ID   AMEL_MONDO              Reviewed;         202 AA.
AC   Q28462;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Amelogenin;
GN   Name=AMEL;
OS   Monodelphis domestica (Gray short-tailed opossum).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Metatheria; Didelphimorphia; Didelphidae; Monodelphis.
OX   NCBI_TaxID=13616;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-42, AND ALTERNATIVE
RP   SPLICING.
RX   PubMed=8955666; DOI=10.1177/00220345960750100401;
RA   Hu C.C., Zhang C., Qian Q., Ryu O.H., Moradian-Oldak J., Fincham A.G.,
RA   Simmer J.P.;
RT   "Cloning, DNA sequence, and alternative splicing of opossum amelogenin
RT   mRNAs.";
RL   J. Dent. Res. 75:1728-1734(1996).
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=1;
CC         Comment=A number of isoforms are produced.;
CC       Name=1;
CC         IsoId=Q28462-1; Sequence=Displayed;
CC   -!- SIMILARITY: Belongs to the amelogenin family. {ECO:0000305}.
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DR   EMBL; U43407; AAB41109.1; -; mRNA.
DR   AlphaFoldDB; Q28462; -.
DR   STRING; 13616.ENSMODP00000021676; -.
DR   eggNOG; ENOG502S4XP; Eukaryota.
DR   InParanoid; Q28462; -.
DR   Proteomes; UP000002280; 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; 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.
FT   CHAIN           1..202
FT                   /note="Amelogenin"
FT                   /id="PRO_0000144062"
FT   REGION          77..202
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        77..91
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        107..180
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         16
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P45561"
FT   CONFLICT        32..33
FT                   /note="HE -> QQ (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   202 AA;  22996 MW;  277FD2935211A6C6 CRC64;
     IPLPPHPGHP GYINFSYEVL TPLKWYQSMM RHEYPSYGYE PMGGWLHHQI IPVLSQQHSP
     SHSLPPQHHI PIMAAQQPAP PQQPVMPVPG QHPMAPTQHH QPNLPQPGQQ PYQPQPAQQP
     QPHQPIQPIQ PIQPIQPMQP MQPMQPMQPM QPMQPQTPVH AVRPLPPQPP LPPMFPMQPM
     SPMLPDMEAW PATDKTKREE VD