ID   AMBN_PIG                Reviewed;         421 AA.
AC   Q28989;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Ameloblastin;
DE   AltName: Full=Sheathlin;
DE   Flags: Precursor;
GN   Name=AMBN;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND PARTIAL PROTEIN
RP   SEQUENCE.
RX   PubMed=9062558; DOI=10.1177/00220345970760020501;
RA   Hu C.C., Fukae M., Uchida T., Qian Q., Zhang C.H., Ryu O.H., Tanabe T.,
RA   Yamakoshi Y., Murakami C., Dohi N., Shimizu M., Simmer J.P.;
RT   "Sheathlin: cloning, cDNA/polypeptide sequences, and immunolocalization of
RT   porcine enamel sheath proteins.";
RL   J. Dent. Res. 76:648-657(1997).
RN   [2]
RP   PROTEIN SEQUENCE OF 27-45, PHOSPHORYLATION AT SER-43, HYDROXYLATION AT
RP   PRO-37, AND GLYCOSYLATION AT SER-112.
RX   PubMed=17890672; DOI=10.1177/154405910708601009;
RA   Kobayashi K., Yamakoshi Y., Hu J.C., Gomi K., Arai T., Fukae M.,
RA   Krebsbach P.H., Simmer J.P.;
RT   "Splicing determines the glycosylation state of ameloblastin.";
RL   J. Dent. Res. 86:962-967(2007).
CC   -!- FUNCTION: Involved in the mineralization and structural organization of
CC       enamel.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q28989-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q28989-2; Sequence=VSP_000225;
CC   -!- TISSUE SPECIFICITY: Ameloblast-specific. Located at the Tomes processes
CC       of secretory ameloblasts and in the sheath space between rod-interrod
CC       enamel.
CC   -!- SIMILARITY: Belongs to the ameloblastin family. {ECO:0000305}.
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DR   EMBL; U43404; AAA85588.1; -; mRNA.
DR   RefSeq; NP_999202.1; NM_214037.1. [Q28989-1]
DR   AlphaFoldDB; Q28989; -.
DR   STRING; 9823.ENSSSCP00000009536; -.
DR   iPTMnet; Q28989; -.
DR   PaxDb; Q28989; -.
DR   Ensembl; ENSSSCT00000009789; ENSSSCP00000009536; ENSSSCG00000008937. [Q28989-1]
DR   Ensembl; ENSSSCT00015053638; ENSSSCP00015021503; ENSSSCG00015039943. [Q28989-1]
DR   Ensembl; ENSSSCT00025052922; ENSSSCP00025022555; ENSSSCG00025038905. [Q28989-1]
DR   Ensembl; ENSSSCT00030019756; ENSSSCP00030008795; ENSSSCG00030014345. [Q28989-1]
DR   Ensembl; ENSSSCT00035102009; ENSSSCP00035043475; ENSSSCG00035075042. [Q28989-1]
DR   Ensembl; ENSSSCT00040095398; ENSSSCP00040042261; ENSSSCG00040069531. [Q28989-1]
DR   Ensembl; ENSSSCT00045046846; ENSSSCP00045032518; ENSSSCG00045027395. [Q28989-1]
DR   Ensembl; ENSSSCT00050083601; ENSSSCP00050035887; ENSSSCG00050061349. [Q28989-1]
DR   Ensembl; ENSSSCT00055001828; ENSSSCP00055001385; ENSSSCG00055001024. [Q28989-1]
DR   Ensembl; ENSSSCT00060046288; ENSSSCP00060019818; ENSSSCG00060034115. [Q28989-1]
DR   Ensembl; ENSSSCT00065033259; ENSSSCP00065013740; ENSSSCG00065024870. [Q28989-1]
DR   Ensembl; ENSSSCT00070016183; ENSSSCP00070013398; ENSSSCG00070008360. [Q28989-1]
DR   GeneID; 397102; -.
DR   KEGG; ssc:397102; -.
DR   CTD; 258; -.
DR   eggNOG; ENOG502QWCP; Eukaryota.
DR   GeneTree; ENSGT00390000018227; -.
DR   HOGENOM; CLU_051782_0_0_1; -.
DR   InParanoid; Q28989; -.
DR   OMA; KPAMGGD; -.
DR   OrthoDB; 1189806at2759; -.
DR   TreeFam; TF337860; -.
DR   Reactome; R-SSC-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR   Reactome; R-SSC-8957275; Post-translational protein phosphorylation.
DR   Proteomes; UP000008227; Chromosome 8.
DR   Proteomes; UP000314985; Chromosome 8.
DR   Bgee; ENSSSCG00000008937; Expressed in forelimb bud and 32 other tissues.
DR   ExpressionAtlas; Q28989; baseline and differential.
DR   Genevisible; Q28989; SS.
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   1: Evidence at protein level;
KW   Alternative splicing; Biomineralization; Direct protein sequencing;
KW   Extracellular matrix; Glycoprotein; Hydroxylation; Phosphoprotein;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000269|PubMed:17890672"
FT   CHAIN           27..421
FT                   /note="Ameloblastin"
FT                   /id="PRO_0000001194"
FT   REGION          104..126
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          264..311
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          333..421
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        104..118
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        376..407
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         37
FT                   /note="Hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:17890672"
FT   MOD_RES         43
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:17890672"
FT   CARBOHYD        112
FT                   /note="O-linked (GalNAc...) serine"
FT                   /evidence="ECO:0000269|PubMed:17890672"
FT   VAR_SEQ         99..113
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:9062558"
FT                   /id="VSP_000225"
SQ   SEQUENCE   421 AA;  44927 MW;  3610D6D9F16F9BFC CRC64;
     MPALKIPLFK MKDMVLILCL LKMSSAVPAF PRQPGTPGVA SLSLETMRQL GSLQGLNMLS
     QYSRFGFGKS FNSLWMHGLL PPHSSFQWMR PREHETQQYE YSLPVHPPPL PSQPSLQPQQ
     PGQKPFLQPT VVTSIQNPVQ KGVPQPPIYQ GHPPLQQVEG PMVQQQVAPS EKPPEAELPG
     LDFADPQDPS MFPIARLISQ GPVPQDKPSP LYPGMFYMSY GANQLNSPAR LGILSSEEMA
     GGRGGPLAYG AMFPGFGGMR PNLGGMPPNS AKGGDFTLEF DSPAAGTKGP EKGEGGAEGS
     PVAEANTADP ESPALFSEVA SGVLGGLLAN PKGKIPNLAR GPAGRSRGPP GVTPADADPL
     MTPGLADAYE TYGADETTTL GLQEEMTMDS TATPYSEHTS MPGNKAQQPQ IKRDAWRFQE
     P