Table 2.

Location of predicted amino acid substitutions in HIFα proteins based upon single nucleotide polymorphisms found by sequencing mRNA pooled from 200 Fundulus heteroclitus embryos

Subunit	Position	Substitutiona	Scoreb	Domainsc
HIF1α	36	F/L	0	bHLH
HIF1α	361	E/A	−1	Between PAC and ODD
HIF1α	370	E/Q	2	Between PAC and ODD
HIF1α	630	T/A	0	Between ODD and TAD-C
HIF2αa	87	A/T	0	Between bHLH and PAS-A
HIF2αa	165	K/R	2	Between PAS-A and PAS-B
HIF2αa	441	H/P	−2	ODD
HIF3α	37	V/G	−3	bHLH
HIF3α	300	T/P	−1	Between PAS-B and PAC
HIF3α	413	E/D	2	Putative prolyl hydroxylation motif
HIF3α	422	S/P	−1	Between PAC and ODD
HIF3α	502	T/A	0	ODD

^aThe first amino acid shown for each substitution is from HIF1α*1 (ALL26120.1; this study), HIF2αa [ALL95711.1 (44)], or HIF3α*1 (ALL26129.1; this study).

^bValues are from BLOSUM62 alignment score matrix (17). Positive scores are conservative substitutions and negative scores are nonconservative substitutions.

^cbHLH, basic helix-loop-helix; PAS, PER-ARNT-SIM domain; PAC, motif COOH-terminal to PAS domain; ODD, oxygen-dependent degradation domain; TAD-C, COOH-terminal transactivation domain.