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VL2_HPV1
ID   VL2_HPV1                Reviewed;         507 AA.
AC   P03105;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   23-FEB-2022, entry version 101.
DE   RecName: Full=Minor capsid protein L2 {ECO:0000255|HAMAP-Rule:MF_04003};
GN   Name=L2 {ECO:0000255|HAMAP-Rule:MF_04003};
OS   Human papillomavirus type 1 (Human papillomavirus type 1a).
OC   Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC   Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC   Mupapillomavirus.
OX   NCBI_TaxID=10583;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6325156; DOI=10.1002/j.1460-2075.1982.tb01152.x;
RA   Danos O., Katinka M., Yaniv M.;
RT   "Human papillomavirus 1a complete DNA sequence: a novel type of genome
RT   organization among papovaviridae.";
RL   EMBO J. 1:231-236(1982).
RN   [2]
RP   SEQUENCE REVISION.
RA   Danos O.;
RL   Submitted (JAN-1985) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; V01116; CAA24317.1; -; Genomic_DNA.
DR   PIR; A03646; P2WL.
DR   RefSeq; NP_040308.1; NC_001356.1.
DR   MINT; P03105; -.
DR   PRIDE; P03105; -.
DR   GeneID; 1489172; -.
DR   KEGG; vg:1489172; -.
DR   Proteomes; UP000006372; Genome.
DR   GO; GO:0044174; C:host cell endosome; IEA:UniProtKB-KW.
DR   GO; GO:0044177; C:host cell Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0019028; C:viral capsid; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
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: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; 1.
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..507
FT                   /note="Minor capsid protein L2"
FT                   /id="PRO_0000133566"
FT   MOTIF           1..9
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04003"
FT   MOTIF           500..506
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04003"
FT   DISULFID        18..24
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04003"
SQ   SEQUENCE   507 AA;  55330 MW;  905CBA5C33403596 CRC64;
     MYRLRRKRAA PKDIYPSCKI SNTCPPDIQN KIEHTTIADK ILQYGSLGVF LGGLGIGTAR
     GSGGRIGYTP LGEGGGVRVA TRPTPVRPTI PVETVGPSEI FPIDVVDPTG PAVIPLQDLG
     RDFPIPTVQV IAEIHPISDI PNIVASSTNE GESAILDVLR GNATIRTVSR TQYNNPSFTV
     ASTSNISAGE ASTSDIVFVS NGSGDRVVGE DIPLVELNLG LETDTSSVVQ ETAFSSSTPI
     AERPSFRPSR FYNRRLYEQV QVQDPRFVEQ PQSMVTFDNP AFEPELDEVS IIFQRDLDAL
     AQTPVPEFRD VVYLSKPTFS REPGGRLRVS RLGKSSTIRT RLGTAIGART HFFYDLSSIA
     PEDSIELLPL GEHSQTTVIS SNLGDTAFIQ GETAEDDLEV ISLETPQLYS EEELLDTNES
     VGENLQLTIT NSEGEVSILD LTQSRVRPPF GTEDTSLHVY YPNSSKGTPI INPEESFTPL
     VIIALNNSTG DFELHPSLRK RRKRAYV
 
 
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