Fig. 1: Sequence alignment of representative ZnT-family members of known structure. | Nature Communications

Fig. 1: Sequence alignment of representative ZnT-family members of known structure.

From: Cryo-EM structures of human zinc transporter ZnT7 reveal the mechanism of Zn2+ uptake into the Golgi apparatus

Fig. 1

Amino acid sequences of human ZnT7 (hZnT7, UniProt ID: Q8NEW0) and human ZnT8 (hZnT8, UniProt ID: Q8IWU4), Escherichia coli YiiP (EcYiiP, UniProt ID: P69380) and Shewanella oneidensis YiiP (SoYiiP, UniProt ID: Q8E919) were aligned. Highly conserved, similar, and weakly conserved residues are colored black, light blue, and rose, respectively. The α-helix and β-strand elements of hZnT7 are indicated by solid and broken green lines above the amino acid sequence, respectively. The histidine-rich loop (His-loop) is indicated by a broken purple line above the sequence. HDHD-motif residues present in TM2 and TM5 are indicated by light green boxes. Zn2+-binding residues present in the cytosolic domain of hZnT8 and Ec/SoYiiP are indicated by red and violet boxes, respectively; and histidine residues in the His-loop of ZnT7 are indicated by blue boxes. Green stars indicate residues involved in Zn2+ binding. The red triangle indicates His164. TM, transmembrane helix; α and β, alpha-helix and beta-strand in the cytosolic domain, respectively.

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