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Figure 2


Fig. 2. A schematic representation of HIF-1{alpha} protein in Rana temporaria and other selected vertebrates. The crucial interaction domains and hydroxylation targets of the molecule are shown. The basic helix-loop-helix (bHLH) and the Per-ARNT-Sim (PAS) domains are involved in DNA binding and dimerization of the protein. The oxygen-dependent degradation (ODD) and the C-terminal transactivation domains (C-TAD) confer oxygen-dependent regulation. The figure also gives the length of the deduced HIF-1{alpha} protein and a comparison of its insertion/deletion patterns. In the block diagram, grey represents teleost-specific insertions that are absent from tetrapods. Black represents protein regions that are present in mammalian molecules, but to a variable degree absent from those of other vertebrates. In the schematic representation of the molecules, lines indicate gaps in the alignment. Accession numbers – Homo sapiens: GenBank, NM_001530; Gallus gallus: GenBank, AB013746; Rana temporaria: GenBank, EU262663; Xenopus laevis: GenBank: BC043769; Danio rerio: GenBank, AY326951; and Takifugu rubripes: Ensembl, SINFRUG00000154390.





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