Capsid protein self-assembles to form an icosahedral capsid with a T=1 symmetry, about 20 nm in diameter, and consisting of 60 copies of two size variants of the capsid proteins, VP1 and VP2, which differ by the presence of an N-terminal extension in the minor protein VP1. The capsid encapsulates the genomic ssDNA. Binds to erythroid progenitor cells expressing high levels of P antigen and uses host ITGA5-ITGB1 and XRCC5/Ku80 autoantigen as coreceptors on the cell surface to provide virion attachment to target cell. This attachment induces virion internalization predominantly through clathrin-dependent endocytosis. Binding to the host receptors also induces capsid rearrangements leading to surface exposure of VP1 N-terminus, specifically its phospholipase A2-like region. The additional N-terminal region of isoform Minor capsid protein VP1, called VP1u, may serve as a lipolytic enzyme to breach the endosomal membrane during entry into host cell and might contribute to virus transport to the nucleus. a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+) Heteromultimer of isoform Minor capsid protein VP1 and isoform Major capsid protein VP2. Heteromultimer of isoform Minor capsid protein VP1 and isoform Major capsid protein VP2. 20 fold more abundant than the minor capsid protein VP1. The N-terminus of VP1, VP1u, contains a phospholipase A2-like region. VP1u is necessary and sufficient for host cell binding and internalization. A nuclear localization signal is present in the C-terminus and can be recognized by cellular nuclear import molecules. After assembly, it is hidden because it is on the inner capsid surface. Minor splicing isoform. Major splicing isoform produced by deletion of the initiating AUG for VP1 and downstream translation of VP2. Belongs to the parvoviridae capsid protein family. Icosahedral capsid structure