ID VP1_POVBA Reviewed; 362 AA. AC P14996; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1990, sequence version 1. DT 19-OCT-2011, entry version 57. DE RecName: Full=Major capsid protein VP1; DE AltName: Full=Major structural protein VP1; OS BK polyomavirus (strain AS) (BKPyV). OC Viruses; dsDNA viruses, no RNA stage; Polyomaviridae; Polyomavirus. OX NCBI_TaxID=10631; OH NCBI_TaxID=9606; Homo sapiens (Human). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=89095020; PubMed=2536111; RA Tavis J.E., Walker D.L., Gardner S.D., Frisque R.J.; RT "Nucleotide sequence of the human polyomavirus AS virus, an antigenic RT variant of BK virus."; RL J. Virol. 63:901-911(1989). RN [2] RP REVIEW. RX PubMed=19157478; DOI=10.1016/j.virol.2008.12.021; RA Neu U., Stehle T., Atwood W.J.; RT "The Polyomaviridae: Contributions of virus structure to our RT understanding of virus receptors and infectious entry."; RL Virology 384:389-399(2009). CC -!- FUNCTION: Forms an icosahedral capsid with a T=7 symmetry and a 50 CC nm diameter. The capsid is composed of 72 pentamers linked to each CC other by disulfide bonds and associated with VP2 or VP3 proteins. CC Interacts with gangliosides GT1b and GD1b containing terminal CC alpha(2-8)-linked sialic acids on the cell surface to provide CC virion attachment to target cell. This attachment induces virion CC internalization predominantly through caveolin-mediated CC endocytosis and traffics to the endoplasmic reticulum. Inside the CC endoplasmic reticulum, the protein folding machinery isomerizes CC VP1 interpentamer disulfide bonds, thereby triggering initial CC uncoating. Next, the virion uses the endoplasmic reticulum- CC associated degradation machinery to probably translocate in the CC cytosol before reaching the nucleus. Nuclear entry of the viral CC DNA involves the selective exposure and importin recognition of CC VP2/Vp3 nuclear localization signal. In late phase of infection, CC neo-synthesized VP1 encapsulates replicated genomic DNA in the CC nucleus, and participates in rearranging nucleosomes around the CC viral DNA (By similarity). CC -!- SUBUNIT: Homomultimer; disulfide-linked. The virus capsid is CC composed of 72 icosahedral units, each one composed of five CC disulfide-linked copies of VP1. Interacts with minor capsid CC proteins VP2 and VP3 (By similarity). CC -!- SUBCELLULAR LOCATION: Virion. Host nucleus (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing, Alternative initiation; Named isoforms=5; CC Name=VP1; CC IsoId=P14996-1; Sequence=Displayed; CC Note=Produced by alternative splicing of the late mRNA; CC Name=VP2; Synonyms=Minor capsid protein VP2; CC IsoId=P14997-1; Sequence=External; CC Note=Produced by alternative splicing of the late mRNA; CC Name=VP3; Synonyms=Minor capsid protein VP3; CC IsoId=P14997-2; Sequence=External; CC Note=Produced by alternative initiation at Met-120 of isoform CC VP2; CC Name=VP4; Synonyms=Viroporin VP4; CC IsoId=P14997-3; Sequence=External; CC Note=Produced by alternative initiation at Met-229 of isoform CC VP2; CC Name=Agno; CC IsoId=P14998-1; Sequence=External; CC Note=Produced by alternative initiation of the late mRNA; CC -!- DOMAIN: The N-terminal region contains a nuclear signal but the CC presence of VP2 and VP3 proteins is required for efficient nuclear CC transport (By similarity). CC -!- DOMAIN: The intrinsically disordered C-terminal region interacts CC with neighboring pentamers. The unstructured nature of this region CC allows to make different interactions depending on the stuctural CC context: pentamers present at the 12 icosahedral fivefold axes CC bind five pentamers, when pentamers present at the 60 icosahedral CC six-fold axes interacts with six pentamers (By similarity). CC -!- SIMILARITY: Belongs to the polyomaviruses coat protein VP1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M23122; AAA46882.1; -; Genomic_DNA. DR PIR; D33278; VVVP1S. DR ProteinModelPortal; P14996; -. DR SMR; P14996; 15-361. DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW. DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro. DR GO; GO:0044419; P:interspecies interaction between organisms; IEA:UniProtKB-KW. DR InterPro; IPR000662; Capsid_VP1_Polyomavir. DR InterPro; IPR011222; dsDNA_vir_gr_I_capsid. DR Gene3D; G3DSA:2.60.175.10; Polyoma_coat_VP1; 1. DR Pfam; PF00718; Polyoma_coat; 1. DR PIRSF; PIRSF003376; Capsid_VP1_Polyomavir; 1. DR SUPFAM; SSF88648; dsDNA_vir_gr_I_capsid; 1. PE 3: Inferred from homology; KW Alternative initiation; Alternative splicing; Capsid protein; KW Caveolin-mediated endocytosis of virus by host; Complete proteome; KW Disulfide bond; Host nucleus; Host-virus interaction; KW Initiation of viral infection; Late protein; Phosphoprotein; KW T=7 icosahedral capsid protein; Viral attachment to host cell; KW Viral penetration into host cytoplasm; Virion; KW Virus endocytosis by host. FT CHAIN 1 362 Major capsid protein VP1. FT /FTId=PRO_0000115017. FT REGION 302 362 Intrinsically disordered (By similarity). FT MOTIF 2 17 Bipartite nuclear localization signal (By FT similarity). FT MOD_RES 338 338 Phosphothreonine; by host (By FT similarity). FT DISULFID 10 10 Interchain (with C-10) (By similarity). FT DISULFID 105 105 Interchain (with C-105) (By similarity). SQ SEQUENCE 362 AA; 40113 MW; 5BDCEC52F247F238 CRC64; MAPTKRKGEC PGAAPKKPKE PVQVPKLLIK GGVEVLEVKT GVDAITEVEC FLNPEMGDPD DNLRGYSQHL SAENAFESDS PDRKMLPCYS TARIPLPNLN EDLTCGNLLM WEAVTVKTEV IGITSMLNLH AGSQKVHENG GGKPVQGSNF HFFAVGGDPL EMQGVLMNYR TKYPQGTITP KNPTAQSQVM NTDHKAYLDK NNAYPVECWI PDPSRNENTR YFGTYTGGEN VPPVLHVTNT ATTVLLDEQG VGPLCKADSL YVSAADICGL FTNSSGTQQW RGLARYFKIR LRKRSVKNPY PISFLLSDLI NRRTQKVDGQ PMYGMESQVE EVRVFDGTEQ LPGDPDMIRY IDRQGQLQTK MV //