TY - JOUR
T1 - Evolutionary Analysis of the Mammalian Tuftelin Sequence Reveals Features of Functional Importance
AU - Delgado, S.
AU - Deutsch, D.
AU - Sire, J. Y.
N1 - Publisher Copyright:
© 2017, Springer Science+Business Media New York.
PY - 2017/4/1
Y1 - 2017/4/1
N2 - Tuftelin (TUFT1) is an acidic, phosphorylated glycoprotein, initially discovered in developing enamel matrix. TUFT1 is expressed in many mineralized and non-mineralized tissues. We performed an evolutionary analysis of 82 mammalian TUFT1 sequences to identify residues and motifs that were conserved during 220 million years (Ma) of evolution. We showed that 168 residues (out of the 390 residues composing the human TUFT1 sequence) are under purifying selection. Our analyses identified several, new, putatively functional domains and confirmed previously described functional domains, such as the TIP39 interaction domain, which correlates with nuclear localization of the TUFT1 protein, that was demonstrated in several tissues. We also identified several sites under positive selection, which could indicate evolutionary changes possibly related to the functional diversification of TUFT1 during evolution in some lineages. We discovered that TUFT1 and MYZAP (myocardial zonula adherens protein) share a common ancestor that was duplicated circa 500 million years ago. Taken together, these findings expand our knowledge of TUFT1 evolution and provide new information that will be useful for further investigation of TUFT1 functions.
AB - Tuftelin (TUFT1) is an acidic, phosphorylated glycoprotein, initially discovered in developing enamel matrix. TUFT1 is expressed in many mineralized and non-mineralized tissues. We performed an evolutionary analysis of 82 mammalian TUFT1 sequences to identify residues and motifs that were conserved during 220 million years (Ma) of evolution. We showed that 168 residues (out of the 390 residues composing the human TUFT1 sequence) are under purifying selection. Our analyses identified several, new, putatively functional domains and confirmed previously described functional domains, such as the TIP39 interaction domain, which correlates with nuclear localization of the TUFT1 protein, that was demonstrated in several tissues. We also identified several sites under positive selection, which could indicate evolutionary changes possibly related to the functional diversification of TUFT1 during evolution in some lineages. We discovered that TUFT1 and MYZAP (myocardial zonula adherens protein) share a common ancestor that was duplicated circa 500 million years ago. Taken together, these findings expand our knowledge of TUFT1 evolution and provide new information that will be useful for further investigation of TUFT1 functions.
KW - Evolution
KW - Mammals
KW - Mineralization
KW - MYZAP
KW - TUFT1
KW - Tuftelin
UR - http://www.scopus.com/inward/record.url?scp=85017457274&partnerID=8YFLogxK
U2 - 10.1007/s00239-017-9789-5
DO - 10.1007/s00239-017-9789-5
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C2 - 28409196
AN - SCOPUS:85017457274
SN - 0022-2844
VL - 84
SP - 214
EP - 224
JO - Journal of Molecular Evolution
JF - Journal of Molecular Evolution
IS - 4
ER -