ID   ODAM_CANLF              Reviewed;         278 AA.
AC   A1YQ91;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Odontogenic ameloblast-associated protein;
DE   AltName: Full=Apin;
DE   Flags: Precursor;
GN   Name=ODAM; Synonyms=APIN;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
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; EF121758; ABL63508.1; -; mRNA.
DR   RefSeq; NP_001091020.1; NM_001097551.1.
DR   AlphaFoldDB; A1YQ91; -.
DR   STRING; 9612.ENSCAFP00000004263; -.
DR   PaxDb; A1YQ91; -.
DR   Ensembl; ENSCAFT00030030614; ENSCAFP00030026698; ENSCAFG00030016596.
DR   Ensembl; ENSCAFT00040009012; ENSCAFP00040007820; ENSCAFG00040004790.
DR   Ensembl; ENSCAFT00845018290; ENSCAFP00845014271; ENSCAFG00845010379.
DR   GeneID; 611755; -.
DR   KEGG; cfa:611755; -.
DR   CTD; 54959; -.
DR   VEuPathDB; HostDB:ENSCAFG00845010379; -.
DR   eggNOG; ENOG502RM1P; Eukaryota.
DR   GeneTree; ENSGT00390000011100; -.
DR   HOGENOM; CLU_096142_0_0_1; -.
DR   InParanoid; A1YQ91; -.
DR   OMA; NHVMPYV; -.
DR   OrthoDB; 1237925at2759; -.
DR   TreeFam; TF338424; -.
DR   Proteomes; UP000002254; Chromosome 13.
DR   Bgee; ENSCAFG00000002882; Expressed in saliva-secreting gland and 3 other tissues.
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..278
FT                   /note="Odontogenic ameloblast-associated protein"
FT                   /id="PRO_5000214103"
FT   REGION          97..123
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        103
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000255"
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        246
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        249
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        272
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   278 AA;  30790 MW;  4B92354A95D8BB6B CRC64;
     MKTIILLGLL GATMSAPLIP QRLMSASNSN ELLLNLNNAQ LQPLPFQGPF NSWIPPFSGI
     LQQQQQAQIP GLSQFSLSAL DRFAGLFPNQ TPFPGRVSFA QGTQVGQQDP SQPQTPPQTQ
     QSPNHVMPYV FSFKMPQEQA QMLQYYPVYM LLPWEQSQQT APQSPPQTGQ QQFEEQMPFY
     TQFGYVPVQV EPVMPGGQQQ LALDPVLGTA PETVVMPAGV IPYLRKEVIN FKHANGGIFV
     PSTSQTPSTT NYFAPAIDPT ITPELMEKKA KTDYLKEP