Capsid protein self-assembles to form an icosahedral capsid with a T=1 symmetry, about 22 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. Capsid proteins are responsible for the attachment to host cell receptor TFRC. This attachment induces virion internalization predominantly through clathrin-endocytosis. Binding to the host receptors also induces capsid rearrangements leading to surface exposure of VP1 N-terminus, specifically its phospholipase A2-like region and nuclear localization signal(s). VP1 N-terminus might serve as a lipolytic enzyme to breach the endosomal membrane during entry into host cell. Intracytoplasmic transport involves microtubules and interaction between capsid proteins and host dynein. Exposure of nuclear localization signal probably allows nuclear import of capsids (By similarity). Interacts with host TFRC. The N-terminus of VP1 is sequestered within the mature capsid. It contains a phospholipase A2-like region and nuclear localization signals that might be exposed by capsid modifications during virus entry (By similarity). The capsids of autonomous parvoviruses expose a proportion of VP2 N-terminus and part of that sequence can be cleaved of to form VP3. 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.