ODAM_RAT
ID ODAM_RAT Reviewed; 278 AA.
AC Q3HS83;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Odontogenic ameloblast-associated protein;
DE AltName: Full=Apin;
DE Flags: Precursor;
GN Name=Odam; Synonyms=Apin; ORFNames=EO-009;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=16674676; DOI=10.1111/j.1600-0722.2006.00318.x;
RA Moffatt P., Smith C.E., Sooknanan R., St Arnaud R., Nanci A.;
RT "Identification of secreted and membrane proteins in the rat incisor enamel
RT organ using a signal-trap screening approach.";
RL Eur. J. Oral Sci. 114:139-146(2006).
RN [2]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=17451507; DOI=10.1111/j.1600-0722.2007.00435.x;
RA Park J.-C., Park J.-T., Son H.-H., Kim H.-J., Jeong M.-J., Lee C.-S.,
RA Dey R., Cho M.-I.;
RT "The amyloid protein APin is highly expressed during enamel mineralization
RT and maturation in rat incisors.";
RL Eur. J. Oral Sci. 115:153-160(2007).
RN [3]
RP TISSUE SPECIFICITY, AND GLYCOSYLATION.
RX PubMed=17647262; DOI=10.1002/jcb.21465;
RA Moffatt P., Smith C.E., St Arnaud R., Nanci A.;
RT "Characterization of Apin, a secreted protein highly expressed in tooth-
RT associated epithelia.";
RL J. Cell. Biochem. 103:941-956(2008).
RN [4]
RP DEVELOPMENTAL STAGE.
RX PubMed=25911094; DOI=10.1074/jbc.m115.648022;
RA Lee H.K., Ji S., Park S.J., Choung H.W., Choi Y., Lee H.J., Park S.Y.,
RA Park J.C.;
RT "Odontogenic ameloblast-associated protein (ODAM) Mediates Junctional
RT Epithelium Attachment to Tooth via Integrin-ODAM-Rho guanine nucleotide
RT exchange factor 5 (ARHGEF5)-Ras homolog gene family member A (RhoA)
RT Signaling.";
RL J. Biol. Chem. 290:14740-14753(2015).
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:0000269|PubMed:17451507}. Cytoplasm
CC {ECO:0000250|UniProtKB:A1E959}. Nucleus {ECO:0000250|UniProtKB:A1E959}.
CC -!- TISSUE SPECIFICITY: Highly expressed in tooth-associated epithelia. In
CC tooth, it is only detected in the ameloblast layer of the enamel organ,
CC starting at post-secretory transition and extending throughout the
CC maturation stage. Also detected in epithelial cells of the gingiva
CC which bind it to the tooth surface (junctional epithelium) (at protein
CC level). Predominantly expressed in mandible, but also expressed at weak
CC level in nasal and salivary glands, and at much lower level in
CC epididymis. {ECO:0000269|PubMed:16674676, ECO:0000269|PubMed:17451507,
CC ECO:0000269|PubMed:17647262}.
CC -!- DEVELOPMENTAL STAGE: Specifically expressed in ameloblasts during
CC maturation stages. Not expressed in pre-ameloblasts, weakly expressed
CC in secretory ameloblasts, and strongly expressed in maturation-stage
CC ameloblasts as well as in the junctional epithelium attached to the
CC enamel of erupted molars. {ECO:0000269|PubMed:17451507,
CC ECO:0000269|PubMed:25911094}.
CC -!- PTM: O-glycosylated. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ODAM family. {ECO:0000305}.
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DR EMBL; DQ198380; ABA54404.1; -; mRNA.
DR RefSeq; NP_001037739.1; NM_001044274.1.
DR AlphaFoldDB; Q3HS83; -.
DR STRING; 10116.ENSRNOP00000035991; -.
DR GlyGen; Q3HS83; 6 sites.
DR PaxDb; Q3HS83; -.
DR PRIDE; Q3HS83; -.
DR GeneID; 641555; -.
DR KEGG; rno:641555; -.
DR UCSC; RGD:1561883; rat.
DR CTD; 54959; -.
DR RGD; 1561883; Odam.
DR eggNOG; ENOG502RM1P; Eukaryota.
DR InParanoid; Q3HS83; -.
DR OrthoDB; 1237925at2759; -.
DR PhylomeDB; Q3HS83; -.
DR PRO; PR:Q3HS83; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0071944; C:cell periphery; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005576; C:extracellular region; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0099512; C:supramolecular fiber; ISO:RGD.
DR GO; GO:0031214; P:biomineral tissue development; IEA:UniProtKB-KW.
DR GO; GO:0006954; P:inflammatory response; ISO:RGD.
DR GO; GO:0042476; P:odontogenesis; IEP:UniProtKB.
DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; ISO:RGD.
DR GO; GO:0060054; P:positive regulation of epithelial cell proliferation involved in wound healing; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISO:RGD.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:RGD.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISO:RGD.
DR GO; GO:0009611; P:response to wounding; ISO:RGD.
DR InterPro; IPR026802; Odam.
DR PANTHER; PTHR16237; PTHR16237; 1.
DR Pfam; PF15424; ODAM; 1.
PE 1: Evidence at protein 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_5000140667"
FT REGION 103..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 126..128
FT /note="Interaction with ARHGEF5"
FT /evidence="ECO:0000250|UniProtKB:A1E959"
FT REGION 230..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 116
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 120
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 240
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 243
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 254
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 278 AA; 30443 MW; 572C784AB4BE0B4D CRC64;
MKIIILLGLI GATSSAPLIT QRLLSASNSH ELLLNLNNGQ LLPLQFQSAF NSWIPPFPGL
LQQQQQQAQV SGHPQFPLST LESFAGLFPN QIPFSRQVGF AQGGQAGQPD FSQQQTPSQT
QQASPMSYVV PVKVPQDQTQ MFQYYPVYML LPWEQPQQTV TSSPQQTGQQ LYEEQIPFYN
QFGFVPQQAE PGVPGGQQHL VLDSFVGTAP ETPGMPAVEG PLYPQKEPIG FKQDNVGVST
PSTSPKPDTG NFFTSEINPT IAPLLPEQKV NADSLREP
