Figure 2

Multiple alignment of the deduced amino acid sequences of gcHIF-1α and gcHIF-4α with selected human and fish HIF-α homologues. Amino acids are designated by single-letter codes. From top to bottom: gcHIF1α, grass carp HIF-1α rtHIF1α, rainbow trout HIF-1α; hHIF1α, human HIF-1α; fHIF2α, Fundulus heteroclitus HIF-2α; hHIF2α, human HIF-2α; hHIF3α, human HIF-3α; gcHIF4α, grass carp HIF-4α. The number on the left of each row denotes the amino acid position. Identical amino acids shared by most of the HIF-α s are shaded in black while similar amino acids are shaded in grey. Dashes (--) indicate gaps inserted for improved alignment. Domains that are typical characteristic of HIF-α proteins are marked on the alignment according to the amino acid positions in human HIF-1α. The two conserved proline residues within the ODD domain are indicated by open arrows (⇩). The closed arrow () indicates the asparagine residue (Asn-803) in C-TAD which controls HIF-1 binding to CBP/p300.