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 24-JAN-2024, entry version 118. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 GlyCosmos; A1E959; 12 sites, No reported glycans. 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; 9606-ENSP00000379401; -. DR PeptideAtlas; A1E959; -. DR Antibodypedia; 24311; 45 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 AGR; HGNC:26043; -. 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; 4642584at2759; -. DR PhylomeDB; A1E959; -. DR TreeFam; TF338424; -. DR PathwayCommons; A1E959; -. DR Reactome; R-HSA-977225; Amyloid fiber formation. DR SignaLink; A1E959; -. DR BioGRID-ORCS; 54959; 10 hits in 1135 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 119 other cell types or tissues. DR ExpressionAtlas; A1E959; baseline and differential. 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; ODONTOGENIC AMELOBLAST-ASSOCIATED PROTEIN; 1. DR PANTHER; PTHR16237:SF3; ODONTOGENIC AMELOBLAST-ASSOCIATED PROTEIN; 1. DR Pfam; PF15424; ODAM; 1. DR Genevisible; A1E959; HS. 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 //