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   13-FEB-2019, entry version 94.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   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
RP   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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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
RT   project: 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
RT   tooth-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
RT   nucleotide exchange factor 5 (ARHGEF5)-Ras homolog gene family member
RT   A (RhoA) 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.,
RA   Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA   Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA   Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA   Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal
RT   cancers.";
RL   Science 314:268-274(2006).
CC   -!- FUNCTION: Tooth-associated epithelia protein that probably plays a
CC       role in odontogenesis, the complex process that results in the
CC       initiation and generation of the tooth. May be incorporated in the
CC       enamel matrix at the end of mineralization process. Involved in
CC       the induction of RHOA activity via interaction with ARHGEF and
CC       expression of downstream factors such as ROCK. Plays a role in
CC       attachment of the junctional epithelium to the tooth surface.
CC       {ECO:0000269|PubMed:25911094}.
CC   -!- SUBUNIT: Interacts (via C-terminus) with ARHGEF5.
CC       {ECO:0000269|PubMed:25911094}.
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
CC       healthy teeth. In periodontitis, absent in the pocket epithelium
CC       of the diseased periodontium but is detected in the gingival
CC       crevicular fluid. {ECO:0000269|PubMed:25911094}.
CC   -!- PTM: O-glycosylated. {ECO:0000250}.
CC   -!- MISCELLANEOUS: ODAM protein is the unique constituent of
CC       calcifying epithelial odontogenic tumors (CEOTs), also known as
CC       Pindborg tumors. CEOTs are benign but locally aggressive
CC       pathologic entities arising mainly in the mandible and commonly
CC       associated with an unerupted or embedded tooth. They are
CC       characterized by the presence of squamous-cell proliferation,
CC       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   UniGene; Hs.143811; -.
DR   ProteinModelPortal; A1E959; -.
DR   BioGrid; 120297; 5.
DR   IntAct; A1E959; 13.
DR   MINT; A1E959; -.
DR   STRING; 9606.ENSP00000379401; -.
DR   iPTMnet; A1E959; -.
DR   PhosphoSitePlus; A1E959; -.
DR   BioMuta; ODAM; -.
DR   PaxDb; A1E959; -.
DR   PRIDE; A1E959; -.
DR   ProteomicsDB; 122; -.
DR   DNASU; 54959; -.
DR   Ensembl; ENST00000396094; ENSP00000379401; ENSG00000109205.
DR   GeneID; 54959; -.
DR   KEGG; hsa:54959; -.
DR   UCSC; uc003hfc.4; human.
DR   CTD; 54959; -.
DR   DisGeNET; 54959; -.
DR   EuPathDB; HostDB:ENSG00000109205.16; -.
DR   GeneCards; ODAM; -.
DR   HGNC; HGNC:26043; ODAM.
DR   HPA; HPA036543; -.
DR   MIM; 614843; gene.
DR   neXtProt; NX_A1E959; -.
DR   OpenTargets; ENSG00000109205; -.
DR   PharmGKB; PA145148342; -.
DR   eggNOG; ENOG410IV9J; Eukaryota.
DR   eggNOG; ENOG411182C; LUCA.
DR   GeneTree; ENSGT00390000011100; -.
DR   HOGENOM; HOG000115257; -.
DR   HOVERGEN; HBG096669; -.
DR   InParanoid; A1E959; -.
DR   OMA; FNSWIPP; -.
DR   OrthoDB; 1237925at2759; -.
DR   PhylomeDB; A1E959; -.
DR   TreeFam; TF338424; -.
DR   Reactome; R-HSA-977225; Amyloid fiber formation.
DR   GeneWiki; ODAM_(gene); -.
DR   GenomeRNAi; 54959; -.
DR   PRO; PR:A1E959; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   Bgee; ENSG00000109205; Expressed in 88 organ(s), highest expression level in minor salivary gland.
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:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
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:0044267; P:cellular protein metabolic process; TAS:Reactome.
DR   GO; GO:0006954; P:inflammatory response; IDA:UniProtKB.
DR   GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEP:HGNC.
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; Complete proteome; Cytoplasm; Glycoprotein;
KW   Nucleus; Polymorphism; Reference proteome; Secreted; Signal.
FT   SIGNAL        1     15       {ECO:0000255}.
FT   CHAIN        16    279       Odontogenic ameloblast-associated
FT                                protein.
FT                                /FTId=PRO_5000183879.
FT   REGION      127    129       Interaction with ARHGEF5.
FT                                {ECO:0000269|PubMed:25911094}.
FT   COMPBIAS     62    206       Gln-rich.
FT   CARBOHYD    115    115       O-linked (GalNAc...) threonine.
FT                                {ECO:0000255}.
FT   CARBOHYD    119    119       O-linked (GalNAc...) threonine.
FT                                {ECO:0000255}.
FT   CARBOHYD    244    244       O-linked (GalNAc...) threonine.
FT                                {ECO:0000255}.
FT   CARBOHYD    249    249       O-linked (GalNAc...) serine.
FT                                {ECO:0000255}.
FT   CARBOHYD    250    250       O-linked (GalNAc...) threonine.
FT                                {ECO:0000255}.
FT   CARBOHYD    251    251       O-linked (GalNAc...) threonine.
FT                                {ECO:0000255}.
FT   CARBOHYD    255    255       O-linked (GalNAc...) threonine.
FT                                {ECO:0000255}.
FT   CARBOHYD    256    256       O-linked (GalNAc...) serine.
FT                                {ECO:0000255}.
FT   CARBOHYD    261    261       O-linked (GalNAc...) threonine.
FT                                {ECO:0000255}.
FT   CARBOHYD    263    263       O-linked (GalNAc...) threonine.
FT                                {ECO:0000255}.
FT   CARBOHYD    273    273       O-linked (GalNAc...) threonine.
FT                                {ECO:0000255}.
FT   CARBOHYD    275    275       O-linked (GalNAc...) serine.
FT                                {ECO:0000255}.
FT   VARIANT     222    222       I -> T (in dbSNP:rs3196714).
FT                                {ECO:0000269|PubMed:14702039}.
FT                                /FTId=VAR_039812.
FT   VARIANT     269    269       E -> D (in a colorectal cancer sample;
FT                                somatic mutation).
FT                                {ECO:0000269|PubMed:16959974}.
FT                                /FTId=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
//