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Fig. 2. Amino acid alignment of human, macaque, rat, mouse, dog, rabbit, sheep,
cow, pig, chicken, turkey, zebrafish and Atlantic cod PepT1. Multiple sequence
alignment was generated using Clustal W 1.82 using the tool at the
www.ebi.ac.uk/clustalw
web site with the following (default) parameters: Matrix=Gonnet 250, Gap
Open=10, End Gaps=–1, Gap Extension=0.2, Gap Distances=4. Putative
transmembrane segments (Ia to XII) were predicted using the TMHMM 2.0 program
(TMHMM Server v. 2.0 at
http://www.cbs.dtu.dk/services/TMHMM-2.0/),
which is part of the Simple Modular Architecture Research Tool (SMART; at
http://www.expasy.org/prosite/),
and are indicated by grey-boxed double-headed broken arrows (with darker grey
designating the core stretch of amino acids within each putative
TMHMM-predicted transmembrane segment that is shared by at least two of the
aligned sequences). Within each sequence, the topological location of each
TMHMM2-predicted transmembrane helix is specifically underlined. Potential
phosphorylation (solid triangle, protein kinase C; solid circle, protein
kinase A) and N-glycosylation (Y) sites are indicated and
correspondently highlighted in dark grey, light grey and dark green,
respectively, along the sequences where found. The proposed `PTR2 family
proton/oligopeptide symporters signature 1' motif (PROSITE pattern: PS01022;
amino acid residues 77–101 in Atlantic cod PepT1) and `PTR2 family
proton/oligopeptide symporters signature 2' motif (PROSITE pattern: PS01023;
amino acid residues 170–182 in Atlantic cod PepT1) are highlighted in
black. Individual amino acid residues identified by site-directed mutagenesis
in PepT1 proteins from various mammalian species and found to be either
involved in transport activity or responsible for incorrect synthesis and/or
transport of the protein to the plasma membrane are indicated in red (for
details, see Table 1).
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