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 three size variants of the capsid protein VP1, VP2 and VP3 which differ in their N-terminus. The capsid encapsulates the genomic ssDNA. Binds to host cell heparan sulfate and uses host ITGA5-ITGB1 as coreceptor 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 receptor also induces capsid rearrangements leading to surface exposure of VP1 N-terminus, specifically its phospholipase A2-like region and putative nuclear localization signal(s). VP1 N-terminus might serve as a lipolytic enzyme to breach the endosomal membrane during entry into host cell and might contribute to virus transport to the nucleus. Capid proteins are first observed in the host nucleolus where capsid assembly may occur, and then are present over the whole nucleoplasm where encapsidation of the viral DNA takes place. The N-terminus of VP1 is sequestered within the mature capsid. It contains a phospholipase A2-like region and putative nuclear localization signals. AAV capsids serve as viral gene transfer vectors that have been shown to affect long-term gene expression and disease correction with low toxicity in animal models, and are well tolerated in human clinical trials. the ratio at which VP1, VP2 and VP3 proteins are synthesized in vivo is about 1:1:10, which is the same as in the mature virus particle. Produced by alternative splicing (2.6 kb mRNA). Produced by alternative splicing (2.3 kb mRNA), with initiatory methionine encoded by an ACG codon. Produced by alternative initiation of the 2.3 kb mRNA. Belongs to the parvoviridae capsid protein family.