AMEL_PIG
ID AMEL_PIG Reviewed; 189 AA.
AC P45561;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Amelogenin;
DE AltName: Full=Amelogenin 173A/173B;
DE AltName: Full=Leucine-rich amelogenin peptide;
DE Short=LRAP;
DE Flags: Precursor;
GN Name=AMEL;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
RX PubMed=8955667; DOI=10.1177/00220345960750100501;
RA Hu C.C., Bartlett J.D., Zhang C.H., Qian Q., Ryu O.H., Simmer J.P.;
RT "Cloning, cDNA sequence, and alternative splicing of porcine amelogenin
RT mRNAs.";
RL J. Dent. Res. 75:1735-1741(1996).
RN [2]
RP PROTEIN SEQUENCE OF 17-61 AND 78-181, AND PHOSPHORYLATION AT SER-32.
RC TISSUE=Tooth;
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).
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 -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=P45561-1; Sequence=Displayed;
CC Name=2; Synonyms=LRAP;
CC IsoId=P45561-2; Sequence=VSP_000232;
CC Name=3; Synonyms=173B;
CC IsoId=P45561-3; Sequence=VSP_000233, VSP_000234;
CC -!- PTM: A number of other isoforms are produced by carboxy-terminal
CC processing.
CC -!- SIMILARITY: Belongs to the amelogenin family. {ECO:0000305}.
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DR EMBL; U43405; AAB41110.1; -; mRNA.
DR EMBL; U43406; AAB41111.1; -; mRNA.
DR RefSeq; NP_998965.1; NM_213800.1. [P45561-3]
DR RefSeq; NP_999071.1; NM_213906.1. [P45561-1]
DR AlphaFoldDB; P45561; -.
DR BMRB; P45561; -.
DR IntAct; P45561; 21.
DR STRING; 9823.ENSSSCP00000028659; -.
DR iPTMnet; P45561; -.
DR Ensembl; ENSSSCT00000013248; ENSSSCP00000012892; ENSSSCG00000012113. [P45561-1]
DR Ensembl; ENSSSCT00000040759; ENSSSCP00000037686; ENSSSCG00000031650. [P45561-3]
DR Ensembl; ENSSSCT00000076493; ENSSSCP00000072463; ENSSSCG00000031650. [P45561-3]
DR Ensembl; ENSSSCT00000091599; ENSSSCP00000064011; ENSSSCG00000012113. [P45561-1]
DR Ensembl; ENSSSCT00005008732; ENSSSCP00005005153; ENSSSCG00005005773. [P45561-3]
DR Ensembl; ENSSSCT00005008777; ENSSSCP00005005186; ENSSSCG00005005773. [P45561-3]
DR Ensembl; ENSSSCT00005070773; ENSSSCP00005044117; ENSSSCG00005043866. [P45561-1]
DR Ensembl; ENSSSCT00015051861; ENSSSCP00015020692; ENSSSCG00015037935. [P45561-1]
DR Ensembl; ENSSSCT00025004405; ENSSSCP00025001706; ENSSSCG00025003235. [P45561-1]
DR Ensembl; ENSSSCT00030098983; ENSSSCP00030045540; ENSSSCG00030070615. [P45561-1]
DR Ensembl; ENSSSCT00035025593; ENSSSCP00035009689; ENSSSCG00035019689. [P45561-1]
DR Ensembl; ENSSSCT00040017028; ENSSSCP00040006909; ENSSSCG00040012574. [P45561-1]
DR Ensembl; ENSSSCT00045029521; ENSSSCP00045020459; ENSSSCG00045017068. [P45561-1]
DR Ensembl; ENSSSCT00050102228; ENSSSCP00050044522; ENSSSCG00050074658. [P45561-1]
DR Ensembl; ENSSSCT00055057320; ENSSSCP00055045857; ENSSSCG00055028770. [P45561-1]
DR Ensembl; ENSSSCT00060061866; ENSSSCP00060026495; ENSSSCG00060045551. [P45561-1]
DR Ensembl; ENSSSCT00065062483; ENSSSCP00065027083; ENSSSCG00065045633. [P45561-1]
DR Ensembl; ENSSSCT00070036740; ENSSSCP00070030713; ENSSSCG00070018617. [P45561-1]
DR GeneID; 396714; -.
DR GeneID; 396940; -.
DR KEGG; ssc:396714; -.
DR KEGG; ssc:396940; -.
DR CTD; 265; -.
DR CTD; 266; -.
DR eggNOG; ENOG502S4XP; Eukaryota.
DR GeneTree; ENSGT00390000009151; -.
DR GeneTree; ENSGT01040000241139; -.
DR HOGENOM; CLU_120753_0_0_1; -.
DR InParanoid; P45561; -.
DR OMA; IPIMAAQ; -.
DR OrthoDB; 1509730at2759; -.
DR Reactome; R-SSC-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-SSC-8957275; Post-translational protein phosphorylation.
DR Proteomes; UP000008227; Chromosome Y.
DR Proteomes; UP000314985; Unassembled WGS sequence.
DR Bgee; ENSSSCG00000012113; Expressed in stomach and 25 other tissues.
DR ExpressionAtlas; P45561; baseline and differential.
DR Genevisible; P45561; SS.
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:0099080; C:supramolecular complex; IMP:CAFA.
DR GO; GO:0005509; F:calcium ion binding; IMP:CAFA.
DR GO; GO:0042802; F:identical protein binding; IPI:BHF-UCL.
DR GO; GO:0030345; F:structural constituent of tooth enamel; IBA:GO_Central.
DR GO; GO:0070166; P:enamel mineralization; IMP:CAFA.
DR DisProt; DP00693; -.
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; 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..189
FT /note="Amelogenin"
FT /id="PRO_0000001203"
FT REGION 87..167
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..164
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 6
FT /note="L -> F (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_000233"
FT VAR_SEQ 14..16
FT /note="AFS -> SLA (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_000234"
FT VAR_SEQ 34..45
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_000232"
SQ SEQUENCE 189 AA; 21387 MW; 6392212E0A31D00C CRC64;
MGTWILFACL LGAAFSMPLP PHPGHPGYIN FSYEVLTPLK WYQNMIRHPY TSYGYEPMGG
WLHHQIIPVV SQQTPQSHAL QPHHHIPMVP AQQPGIPQQP MMPLPGQHSM TPTQHHQPNL
PLPAQQPFQP QPVQPQPHQP LQPQSPMHPI QPLLPQPPLP PMFSMQSLLP DLPLEAWPAT
DKTKREEVD
