
RT and the phosphorylation of bovine and porcine 'TRAP' and 'LRAP'
RT amelogenins.";
RL Biochem. Biophys. Res. Commun. 197:248-255(1993).
RN [5]
RP STRUCTURE BY NMR.
RX PubMed=2598664;
RA Renugopalakrishnan V., Prabhakaran M., Huang S.G., Balasubramaniam A.,
RA Strawich E., Glimcher M.J.;
RT "Secondary structure and limited three-dimensional structure of bovine
RT amelogenin.";
RL Connect. Tissue Res. 22:131-138(1989).
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=2;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=P02817-1; Sequence=Displayed;
CC Name=2; Synonyms=LRAP;
CC IsoId=P02817-2; Sequence=VSP_000227;
CC -!- DEVELOPMENTAL STAGE: Transiently but abundantly expressed by
CC ameloblasts during tooth development. Amelogenin is the predominant
CC protein in developing dental enamel. {ECO:0000269|PubMed:1989679}.
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; M63499; AAA30372.1; -; mRNA.
DR EMBL; M63631; AAA30625.1; -; mRNA.
DR PIR; A37998; JMBO.
DR RefSeq; NP_001014984.1; NM_001014984.1. [P02817-1]
DR RefSeq; XP_015317278.1; XM_015461792.1.
DR AlphaFoldDB; P02817; -.
DR STRING; 9913.ENSBTAP00000016034; -.
DR iPTMnet; P02817; -.
DR PaxDb; P02817; -.
DR PRIDE; P02817; -.
DR Ensembl; ENSBTAT00000016034; ENSBTAP00000016034; ENSBTAG00000012089. [P02817-1]
DR GeneID; 281620; -.
DR KEGG; bta:281620; -.
DR CTD; 265; -.
DR VEuPathDB; HostDB:ENSBTAG00000012089; -.
DR eggNOG; ENOG502S4XP; Eukaryota.
DR GeneTree; ENSGT00390000009151; -.
DR InParanoid; P02817; -.
DR OMA; IPIMAAQ; -.
DR OrthoDB; 1509730at2759; -.
DR TreeFam; TF337092; -.
DR Reactome; R-BTA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-BTA-8957275; Post-translational protein phosphorylation.
DR Proteomes; UP000009136; Unplaced.
DR Bgee; ENSBTAG00000012089; Expressed in Ammon's horn and 11 other tissues.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0030345; F:structural constituent of tooth enamel; IBA:GO_Central.
DR GO; GO:0002062; P:chondrocyte differentiation; IDA:BHF-UCL.
DR GO; GO:0070166; P:enamel mineralization; IBA:GO_Central.
DR GO; GO:0001837; P:epithelial to mesenchymal transition; IDA:BHF-UCL.
DR GO; GO:0001649; P:osteoblast differentiation; IDA:BHF-UCL.
DR GO; GO:0032967; P:positive regulation of collagen biosynthetic process; IDA:BHF-UCL.
DR InterPro; IPR004116; Amelogenin.
DR PANTHER; PTHR46794; PTHR46794; 2.
DR PRINTS; PR01757; AMELOGENIN.
DR SMART; SM00818; Amelogenin; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Biomineralization; Direct protein sequencing;
KW Extracellular matrix; Phosphoprotein; Reference proteome; Repeat; Secreted;
KW Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000269|PubMed:8250931"
FT CHAIN 17..213
FT /note="Amelogenin, X isoform"
FT /id="PRO_0000001196"
FT REGION 96..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..197
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8250931"
FT VAR_SEQ 50..187
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_000227"
SQ SEQUENCE 213 AA; 24119 MW; 163BD538806366DF CRC64;
MGTWILFACL LGAAFSMPLP PHPGHPGYIN FSYEVLTPLK WYQSMIRHPY PSYGYEPMGG
WLHHQIIPVV SQQTPQNHAL QPHHHIPMVP AQQPVVPQQP MMPVPGQHSM TPTQHHQPNL
PLPAQQPFQP QSIQPQPHQP LQPHQPLQPM QPMQPLQPLQ PLQPQPPVHP IQPLPPQPPL
PPIFPMQPLP PMLPDLPLEA WPATDKTKRE EVD
