ID   AMBN_BOVIN              Reviewed;         392 AA.
AC   Q9XSX7;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   10-OCT-2002, sequence version 2.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=Ameloblastin;
DE   Flags: Precursor;
GN   Name=AMBN;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Tooth enamel;
RA   Machule D., Li W., DenBesten P.;
RT   "Bovine enamel ameloblastin sequence.";
RL   Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the mineralization and structural organization of
CC       enamel. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ameloblastin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD39833.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF157019; AAD39833.2; ALT_INIT; mRNA.
DR   RefSeq; NP_776413.1; NM_173988.2.
DR   AlphaFoldDB; Q9XSX7; -.
DR   STRING; 9913.ENSBTAP00000052338; -.
DR   PaxDb; Q9XSX7; -.
DR   PRIDE; Q9XSX7; -.
DR   GeneID; 280995; -.
DR   KEGG; bta:280995; -.
DR   CTD; 258; -.
DR   eggNOG; ENOG502QWCP; Eukaryota.
DR   HOGENOM; CLU_051782_0_0_1; -.
DR   InParanoid; Q9XSX7; -.
DR   OrthoDB; 1189806at2759; -.
DR   TreeFam; TF337860; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0008083; F:growth factor activity; IBA:GO_Central.
DR   GO; GO:0030345; F:structural constituent of tooth enamel; IEA:InterPro.
DR   GO; GO:0031214; P:biomineral tissue development; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR   GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEA:InterPro.
DR   InterPro; IPR007798; Amelin.
DR   PANTHER; PTHR14115; PTHR14115; 1.
DR   Pfam; PF05111; Amelin; 1.
DR   SMART; SM00817; Amelin; 1.
PE   2: Evidence at transcript level;
KW   Biomineralization; Extracellular matrix; Hydroxylation; Phosphoprotein;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..392
FT                   /note="Ameloblastin"
FT                   /id="PRO_0000001191"
FT   REGION          86..109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          247..280
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          349..392
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        95..109
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        349..377
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         37
FT                   /note="Hydroxyproline"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         43
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q28989"
SQ   SEQUENCE   392 AA;  42239 MW;  E81225479D6F598E CRC64;
     MPALKIPLFK MKDMILILCL LKMSSAVPAF PQQPGIPGMA SLSLETMRQL GSLQGLNLLS
     QYSRFGFGKS FNSLWMNGLL PPHSSFPWMR PREHETQQPS LQPQQPGQKP FLQPTVVTSM
     QNAVQKGVPQ PPIYQGHPPL QQAEGPMVEQ QVAPSEKPPT TELPGMDFAD LQDPPMFPIA
     HLISRGPMPQ NKPSQLYPGI FYVTYGANQL GGRGDPLAYG AIFPGFGGMR PRLGGMPHNP
     DMGGDFTLEF DSPVAATKGP EKGEGGAQDS PVPEAHLADP ESPALLSELA PGALEGLLAN
     PEGNIPNLAR GPAGRSRGFL RGVTPAAADP LMTPGLAEVY ETYGADETTT LGLQEETTVD
     STATPDTQHT LMPRNKAQQP QIKHDAWHFQ EP