Evolution of duplications in the transferrin family of proteins.

Department of Biology, Chatham College, Woodland Road, Pittsburgh, PA 15232, USA.
Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology (Impact Factor: 1.9). 02/2005; 140(1):11-25. DOI: 10.1016/j.cbpc.2004.09.012
Source: PubMed

ABSTRACT The transferrin family is a group of proteins, defined by conserved amino acid motifs and putative function, found in both vertebrates and invertebrates. Included in this group are molecules known to bind iron, including serum transferrin, ovotransferrin, lactotransferrin, and melanotransferrin (MTF). Additional members of this family include inhibitor of carbonic anhydrase (ICA; mammals), major yolk protein (sea urchins), saxiphilin (frog), pacifastin (crayfish), and TTF-1 (algae). Most family members contain two lobes (N and C) of around 340 amino acids, the result of an ancient duplication event. In this article, we review the known functions of these proteins and speculate as to when the different homologs arose. From multiple-sequence alignments and neighbor-joining trees using 71 transferrin family sequences from 51 different species, including several novel sequences found in the Takifugu and Ciona genome databases, we conclude that melanotransferrins are much older (>670 MY) and more pervasive than previously thought, and the serum transferrin/melanotransferrin split may have occurred not long after lobe duplication. All subsequent duplication events diverged from the serum transferrin gene. The creation of such a large multiple-sequence alignment provides important information and could, in the future, highlight the role of specific residues in protein function.

  • Source
    • "Members of the transferrin family include serotransferrin (STF) that is found in mammalian blood, ovotransferrin (OTF) encoded by the avian egg white, lactotransferrin (LTF) found in most milk and tears, saliva and other secretory fluids, and melanotransferrin (MTF) isolated from melanoma cells. Functions of transferrin include iron transport from plasma to target cells and regulation of iron levels in biological fluids of organisms (Lambert et al. 2005a). Aquatic animals require certain essential elements for normal life processes, e.g., Fe, Mn, Cu, Co and Zn (Santosh 2002). "
    [Show abstract] [Hide abstract]
    ABSTRACT: In this study, full-length tilapia transferrin (OnTF) isolated from liver cDNA of Nile tilapia (Oreochromis niloticus) was found to have an open reading frame of 2,091-bp encoding 696 amino acid residues. Two additional amino acids: Gly(369) and Gly(370) were observed compared with the reported Nile tilapia transferrin protein sequence. Pre-mature protein has a predicted molecular weight of 78.2 kDa, while mature protein is 73.28 kDa in size. Comparative sequence analysis with transferrin from other species revealed two major putative iron-binding domains designated as the N-lobe and the C-lobe in accordance with the transferrin protein characteristics. The predicted tertiary structure of tilapia transferrin confirmed the presence of iron and anion-binding sites on both lobes that are conserved among transferrins from other species. Quantitative real-time PCR analysis showed significantly higher expression of tilapia transferrin gene in liver than in other tissues (p < 0.05). Transferrin expression in tilapia experimentally infected with 10(6) and 10(8) colony-forming units mL(-1) of Streptococcus agalactiae was significantly upregulated at 24 and 12 h post-infection (hpi), respectively, and decreased afterward. Iron-deficiency in serum of bacterially infected fish was detected at 48 and 24 hpi, respectively. The expression pattern of the transferrin gene and the iron levels of infected tilapia in this study were consistent with the function of transferrin in innate immunity.
    Fish Physiology and Biochemistry 04/2014; 40(5). DOI:10.1007/s10695-014-9941-8 · 1.68 Impact Factor
  • Source
    • "Transferrin of shrimp is poorly studied. Transferrinlike sequences has been found to occur in the crayfish, Pacifastacus leniusculus (Liang et al., 1997; Lambert et al., 2005). Lectin Lectins are important PRP/R to recognise microbial glycoprotein pattern (Lieschke and Trede, 2009). "
    Perspective of Fisheries and Aquaculture in Malaysia, Edited by Nurul Amin S. M., Kamarudin M.S., Arshad A., Romano N, 01/2014: chapter Fish and Crustaceans: Immune System, Vaccine Development and Implications: pages 188 - 207; Universiti Putra Malaysia Press., ISBN: 978-967-344-419-9
  • Source
    • "Each lobe contains a high affinity reversible Fe 3þ binding site. This structure has been proposed to result from a duplication and fusion of an ancestral gene, increasing the number of iron binding sites and therefore protein functionality [13] [14]. Tf is mainly synthesized in the liver, but mRNA transcripts have also been isolated from different tissues [15], including the brain, where Tf expression seems to be species-dependent [16]. "
    [Show abstract] [Hide abstract]
    ABSTRACT: Transferrin (Tf) is a multi-function protein with a central role in iron metabolism, and it is this function that is associated with a role in the innate immune system response. The clear link between Tf and immune defense mechanism lead to propose Tf as a candidate gene for disease resistance. In this study, genomic and cDNA sequences of Tf gene in gilthead seabream (Sparus aurata L.) (SaTf gene), were identified and characterized. SaTf gene structure consists of a coding region of 2076 nucleotides divided into 17 exons and a no-coding region that includes 16 introns and spans 5495 nucleotides. The deduced Tf protein for gilthead seabream is composed of 691 amino acids and consists of an initial peptide and two lobes (N- and C-lobes). This gene structure is similar to that of previously described Tf genes in other fish species. RT-PCR analyses carried out in different tissues and two developmental stages showed tissue-and stage-specific Tf expression in gilthead seabream. Finally, by sequencing the transferrin genomic sequences of 20 unrelated seabreams, 31 SNPs were identified. These data allowed the estimation of the frequency of nucleotide substitution in the SaTf gene as 1SNP per 253 bp. SNPs were detected in different regions of the genomic sequence but they were mainly localized in non-coding regions, specifically, SNP frequency in non-coding regions was fifteen-fold higher than within coding regions.
    Fish &amp Shellfish Immunology 10/2011; 31(4):548-56. DOI:10.1016/j.fsi.2011.07.003 · 3.03 Impact Factor
Show more