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Fig. 1. Amino acid alignment of ccKir2.5 channel with other members of the
vertebrate Kir2 subfamily (A) and sequence similarities of vertebrate Kir
channels (B). (A) Functionally important transmembrane domains (M1 and M2) and
the intervening pore domain (P) are indicated with horizontal lines. Amino
acids involved in Ba2+, polyamine and phosphatidylinositol
4,5-bisphosphate binding are identified with filled circles, filled triangles
and asterisks, respectively. (B) Nucleic acid identity (above the line) and
amino acid identity (below the line) of vertebrate Kir2.1 (top) and Kir2.2
(middle). Species included are: crucian carp (cc; EU182582 for Kir2.1 and
EU182583 for Kir2.2), rainbow trout (om; DQ435674 and DQ435676), human (h;
NP_000882 and NP_066292), guinea-pig (gp; Q549A2 and AAG17048), rat (r;
NP_058992 and NP_446433) and mouse (m; NP_032451 and NP_034733). Nucleotide
and amino acid sequence identities and similarities of crucian carp Kir2.5
(EU182584) with all known mouse Kirs are shown at the bottom, including Kir1.1
(NM_001012387), Kir2.1 (NM_008425), Kir2.2 (NM_010603), Kir2.3 (NM_008427),
Kir2.4 (NM_145963), Kir3.1 (NM_008426), Kir3.2 (NM_001025584), Kir3.3
(NM_008429), Kir3.4 (NM_010605), Kir4.1 (NM_001039484), Kir4.2 (NM_001039057),
Kir5.1 (NM_010604), Kir6.1 (NM_008428), Kir6.2 (NM_010602) and Kir7.1
(XM_001473740). Zebrafish Kir6.3 (NM_001012387) is also included.
