ODAM_MOUSE
ID ODAM_MOUSE Reviewed; 273 AA.
AC A1E960; Q9D7E6;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Odontogenic ameloblast-associated protein;
DE AltName: Full=Apin;
DE Flags: Precursor;
GN Name=Odam; Synonyms=Apin;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=CD-1; TISSUE=Mandible;
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 MRNA] OF 105-273.
RC STRAIN=C57BL/6J; TISSUE=Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 114-273.
RC TISSUE=Brain;
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 [4]
RP TISSUE SPECIFICITY.
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).
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 -!- TISSUE SPECIFICITY: Highly expressed in tooth-associated epithelia.
CC Predominantly expressed in mandible. {ECO:0000269|PubMed:17647262}.
CC -!- PTM: O-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ODAM family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI32395.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAI32397.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB26200.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; EF113909; ABL11578.1; -; mRNA.
DR EMBL; AK009298; BAB26200.1; ALT_INIT; mRNA.
DR EMBL; BC132394; AAI32395.1; ALT_INIT; mRNA.
DR EMBL; BC132396; AAI32397.1; ALT_INIT; mRNA.
DR CCDS; CCDS19394.2; -.
DR RefSeq; NP_081404.2; NM_027128.2.
DR RefSeq; XP_006535273.1; XM_006535210.3.
DR AlphaFoldDB; A1E960; -.
DR STRING; 10090.ENSMUSP00000117898; -.
DR GlyGen; A1E960; 9 sites.
DR PhosphoSitePlus; A1E960; -.
DR PaxDb; A1E960; -.
DR PRIDE; A1E960; -.
DR Antibodypedia; 24311; 31 antibodies from 14 providers.
DR DNASU; 69592; -.
DR Ensembl; ENSMUST00000113274; ENSMUSP00000108899; ENSMUSG00000009580.
DR Ensembl; ENSMUST00000129757; ENSMUSP00000117898; ENSMUSG00000009580.
DR GeneID; 69592; -.
DR KEGG; mmu:69592; -.
DR UCSC; uc008xzd.1; mouse.
DR CTD; 54959; -.
DR MGI; MGI:1916842; Odam.
DR VEuPathDB; HostDB:ENSMUSG00000009580; -.
DR eggNOG; ENOG502RM1P; Eukaryota.
DR GeneTree; ENSGT00390000011100; -.
DR HOGENOM; CLU_096142_0_0_1; -.
DR InParanoid; A1E960; -.
DR OMA; NHVMPYV; -.
DR OrthoDB; 1237925at2759; -.
DR PhylomeDB; A1E960; -.
DR TreeFam; TF338424; -.
DR BioGRID-ORCS; 69592; 3 hits in 74 CRISPR screens.
DR PRO; PR:A1E960; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; A1E960; protein.
DR Bgee; ENSMUSG00000009580; Expressed in molar tooth and 23 other tissues.
DR Genevisible; A1E960; MM.
DR GO; GO:0071944; C:cell periphery; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0072686; C:mitotic spindle; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0099512; C:supramolecular fiber; ISO:MGI.
DR GO; GO:0031214; P:biomineral tissue development; IEA:UniProtKB-KW.
DR GO; GO:0006954; P:inflammatory response; ISO:MGI.
DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IBA:GO_Central.
DR GO; GO:0060054; P:positive regulation of epithelial cell proliferation involved in wound healing; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISO:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISO:MGI.
DR GO; GO:0009611; P:response to wounding; IDA:UniProtKB.
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..273
FT /note="Odontogenic ameloblast-associated protein"
FT /id="PRO_5000183880"
FT REGION 100..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 125..127
FT /note="Interaction with ARHGEF5"
FT /evidence="ECO:0000250|UniProtKB:A1E959"
FT REGION 240..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 114
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 118
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 159
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 241
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 247
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 252
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 258
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 267
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 273 AA; 29820 MW; CA8B395AE68985B6 CRC64;
MKIIILLGLI GASSSAPLIS QRLLSASNSH ELLLNLNNGQ LLPLQFQGAF NSWIPPFPGF
LQQQQAQVSG RPQFTLSTLE SFAGLFPNQI PLSRQVGLAQ GGQAGQPDLS QQQTPPQTQQ
SASPMSYVVP VKVPQDQTQM FQYYPVYMLL PWEQPQTVTS SPQHTGQQLF EEQIPFYNQF
GFAPPQAEPG VPGGQQHLAF DSFVGTAPET PGMPVEGSLL YPQKEPISFK HDNAGVFMPT
TSPKPSTDNF FTSGIDPTIA PEQKVKTDSL REP
