ID   ODAM_MACMU              Reviewed;         279 AA.
AC   A1YQ92;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Odontogenic ameloblast-associated protein;
DE   AltName: Full=Apin;
DE   Flags: Precursor;
GN   Name=ODAM; Synonyms=APIN;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Moffatt P., Smith C.E., Nanci A.;
RL   Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Tooth-associated epithelia protein that probably plays a role
CC       in odontogenesis, the complex process that results in the initiation
CC       and generation of the tooth. May be incorporated in the enamel matrix
CC       at the end of mineralization process. Involved in the induction of RHOA
CC       activity via interaction with ARHGEF and expression of downstream
CC       factors such as ROCK. Plays a role in attachment of the junctional
CC       epithelium to the tooth surface. {ECO:0000250|UniProtKB:A1E959}.
CC   -!- SUBUNIT: Interacts (via C-terminus) with ARHGEF5.
CC       {ECO:0000250|UniProtKB:A1E959}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q3HS83}.
CC       Cytoplasm {ECO:0000250|UniProtKB:A1E959}. Nucleus
CC       {ECO:0000250|UniProtKB:A1E959}.
CC   -!- PTM: O-glycosylated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ODAM family. {ECO:0000305}.
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DR   EMBL; EF121759; ABL63509.1; -; mRNA.
DR   RefSeq; NP_001073604.1; NM_001080135.1.
DR   AlphaFoldDB; A1YQ92; -.
DR   STRING; 9544.ENSMMUP00000007918; -.
DR   Ensembl; ENSMMUT00000072769; ENSMMUP00000053531; ENSMMUG00000006029.
DR   GeneID; 707906; -.
DR   KEGG; mcc:707906; -.
DR   CTD; 54959; -.
DR   VEuPathDB; HostDB:ENSMMUG00000006029; -.
DR   eggNOG; ENOG502RM1P; Eukaryota.
DR   GeneTree; ENSGT00390000011100; -.
DR   HOGENOM; CLU_144254_0_0_1; -.
DR   InParanoid; A1YQ92; -.
DR   OrthoDB; 1237925at2759; -.
DR   Proteomes; UP000006718; Chromosome 5.
DR   Bgee; ENSMMUG00000006029; Expressed in olfactory segment of nasal mucosa and 1 other tissue.
DR   GO; GO:0071944; C:cell periphery; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR   GO; GO:0072686; C:mitotic spindle; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0099512; C:supramolecular fiber; IEA:Ensembl.
DR   GO; GO:0031214; P:biomineral tissue development; IEA:UniProtKB-KW.
DR   GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
DR   GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IBA:GO_Central.
DR   GO; GO:0060054; P:positive regulation of epithelial cell proliferation involved in wound healing; IEA:Ensembl.
DR   GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR   GO; GO:0043547; P:positive regulation of GTPase activity; IEA:Ensembl.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; IEA:Ensembl.
DR   GO; GO:0032956; P:regulation of actin cytoskeleton organization; IEA:Ensembl.
DR   InterPro; IPR026802; Odam.
DR   PANTHER; PTHR16237; PTHR16237; 1.
DR   Pfam; PF15424; ODAM; 1.
PE   2: Evidence at transcript level;
KW   Biomineralization; Cytoplasm; Glycoprotein; Nucleus; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000255"
FT   CHAIN           16..279
FT                   /note="Odontogenic ameloblast-associated protein"
FT                   /id="PRO_5000214104"
FT   REGION          100..125
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          127..129
FT                   /note="Interaction with ARHGEF5"
FT                   /evidence="ECO:0000250|UniProtKB:A1E959"
FT   COMPBIAS        100..120
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        115
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        119
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        168
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        244
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        250
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        251
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        255
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        273
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   279 AA;  30791 MW;  F40D9E2464FEC70B CRC64;
     MKIIILLGFL GATLSAPLIP QRLMSASNSN ELLLNLNNGQ LLPLRLQGPL NSWIPPFSGV
     LQQQQQAQIP GLAQFSLSAL DQFAGLFPNQ IPFPGQASFA QGAQAGQVDP SQAQTPPQTQ
     PGPNHVMPYV FSFKMPQEQG QMFEYYPVYV LLPWEQPQQT VPRSPPQTRQ QQYEEQIPFY
     DQFGYIPQLA EPAIPGGQQQ LAFDPQLGTA PEIAVMSTGE EIPYLQKEVI NFRRDSAGVL
     MPSTSPKPST TNVFTSAIDR TITAKFPEEK AKTDGLREP