VL2_BPV1
ID VL2_BPV1 Reviewed; 469 AA.
AC P03109;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 02-JUN-2021, entry version 90.
DE RecName: Full=Minor capsid protein L2 {ECO:0000255|HAMAP-Rule:MF_04003};
GN Name=L2 {ECO:0000255|HAMAP-Rule:MF_04003};
OS Bovine papillomavirus type 1.
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC Deltapapillomavirus.
OX NCBI_TaxID=337052;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6289124; DOI=10.1038/299529a0;
RA Chen E.Y., Howley P.M., Levinson A.D., Seeburg P.H.;
RT "The primary structure and genetic organization of the bovine
RT papillomavirus type 1 genome.";
RL Nature 299:529-534(1982).
CC -!- FUNCTION: Minor protein of the capsid that localizes along the inner
CC surface of the virion, within the central cavities beneath the L1
CC pentamers. Plays a role in capsid stabilization through interaction
CC with the major capsid protein L1. Once the virion enters the host cell,
CC L2 escorts the genomic DNA into the nucleus by promoting escape from
CC the endosomal compartments and traffic through the host Golgi network.
CC Mechanistically, the C-terminus of L2 possesses a cell-penetrating
CC peptide that protudes from the host endosome, interacts with host
CC cytoplasmic retromer cargo and thereby mediates the capsid delivery to
CC the host trans-Golgi network. Plays a role through its interaction with
CC host dynein in the intracellular microtubule-dependent transport of
CC viral capsid toward the nucleus. Mediates the viral genome import into
CC the nucleus through binding to host importins. Once within the nucleus,
CC L2 localizes viral genomes to host PML bodies in order to activate
CC early gene expression for establishment of infection. Later on,
CC promotes late gene expression by interacting with the viral E2 protein
CC and by inhibiting its transcriptional activation functions. During
CC virion assembly, encapsidates the genome by direct interaction with the
CC viral DNA. {ECO:0000255|HAMAP-Rule:MF_04003}.
CC -!- SUBUNIT: Interacts with major capsid protein L1. Interacts with E2;
CC this interaction inhibits E2 transcriptional activity but not the DNA
CC replication function E2. Interacts with host GADD45GIP1. Interacts with
CC host HSPA8; this interaction is required for L2 nuclear translocation.
CC Interacts with host importins KPNB2 and KPNB3. Forms a complex with
CC importin alpha2-beta1 heterodimers via interaction with the importin
CC alpha2 adapter. Interacts with host DYNLT1; this interaction is
CC essential for virus intracellular transport during entry. Interacts
CC (via C-terminus) with host retromer subunits VPS35 AND VPS29.
CC {ECO:0000255|HAMAP-Rule:MF_04003}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04003}. Host
CC nucleus {ECO:0000255|HAMAP-Rule:MF_04003}. Host early endosome
CC {ECO:0000255|HAMAP-Rule:MF_04003}. Host Golgi apparatus
CC {ECO:0000255|HAMAP-Rule:MF_04003}.
CC -!- PTM: Highly phosphorylated. {ECO:0000255|HAMAP-Rule:MF_04003}.
CC -!- SIMILARITY: Belongs to the papillomaviridae L2 protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04003}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X02346; CAB57284.1; -; Genomic_DNA.
DR PIR; A03653; P2WLB.
DR RefSeq; NP_056743.1; NC_001522.1.
DR GeneID; 1489023; -.
DR KEGG; vg:1489023; -.
DR Proteomes; UP000006567; Genome.
DR GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IDA:AgBase.
DR GO; GO:0044177; C:host cell Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0044185; C:host cell late endosome membrane; IDA:AgBase.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0019028; C:viral capsid; IDA:AgBase.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000149; F:SNARE binding; IPI:AgBase.
DR GO; GO:0005198; F:structural molecule activity; IEA:UniProtKB-UniRule.
DR GO; GO:0075521; P:microtubule-dependent intracellular transport of viral material towards nucleus; IEA:UniProtKB-UniRule.
DR GO; GO:0044418; P:translocation of DNA into host; TAS:AgBase.
DR GO; GO:0019073; P:viral DNA genome packaging; TAS:AgBase.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0075732; P:viral penetration into host nucleus; IEA:UniProtKB-KW.
DR HAMAP; MF_04003; PPV_L2; 1.
DR InterPro; IPR000784; Late_L2.
DR Pfam; PF00513; Late_protein_L2; 2.
PE 3: Inferred from homology;
KW Capsid protein; Cytoplasmic inwards viral transport; Disulfide bond;
KW DNA-binding; Host endosome; Host Golgi apparatus; Host nucleus;
KW Host-virus interaction; Late protein; Microtubular inwards viral transport;
KW Phosphoprotein; Reference proteome; Viral penetration into host nucleus;
KW Virion; Virus entry into host cell.
FT CHAIN 1..469
FT /note="Minor capsid protein L2"
FT /id="PRO_0000133560"
FT REGION 401..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1..10
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04003"
FT MOTIF 461..468
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04003"
FT DISULFID 19..25
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04003"
SQ SEQUENCE 469 AA; 50015 MW; F872094E267296FF CRC64;
MSARKRVKRA SAYDLYRTCK QAGTCPPDVI PKVEGDTIAD KILKFGGLAI YLGGLGIGTW
STGRVAAGGS PRYTPLRTAG STSSLASIGS RAVTAGTRPS IGAGIPLDTL ETLGALRPGV
YEDTVLPEAP AIVTPDAVPA DSGLDALSIG TDSSTETLIT LLEPEGPEDI AVLELQPLDR
PTWQVSNAVH QSSAYHAPLQ LQSSIAETSG LENIFVGGSG LGDTGGENIE LTYFGSPRTS
TPRSIASKSR GILNWFSKRY YTQVPTEDPE VFSSQTFANP LYEAEPAVLK GPSGRVGLSQ
VYKPDTLTTR SGTEVGPQLH VRYSLSTIHE DVEAIPYTVD ENTQGLAFVP LHEEQAGFEE
IELDDFSETH RLLPQNTSST PVGSGVRRSL IPTQEFSATR PTGVVTYGSP DTYSASPVTD
PDSTSPSLVI DDTTTTPIII IDGHTVDLYS SNYTLHPSLL RKRKKRKHA
