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-JAN-2010, entry version 49.
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).
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. In late phase of infection, neo-
CC       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 transcripts;
CC       Name=VP2;
CC         IsoId=P14997-1; Sequence=External;
CC         Note=Produced by alternative splicing of the late transcripts;
CC       Name=VP3;
CC         IsoId=P14997-2; Sequence=External;
CC         Note=Produced by alternative initiation at Met-120 of isoform
CC         VP2;
CC       Name=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 leader
CC         region;
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   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   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.
PE   3: Inferred from homology;
KW   Alternative initiation; Alternative splicing; Capsid protein;
KW   Complete proteome; Disulfide bond; Host nucleus; Late protein;
KW   Phosphoprotein; Virion.
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
//