TUFT1_BOVIN
ID TUFT1_BOVIN Reviewed; 390 AA.
AC P27628; O97683;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2002, sequence version 2.
DT 25-MAY-2022, entry version 111.
DE RecName: Full=Tuftelin {ECO:0000303|PubMed:1874744};
DE AltName: Full=Enamelin;
GN Name=TUFT1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=Holstein; TISSUE=Ameloblast;
RX PubMed=1874744; DOI=10.1016/s0021-9258(18)98510-8;
RA Deutsch D., Palmon A., Fisher L.W., Kolodny N., Termine J.D., Young M.F.;
RT "Sequencing of bovine enamelin ('tuftelin') a novel acidic enamel
RT protein.";
RL J. Biol. Chem. 266:16021-16028(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
RC TISSUE=Enamel organ;
RX PubMed=9296268; DOI=10.1016/s0003-9969(97)00039-3;
RA Bashir M.M., Abrams W.R., Rosenbloom J.;
RT "Molecular cloning and characterization of the bovine tuftelin gene.";
RL Arch. Oral Biol. 42:489-496(1997).
RN [3]
RP SEQUENCE REVISION.
RA Bashir M.M., Abrams W.R., Rosenbloom J.;
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the mineralization and structural organization of
CC enamel. {ECO:0000303|PubMed:1874744}.
CC -!- SUBUNIT: Interacts with TFIP11. {ECO:0000250|UniProtKB:O08970}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000303|PubMed:1874744}.
CC Note=Secreted at a very early stage of enamel formation, and tightly
CC bound to the surface of the growing crystallites.
CC {ECO:0000303|PubMed:1874744}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=P27628-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P27628-2; Sequence=VSP_006682;
CC Name=3;
CC IsoId=P27628-3; Sequence=VSP_006683;
CC Name=4;
CC IsoId=P27628-4; Sequence=VSP_006684;
CC -!- TISSUE SPECIFICITY: Present in the extracellular enamel and is mainly
CC associated with the crystal component. {ECO:0000269|PubMed:1874744}.
CC -!- SIMILARITY: Belongs to the tuftelin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA30797.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M64924; AAA30797.1; ALT_FRAME; mRNA.
DR EMBL; AF105228; AAC84147.1; -; mRNA.
DR PIR; A40809; A40809.
DR RefSeq; NP_776904.1; NM_174479.2. [P27628-1]
DR AlphaFoldDB; P27628; -.
DR SMR; P27628; -.
DR STRING; 9913.ENSBTAP00000043710; -.
DR PaxDb; P27628; -.
DR GeneID; 282104; -.
DR KEGG; bta:282104; -.
DR CTD; 7286; -.
DR eggNOG; ENOG502QW76; Eukaryota.
DR InParanoid; P27628; -.
DR OrthoDB; 1003198at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IPI:BHF-UCL.
DR GO; GO:0031214; P:biomineral tissue development; IEA:UniProtKB-KW.
DR InterPro; IPR024846; Tuftelin.
DR PANTHER; PTHR23171:SF4; PTHR23171:SF4; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Biomineralization; Coiled coil; Phosphoprotein;
KW Reference proteome; Secreted.
FT CHAIN 1..390
FT /note="Tuftelin"
FT /id="PRO_0000183185"
FT COILED 88..126
FT /evidence="ECO:0000255"
FT COILED 162..351
FT /evidence="ECO:0000255"
FT MOD_RES 171
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 21..45
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_006682"
FT VAR_SEQ 109..138
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_006683"
FT VAR_SEQ 139..160
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_006684"
FT CONFLICT 242
FT /note="E -> D (in Ref. 2; AAA30797)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 390 AA; 44343 MW; E276261E098E3444 CRC64;
MNGTRNWCTL VDVHPEGQTA GSVDVLRLTL QSELTGDELE RIAQKAGRKT YAMVSSHSTS
HSLASELVES NDGHEEIIKV YLKGRSGDKM IHEKNINQLK SEVQYIQEAR NCLQKLREDI
SSKLDRDPGD SVHKQEIQVV LEKQNGLSEG PLTTYSSPPE VDTHINEDVE SLRKTVQDLL
VKLQEAEQQH QSDCSAFKVT LSQYQREAKQ SQVALQRAED RAEQKEAEVG ELQRRLQGME
TEYQAILAKV REGETALEEL RSKNVDCQAE QEKAANLEKE VAGLREKIHH LDDMLKSQQR
KVRQMIEQLQ NSKAVIQSKD TTIQELKEKI AYLEAENLEM HDRMEHLIEK QISHGNFSTQ
NRAKTENLGS IRISKPPSPK PMPLIRVVET