ID   ODAM_PANTR              Reviewed;         279 AA.
AC   A1YQ94;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 54.
DE   RecName: Full=Odontogenic ameloblast-associated protein;
DE   AltName: Full=Apin;
DE   Flags: Precursor;
GN   Name=ODAM; Synonyms=APIN;
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598;
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; EF121761; ABL63511.1; -; mRNA.
DR   RefSeq; NP_001073385.1; NM_001079916.1.
DR   AlphaFoldDB; A1YQ94; -.
DR   STRING; 9598.ENSPTRP00000027726; -.
DR   PaxDb; A1YQ94; -.
DR   GeneID; 461282; -.
DR   KEGG; ptr:461282; -.
DR   CTD; 54959; -.
DR   eggNOG; ENOG502RM1P; Eukaryota.
DR   InParanoid; A1YQ94; -.
DR   OrthoDB; 1237925at2759; -.
DR   Proteomes; UP000002277; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0031214; P:biomineral tissue development; IEA:UniProtKB-KW.
DR   GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IBA:GO_Central.
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_5000214106"
FT   REGION          127..129
FT                   /note="Interaction with ARHGEF5"
FT                   /evidence="ECO:0000250|UniProtKB:A1E959"
FT   REGION          243..279
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        243..262
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        264..279
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        115
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        249
FT                   /note="O-linked (GalNAc...) serine"
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        256
FT                   /note="O-linked (GalNAc...) serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        261
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        263
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        273
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        275
FT                   /note="O-linked (GalNAc...) serine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   279 AA;  30688 MW;  DA3A43EFACEC5276 CRC64;
     MKIIILLGFL GATLSAPLIP QRLTSASNSN ELLLNLNNGQ LLPLQLQGPL NSWIPPFSGI
     LQQQQQAQIP GLSQFSLSAL DQFAGLLPNQ IPFPGQASFA QGAQAGHVDP LQLQTPPQTQ
     PGPSHVMPYV FSFKMPQEQG QMFQYYPVYM LLPWEQPQQT VPRSPQQTRQ QQYEEQIPFY
     AQFGYIPQLA EPATSGGQQQ LAFDPQLGTA PEIAVMSTGE EIPYLGKEAI NFRHDSAGVF
     MPSTSPKPST TNAFTSAVDQ TITPELPEEK DKTDSLREP