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. 2019 Dec 5;61(3):432–444. doi: 10.1194/jlr.M094540

Fig. 1.

Fig. 1.

Sequence alignment of apo(a) and plasminogen kringle domains show the R990 and R1771 residues to be homologous to plasminogen deficiency mutations. Alignment of single copy kringle domains and the first KIV-2 domain of apo(a) as well as kringle domains of plasminogen performed using Clustal Omega. Shading was performed in Jalview with residue sequence identity set to 50%. Conserved cysteine residues involved in intra-kringle disulfide linkages are shaded yellow and surrounded by blue boxes. The R990Q and R1771C residues and those mutated in cases of plasminogen deficiency (R153K, R235H, R325H, and R532H) are shaded blue, and this position is surrounded by blue boxes. The numbering scheme for apo(a) kringle domains is based on the NCBI apo(a) precursor protein sequence (NP_005568.2). The numbering scheme for amino acids in the plasminogen kringle domains is based on GenBank plasminogen sequence AAA60113.1. This plasminogen sequence contains the signal peptide hence the numbering of the mutant plasminogen residues shown in blue here is +19 to the positions previously described as R134K, R216H, R306H, and R513H.