ODAM_HUMAN
ID ODAM_HUMAN Reviewed; 279 AA.
AC A1E959; Q8WWE5; Q9NWZ9;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Odontogenic ameloblast-associated protein;
DE AltName: Full=Apin;
DE Flags: Precursor;
GN Name=ODAM; Synonyms=APIN;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Moffatt P., Smith C.E., Nanci A.;
RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 112-279, AND VARIANT THR-222.
RC TISSUE=Carcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 127-279.
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INVOLVEMENT IN CEOT.
RX PubMed=14647039; DOI=10.1016/s0022-2143(03)00149-5;
RA Solomon A., Murphy C.L., Weaver K., Weiss D.T., Hrncic R., Eulitz M.,
RA Donnell R.L., Sletten K., Westermark G., Westermark P.;
RT "Calcifying epithelial odontogenic (Pindborg) tumor-associated amyloid
RT consists of a novel human protein.";
RL J. Lab. Clin. Med. 142:348-355(2003).
RN [6]
RP IDENTIFICATION.
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 [7]
RP FUNCTION, INTERACTION WITH ARHGEF5, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
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).
RN [8]
RP VARIANT [LARGE SCALE ANALYSIS] ASP-269.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
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:0000269|PubMed:25911094}.
CC -!- SUBUNIT: Interacts (via C-terminus) with ARHGEF5.
CC {ECO:0000269|PubMed:25911094}.
CC -!- INTERACTION:
CC A1E959; Q13444-2: ADAM15; NbExp=3; IntAct=EBI-5774125, EBI-12137265;
CC A1E959; Q03989: ARID5A; NbExp=3; IntAct=EBI-5774125, EBI-948603;
CC A1E959; O14964: HGS; NbExp=3; IntAct=EBI-5774125, EBI-740220;
CC A1E959; Q71SY5: MED25; NbExp=3; IntAct=EBI-5774125, EBI-394558;
CC A1E959; Q7Z3K3: POGZ; NbExp=3; IntAct=EBI-5774125, EBI-1389308;
CC A1E959; O00560: SDCBP; NbExp=3; IntAct=EBI-5774125, EBI-727004;
CC A1E959; P09234: SNRPC; NbExp=3; IntAct=EBI-5774125, EBI-766589;
CC A1E959; Q8IWB4: SPATA31A7; NbExp=3; IntAct=EBI-5774125, EBI-1222614;
CC A1E959; O95231: VENTX; NbExp=3; IntAct=EBI-5774125, EBI-10191303;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q3HS83}.
CC Cytoplasm {ECO:0000269|PubMed:25911094}. Nucleus
CC {ECO:0000269|PubMed:25911094}.
CC -!- TISSUE SPECIFICITY: Expressed in the junctional epithelium of healthy
CC teeth. In periodontitis, absent in the pocket epithelium of the
CC diseased periodontium but is detected in the gingival crevicular fluid.
CC {ECO:0000269|PubMed:25911094}.
CC -!- PTM: O-glycosylated. {ECO:0000250}.
CC -!- MISCELLANEOUS: ODAM protein is the unique constituent of calcifying
CC epithelial odontogenic tumors (CEOTs), also known as Pindborg tumors.
CC CEOTs are benign but locally aggressive pathologic entities arising
CC mainly in the mandible and commonly associated with an unerupted or
CC embedded tooth. They are characterized by the presence of squamous-cell
CC proliferation, calcification, and, notably, amyloid deposits.
CC -!- SIMILARITY: Belongs to the ODAM family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91226.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; EF113908; ABL11577.1; -; mRNA.
DR EMBL; CH471057; EAX05612.1; -; Genomic_DNA.
DR EMBL; AK000520; BAA91226.1; ALT_INIT; mRNA.
DR EMBL; BC017796; AAH17796.1; -; mRNA.
DR CCDS; CCDS3536.2; -.
DR RefSeq; NP_060325.3; NM_017855.3.
DR AlphaFoldDB; A1E959; -.
DR BioGRID; 120297; 15.
DR IntAct; A1E959; 13.
DR MINT; A1E959; -.
DR STRING; 9606.ENSP00000379401; -.
DR GlyGen; A1E959; 13 sites, 1 O-linked glycan (1 site).
