ID   ODAM_BOVIN              Reviewed;         277 AA.
AC   A1YQ93;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Odontogenic ameloblast-associated protein;
DE   AltName: Full=Apin;
DE   Flags: Precursor;
GN   Name=ODAM; Synonyms=APIN;
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].
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; EF121760; ABL63510.1; -; mRNA.
DR   RefSeq; NP_001073784.1; NM_001080315.1.
DR   AlphaFoldDB; A1YQ93; -.
DR   STRING; 9913.ENSBTAP00000039362; -.
DR   PaxDb; A1YQ93; -.
DR   Ensembl; ENSBTAT00000039572; ENSBTAP00000039362; ENSBTAG00000006810.
DR   GeneID; 613976; -.
DR   KEGG; bta:613976; -.
DR   CTD; 54959; -.
DR   VEuPathDB; HostDB:ENSBTAG00000006810; -.
DR   VGNC; VGNC:50115; ODAM.
DR   eggNOG; ENOG502RM1P; Eukaryota.
DR   GeneTree; ENSGT00390000011100; -.
DR   InParanoid; A1YQ93; -.
DR   OMA; NHVMPYV; -.
DR   OrthoDB; 1237925at2759; -.
DR   Proteomes; UP000009136; Chromosome 6.
DR   Bgee; ENSBTAG00000006810; Expressed in milk and 4 other tissues.
DR   ExpressionAtlas; A1YQ93; baseline.
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..277
FT                   /note="Odontogenic ameloblast-associated protein"
FT                   /id="PRO_5000214105"
FT   REGION          103..124
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   CARBOHYD        115
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        208
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        248
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        271
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   277 AA;  31163 MW;  B24B6CF68084B2E6 CRC64;
     MRTLILLGIL GATMSAPLIP QHLMSASNSN ELLLNLNNAQ LRPLQLQGPF NSWFPPFPGI
     LQQQQQNQVP GLSPFSLSTR EWFAGLVPNQ IFVPGQVSFA QGTQAGQLDP SQPQTPQQTQ
     RGPKNVMPSV FFKMPQEQAQ MLQYYPVYMF LPWEQPQQTV AQSPPQTREQ LFEKQMPFYT
     EFGYIPQQVE PVMPVEQQQP VFDPFLGTAP EIAAMPAEVS PYLQKEMINF QHTNAGIFIP
     STSQKPSTTI FFTSAVDPII TRELTEKKAK TDSLKEP