ID   AMEL_ORNAN              Reviewed;         121 AA.
AC   O97646;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Amelogenin;
DE   Flags: Fragment;
GN   Name=AMEL;
OS   Ornithorhynchus anatinus (Duckbill platypus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Monotremata; Ornithorhynchidae; Ornithorhynchus.
OX   NCBI_TaxID=9258;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9789040; DOI=10.1073/pnas.95.22.13056;
RA   Toyosawa S., O'Huigin C., Figueroa F., Tichy H., Klein J.;
RT   "Identification and characterization of amelogenin genes in monotremes,
RT   reptiles, and amphibians.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:13056-13061(1998).
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 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix.
CC   -!- SIMILARITY: Belongs to the amelogenin family. {ECO:0000305}.
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DR   EMBL; AF095566; AAC78131.1; -; Genomic_DNA.
DR   AlphaFoldDB; O97646; -.
DR   STRING; 9258.ENSOANP00000004174; -.
DR   eggNOG; ENOG502S4XP; Eukaryota.
DR   InParanoid; O97646; -.
DR   Proteomes; UP000002279; Unplaced.
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:0070166; P:enamel mineralization; IBA:GO_Central.
DR   InterPro; IPR004116; Amelogenin.
DR   PANTHER; PTHR46794; PTHR46794; 1.
DR   PRINTS; PR01757; AMELOGENIN.
DR   SMART; SM00818; Amelogenin; 1.
PE   3: Inferred from homology;
KW   Biomineralization; Extracellular matrix; Reference proteome; Repeat;
KW   Secreted.
FT   CHAIN           <1..>121
FT                   /note="Amelogenin"
FT                   /id="PRO_0000144063"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          32..121
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        47..64
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        65..114
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT   NON_TER         121
SQ   SEQUENCE   121 AA;  13539 MW;  23A46094B2C4326F CRC64;
     LHHQIIPVLS QQQTPTHALQ PHHHIPVMAA QQPMQPQQPM MPMPGQPSVT PTQHHQSNLP
     QPAQQPFQPQ VPQQPPHQPI QPQAPAHPMP PMPQPPLPPM FPMQPLPPLL PDLPLEQWPA
     T