ID   STAT_MACFA              Reviewed;          61 AA.
AC   P02809;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 2.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Statherin;
DE   Flags: Precursor;
GN   Name=STATH;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   PARTIAL PROTEIN SEQUENCE OF 1-19.
RX   PubMed=3476566; DOI=10.1177/00220345870660021301;
RA   Oppenheim F.G., Hay D.I., Smith D.J., Offner G.D., Troxler R.F.;
RT   "Molecular basis of salivary proline-rich protein and peptide synthesis:
RT   cell-free translations and processing of human and macaque statherin mRNAs
RT   and partial amino acid sequence of their signal peptides.";
RL   J. Dent. Res. 66:462-466(1987).
RN   [2]
RP   PROTEIN SEQUENCE OF 20-61, AND PHOSPHORYLATION AT SER-21 AND SER-22.
RX   PubMed=7107568; DOI=10.1016/s0021-9258(18)34064-x;
RA   Oppenheim F.G., Offner G.D., Troxler R.F.;
RT   "Phosphoproteins in the parotid saliva from the subhuman primate Macaca
RT   fascicularis. Isolation and characterization of a proline-rich
RT   phosphoglycoprotein and the complete covalent structure of a proline-rich
RT   phosphopeptide.";
RL   J. Biol. Chem. 257:9271-9282(1982).
CC   -!- FUNCTION: Salivary protein that stabilizes saliva supersaturated with
CC       calcium salts by inhibiting the precipitation of calcium phosphate
CC       salts. It also modulates hydroxyapatite crystal formation on the tooth
CC       surface.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Secreted by parotid and submandibular glands.
CC   -!- SIMILARITY: Belongs to the histatin/statherin family. {ECO:0000305}.
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DR   PIR; B32524; SBMQPI.
DR   iPTMnet; P02809; -.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046848; F:hydroxyapatite binding; IEA:InterPro.
DR   GO; GO:0031214; P:biomineral tissue development; IEA:UniProtKB-KW.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:InterPro.
DR   GO; GO:0030500; P:regulation of bone mineralization; IEA:InterPro.
DR   InterPro; IPR030773; Histatin/statherin.
DR   InterPro; IPR005575; Statherin.
DR   PANTHER; PTHR15057; PTHR15057; 1.
DR   Pfam; PF03875; Statherin; 1.
DR   PIRSF; PIRSF002565; Statherin; 1.
PE   1: Evidence at protein level;
KW   Biomineralization; Direct protein sequencing; Phosphoprotein;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000269|PubMed:3476566,
FT                   ECO:0000269|PubMed:7107568"
FT   CHAIN           20..61
FT                   /note="Statherin"
FT                   /id="PRO_0000022423"
FT   REGION          20..25
FT                   /note="Hydroxyapatite-binding; inhibits crystal growth"
FT   REGION          36..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          37..61
FT                   /note="Hydrophobic; inhibits precipitation of calcium
FT                   phosphate salts"
FT   COMPBIAS        44..61
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         21
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:7107568"
FT   MOD_RES         22
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:7107568"
SQ   SEQUENCE   61 AA;  7464 MW;  64241AA8B5641A5B CRC64;
     MXFLXFXLXL LXMXXMXXXD SSEEKFLRRL RRFDEGRYGP YQPFAPQPLY PQPYQPYQPQ
     Y