VP1_POVMK
ID VP1_POVMK Reviewed; 373 AA.
AC P24595;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 23-FEB-2022, entry version 96.
DE RecName: Full=Major capsid protein VP1;
DE AltName: Full=Major structural protein VP1;
OS Murine polyomavirus (strain Kilham) (MPyV) (Murine pneumotropic virus).
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Sepolyvirales; Polyomaviridae; Betapolyomavirus.
OX NCBI_TaxID=10638;
OH NCBI_TaxID=10090; Mus musculus (Mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1849675; DOI=10.1016/0042-6822(91)90879-g;
RA Mayer M., Doerries K.;
RT "Nucleotide sequence and genome organization of the murine polyomavirus,
RT Kilham strain.";
RL Virology 181:469-480(1991).
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 understanding
RT 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 40 nm
CC diameter. The capsid is composed of 72 pentamers linked to each other
CC by disulfide bonds and associated with VP2 or VP3 proteins. Interacts
CC with terminal alpha(2,3)-linked sialic acids on the cell surface to
CC provide virion attachment to target cell. This attachment induces
CC virion internalization predominantly through caveolin-mediated
CC endocytosis. Once attached, the virion is internalized by caveolin-
CC mediated endocytosis and traffics to the endoplasmic reticulum. Inside
CC the endoplasmic reticulum, the protein folding machinery isomerizes VP1
CC interpentamer disulfide bonds, thereby triggering initial uncoating.
CC Next, the virion uses the endoplasmic reticulum-associated degradation
CC machinery to probably translocate in the cytosol before reaching the
CC nucleus. Nuclear entry of the viral DNA involves the selective exposure
CC and importin recognition of VP2/Vp3 nuclear localization signal. In
CC late phase of infection, neo-synthesized VP1 encapsulates replicated
CC genomic DNA in the nucleus, and participates in rearranging nucleosomes
CC around the viral DNA. {ECO:0000250|UniProtKB:P03087,
CC ECO:0000305|PubMed:19157478}.
CC -!- SUBUNIT: Homomultimer; disulfide-linked. The virus capsid is composed
CC of 72 icosahedral units, each one composed of five disulfide-linked
CC copies of VP1. Interacts with minor capsid proteins VP2 and VP3.
CC {ECO:0000250|UniProtKB:P03087}.
CC -!- SUBCELLULAR LOCATION: Virion. Host nucleus
CC {ECO:0000250|UniProtKB:P03087}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing, Alternative initiation; Named isoforms=3;
CC Name=VP1;
CC IsoId=P24595-1; Sequence=Displayed;
CC Name=VP2; Synonyms=Minor capsid protein VP2;
CC IsoId=P24596-1; Sequence=External;
CC Name=VP3; Synonyms=Minor capsid protein VP3;
CC IsoId=P24596-2; Sequence=External;
CC -!- DOMAIN: The intrinsically disordered C-terminal arm interacts with
CC neighboring pentamers. The unstructured nature of this region allows to
CC make different interactions depending on the structural context:
CC pentamers present at the 12 icosahedral fivefold axes bind five
CC pentamers, whereas pentamers present at the 60 icosahedral six-fold
CC axes interact with six pentamers. {ECO:0000250|UniProtKB:P03087}.
CC -!- MISCELLANEOUS: The virus attaches to the surface of cells by
CC recognition of oligosaccharides terminating in alpha(2,3)-linked sialic
CC acid. Strains that have Gly-92 (small-plaque strains) can also
CC recognize branched oligosaccharides that carry a second alpha(2,6)-
CC linked sialic acid.
CC -!- MISCELLANEOUS: [Isoform VP1]: Produced by alternative splicing of the
CC late mRNA.
CC -!- SIMILARITY: Belongs to the polyomaviruses coat protein VP1 family.
CC {ECO:0000305}.
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DR EMBL; M55904; AAA46553.1; -; Genomic_DNA.
DR PIR; C37945; VVVPK1.
DR RefSeq; NP_041234.1; NC_001505.2.
DR SMR; P24595; -.
DR GeneID; 29031028; -.
DR KEGG; vg:29031028; -.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0039620; C:T=7 icosahedral viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0075513; P:caveolin-mediated endocytosis of virus by host cell; IEA:UniProtKB-KW.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR Gene3D; 2.60.175.10; -; 1.
DR InterPro; IPR000662; Capsid_VP1_Polyomavir.
DR InterPro; IPR011222; dsDNA_vir_gr_I_capsid.
DR InterPro; IPR036931; Polyomavir_VP1_sf.
DR Pfam; PF00718; Polyoma_coat; 1.
DR PIRSF; PIRSF003376; Capsid_VP1_Polyomavir; 1.
DR SUPFAM; SSF88648; SSF88648; 1.
PE 3: Inferred from homology;
KW Alternative initiation; Alternative splicing; Capsid protein;
KW Caveolin-mediated endocytosis of virus by host; Disulfide bond;
KW Host nucleus; Host-virus interaction; Late protein; Phosphoprotein;
KW T=7 icosahedral capsid protein; Viral attachment to host cell;
KW Viral penetration into host cytoplasm; Virion; Virus endocytosis by host;
KW Virus entry into host cell.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000250"
FT CHAIN 2..373
FT /note="Major capsid protein VP1"
FT /id="PRO_0000115027"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 299..373
FT /note="C-terminal arm"
FT /evidence="ECO:0000250|UniProtKB:P03087"
FT DISULFID 102
FT /note="Interchain (with C-102)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 373 AA; 41602 MW; EDC854FC0DF0C16E CRC64;
MAPTVKKRTS QNQGLSPQKS QNSVVVGGIQ VLDVRTGPDS ITQIEAFLNP RMGKPVDSDF
YGFSDNITVS ADYTQDMPRI KELPCYSMAK ISLPMLNEDM TCDTILMWEA ISCKTEVVGV
SSLTNCHSAV KRLYDNEGAG FPVQGLNFHF FSVGGEALDL QWLWKNYRCN YPAGVAALQA
APKAAQVLDP KLKAKLTADG KFPIEAWSPD PAKNENTRYF GTYTGGLQTP PVLQITNTTT
TILLNENGVG PLCKGDGLYL ASADIVGFRT QQNNKMHLRG LPRYFSIHLR KGCANPYPVS
SLLNTFSSEM MPLNSWMLQV EEVRIYDGVE RLPGDPDMIR YRIIWPGRLL SLIFPAMRHK
HLYFFVMQAF IVL
