ID   AMELY_PANTR             Reviewed;         203 AA.
AC   Q861X8;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Amelogenin, Y isoform;
DE   Flags: Precursor; Fragment;
GN   Name=AMELY;
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=12672962; DOI=10.1073/pnas.0635848100;
RA   Iwase M., Satta Y., Hirai Y., Hirai H., Imai H., Takahata N.;
RT   "The amelogenin loci span an ancient pseudoautosomal boundary in diverse
RT   mammalian species.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:5258-5263(2003).
CC   -!- FUNCTION: Plays a role in biomineralization. Seems to regulate the
CC       formation of crystallites during the secretory stage of tooth enamel
CC       development. Thought to play a major role in the structural
CC       organization and mineralization of developing enamel (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the amelogenin family. {ECO:0000305}.
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DR   EMBL; AB091782; BAC66102.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q861X8; -.
DR   STRING; 9598.ENSPTRP00000038754; -.
DR   PRIDE; Q861X8; -.
DR   eggNOG; ENOG502S4XP; Eukaryota.
DR   InParanoid; Q861X8; -.
DR   Proteomes; UP000002277; 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; Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000250"
FT   CHAIN           17..203
FT                   /note="Amelogenin, Y isoform"
FT                   /id="PRO_0000045794"
FT   REGION          116..180
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        116..136
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        137..180
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         203
SQ   SEQUENCE   203 AA;  22897 MW;  F829F8C4C68E4A4D CRC64;
     MGTWILFACL VGAAFAMPLP PHPGHPGYIN FSYENSHSQA INVDRIALVL TPLKWYQSMI
     RPPYSSYGYE PMGGWLHHQI IPVVSQQHPL THTLQSHHHI PVVPAQQPRV PQQAMMPVPG
     QQSMTPTQHH QPNLPLPAQQ PFQPQPVQPL PHQPMQPQPP VQPMQPLLPQ PPLPPMFPMR
     PLPPILPDLH LEAWPATDKT KRE