ODAM_PIG
ID ODAM_PIG Reviewed; 276 AA.
AC Q003G9;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 25-MAY-2022, entry version 55.
DE RecName: Full=Odontogenic ameloblast-associated protein;
DE AltName: Full=Apin;
DE Flags: Precursor;
GN Name=ODAM; Synonyms=APIN;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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 -!- PTM: O-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ODAM family. {ECO:0000305}.
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DR EMBL; DQ980195; ABI98813.1; -; mRNA.
DR RefSeq; NP_001072154.1; NM_001078686.1.
DR AlphaFoldDB; Q003G9; -.
DR STRING; 9823.ENSSSCP00000009881; -.
DR PaxDb; Q003G9; -.
DR GeneID; 780437; -.
DR KEGG; ssc:780437; -.
DR CTD; 54959; -.
DR eggNOG; ENOG502RM1P; Eukaryota.
DR InParanoid; Q003G9; -.
DR OrthoDB; 1237925at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0031214; P:biomineral tissue development; IEA:UniProtKB-KW.
DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IBA:GO_Central.
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..276
FT /note="Odontogenic ameloblast-associated protein"
FT /id="PRO_5000006628"
FT REGION 125..127
FT /note="Interaction with ARHGEF5"
FT /evidence="ECO:0000250|UniProtKB:A1E959"
FT CARBOHYD 101
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 113
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 117
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 246
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 247
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 248
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 253
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 254
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 260
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 270
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 272
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 276 AA; 30700 MW; 323B0F8C563C5793 CRC64;
MRTLILLGIL GATMSAPLIP QRLMSASNSN ELLLNLNNAQ LQPLQLQGPW IPPFPVILQQ
RQQQAQIPGL SQFSLANLDW FAGLVPNQRA FPGQVSFAQV TEARQLDPSQ PQTSPQTQQG
PNYVMPSLLS FKMPPEQGQM LQYYPVYMLL PWEQAQQTAA QSPPQTGQQL FEEQMPFYTE
LGYVPQQVEP VMPGGQQQPV FDPFLGTAPE TAVMTAEVLP YFQKEMIQFK HSNGGIFIPS
TSQKPSTTNV FTSTVDPTIT PKVMEKKAKT DSLKEP