DR iPTMnet; A1E959; -.
DR PhosphoSitePlus; A1E959; -.
DR BioMuta; ODAM; -.
DR MassIVE; A1E959; -.
DR PaxDb; A1E959; -.
DR PeptideAtlas; A1E959; -.
DR PRIDE; A1E959; -.
DR Antibodypedia; 24311; 31 antibodies from 14 providers.
DR DNASU; 54959; -.
DR Ensembl; ENST00000396094.6; ENSP00000379401.2; ENSG00000109205.17.
DR Ensembl; ENST00000683306.1; ENSP00000507531.1; ENSG00000109205.17.
DR GeneID; 54959; -.
DR KEGG; hsa:54959; -.
DR MANE-Select; ENST00000683306.1; ENSP00000507531.1; NM_017855.4; NP_060325.3.
DR UCSC; uc003hfc.4; human.
DR CTD; 54959; -.
DR DisGeNET; 54959; -.
DR GeneCards; ODAM; -.
DR HGNC; HGNC:26043; ODAM.
DR HPA; ENSG00000109205; Tissue enriched (salivary).
DR MIM; 614843; gene.
DR neXtProt; NX_A1E959; -.
DR OpenTargets; ENSG00000109205; -.
DR PharmGKB; PA145148342; -.
DR VEuPathDB; HostDB:ENSG00000109205; -.
DR eggNOG; ENOG502RM1P; Eukaryota.
DR GeneTree; ENSGT00390000011100; -.
DR HOGENOM; CLU_096142_0_0_1; -.
DR InParanoid; A1E959; -.
DR OMA; NHVMPYV; -.
DR OrthoDB; 1237925at2759; -.
DR PhylomeDB; A1E959; -.
DR TreeFam; TF338424; -.
DR PathwayCommons; A1E959; -.
DR Reactome; R-HSA-977225; Amyloid fiber formation.
DR SignaLink; A1E959; -.
DR BioGRID-ORCS; 54959; 9 hits in 1057 CRISPR screens.
DR ChiTaRS; ODAM; human.
DR GeneWiki; ODAM_(gene); -.
DR GenomeRNAi; 54959; -.
DR Pharos; A1E959; Tbio.
DR PRO; PR:A1E959; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; A1E959; protein.
DR Bgee; ENSG00000109205; Expressed in periodontal ligament and 117 other tissues.
DR ExpressionAtlas; A1E959; baseline and differential.
DR Genevisible; A1E959; HS.
DR GO; GO:0071944; C:cell periphery; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0072686; C:mitotic spindle; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0099512; C:supramolecular fiber; IDA:UniProtKB.
DR GO; GO:0031214; P:biomineral tissue development; IEA:UniProtKB-KW.
DR GO; GO:0006954; P:inflammatory response; IDA:UniProtKB.
DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEP:HGNC-UCL.
DR GO; GO:0060054; P:positive regulation of epithelial cell proliferation involved in wound healing; IEP:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IMP:UniProtKB.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:UniProtKB.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IDA:UniProtKB.
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..279
FT /note="Odontogenic ameloblast-associated protein"
FT /id="PRO_5000183879"
FT REGION 127..129
FT /note="Interaction with ARHGEF5"
FT /evidence="ECO:0000269|PubMed:25911094"
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 119
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"
FT VARIANT 222
FT /note="I -> T (in dbSNP:rs3196714)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_039812"
FT VARIANT 269
FT /note="E -> D (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_039813"
SQ SEQUENCE 279 AA; 30777 MW; DE0E42076B572318 CRC64;
MKIIILLGFL GATLSAPLIP QRLMSASNSN ELLLNLNNGQ LLPLQLQGPL NSWIPPFSGI
LQQQQQAQIP GLSQFSLSAL DQFAGLLPNQ IPLTGEASFA QGAQAGQVDP LQLQTPPQTQ
PGPSHVMPYV FSFKMPQEQG QMFQYYPVYM VLPWEQPQQT VPRSPQQTRQ QQYEEQIPFY
AQFGYIPQLA EPAISGGQQQ LAFDPQLGTA PEIAVMSTGE EIPYLQKEAI NFRHDSAGVF
MPSTSPKPST TNVFTSAVDQ TITPELPEEK DKTDSLREP
