ID   AMEL_CAVPO              Reviewed;         226 AA.
AC   Q9Z0K9;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Amelogenin;
DE   Flags: Precursor;
GN   Name=AMEL;
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Cerny R.;
RT   "Cloning, cDNA sequence, and splicing variants of guinea-pig amelogenin
RT   mRNA.";
RL   Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
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 {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the amelogenin family. {ECO:0000305}.
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DR   EMBL; AJ012200; CAA09957.1; -; mRNA.
DR   RefSeq; NP_001166340.1; NM_001172869.1.
DR   AlphaFoldDB; Q9Z0K9; -.
DR   STRING; 10141.ENSCPOP00000016676; -.
DR   PRIDE; Q9Z0K9; -.
DR   GeneID; 100379562; -.
DR   KEGG; cpoc:100379562; -.
DR   CTD; 265; -.
DR   eggNOG; ENOG502S4XP; Eukaryota.
DR   InParanoid; Q9Z0K9; -.
DR   OrthoDB; 1509730at2759; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
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; 2.
DR   PRINTS; PR01757; AMELOGENIN.
DR   SMART; SM00818; Amelogenin; 1.
PE   2: Evidence at transcript level;
KW   Biomineralization; Extracellular matrix; Phosphoprotein;
KW   Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..226
FT                   /note="Amelogenin"
FT                   /id="PRO_0000001198"
FT   REGION          86..196
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        139..155
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        164..195
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         32
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P45561"
SQ   SEQUENCE   226 AA;  25379 MW;  89215B9F1D8AA535 CRC64;
     MGTWILFACL LGTAFAMPLP PHPGHPGYIN FSYEKSHSNA INIDRTALVL TPLKWYQSMI
     RQPYPSYGYE SMGGWVHHQV IPVLSQQHPP SHTTLPPHHH IPVGPAQQPV VPQQPLMPVP
     GHHSMTPNQH HQPNLPPTSQ QPFQQPFPTQ PVQPQHHQPI QPIQPIQPIQ PIQPIQPQSP
     LHPIQPLPPQ QALPPMFSMQ PIAPLLPDLP LEAWPATDKT KREEVD