ID   AMEL_TACAC              Reviewed;         121 AA.
AC   O97647;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 55.
DE   RecName: Full=Amelogenin;
DE   Flags: Fragment;
GN   Name=AMEL;
OS   Tachyglossus aculeatus aculeatus (Southeast Australian short-beaked
OS   echidna).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Monotremata; Tachyglossidae; Tachyglossus.
OX   NCBI_TaxID=49271;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF095567; AAC78132.1; -; Genomic_DNA.
DR   AlphaFoldDB; O97647; -.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:InterPro.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0031214; P:biomineral tissue development; IEA:UniProtKB-KW.
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; Repeat; Secreted.
FT   CHAIN           <1..>121
FT                   /note="Amelogenin"
FT                   /id="PRO_0000144065"
FT   REGION          1..121
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..31
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        45..64
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        65..121
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT   NON_TER         121
SQ   SEQUENCE   121 AA;  13609 MW;  A796D2F278D9C136 CRC64;
     LHHQIIPVLS QHQTPTHALQ SHHHIPVMAT QQPTQPPQPM MPMPGQHSVT PTQHHQSNLP
     QPGQQPFQPQ FPQKPTHRPI QPQAPVHPMP PMPQPQLPPM FPLQPLPPLL PDLPLEPWPA
     S