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VL2_HPV11
ID   VL2_HPV11               Reviewed;         455 AA.
AC   P04013;
DT   23-OCT-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-1986, sequence version 1.
DT   23-FEB-2022, entry version 92.
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 11.
OC   Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC   Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC   Alphapapillomavirus.
OX   NCBI_TaxID=10580;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3008427; DOI=10.1016/0042-6822(86)90110-8;
RA   Dartmann K., Schwarz E., Gissmann L., zur Hausen H.;
RT   "The nucleotide sequence and genome organization of human papilloma virus
RT   type 11.";
RL   Virology 151:124-130(1986).
RN   [2]
RP   FUNCTION, AND INTERACTION WITH IMPORTINS KPNB1; KPNB2 AND KPNB3.
RX   PubMed=16873281; DOI=10.1128/jvi.00776-06;
RA   Bordeaux J., Forte S., Harding E., Darshan M.S., Klucevsek K., Moroianu J.;
RT   "The l2 minor capsid protein of low-risk human papillomavirus type 11
RT   interacts with host nuclear import receptors and viral DNA.";
RL   J. Virol. 80:8259-8262(2006).
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; M14119; AAA46934.1; -; Genomic_DNA.
DR   PIR; A03648; P2WL11.
DR   MINT; P04013; -.
DR   Proteomes; UP000008222; 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; 2.
PE   1: Evidence at protein level;
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..455
FT                   /note="Minor capsid protein L2"
FT                   /id="PRO_0000133578"
FT   MOTIF           1..11
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04003"
FT   MOTIF           438..446
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04003"
FT   DISULFID        20..26
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04003"
SQ   SEQUENCE   455 AA;  49096 MW;  905CAB7597227D5C CRC64;
     MKPRARRRKR ASATQLYQTC KATGTCPPDV IPKVEHTTIA DQILKWGSLG VFFGGLGIGT
     GAGSGGRAGY IPLGSSPKPA ITGGPAARPP VLVEPVAPSD PSIVSLIEES AIINAGAPEV
     VPPTQGGFTI TSSESTTPAI LDVSVTNHTT TSVFQNPLFT EPSVIQPQPP VEASGHILIS
     APTITSQHVE DIPLDTFVVS SSDSGPTSST PLPRAFPRPR VGLYSRALQQ VQVTDPAFLS
     TPQRLVTYDN PVYEGEDVSL QFTHESIHNA PDEAFMDIIR LHRPAITSRR GLVRFSRIGQ
     RGSMYTRSGQ HIGARIHYFQ DISPVTQAAE EIELHPLVAA ENDTFDIYAE PFDPIPDPVQ
     HSVTQSYLTS TPNTLSQSWG NTTVPLSIPS DWFVQSGPDI TFPTASMGTP FSPVTPALPT
     GPVFITGSDF YLHPTWYFAR RRRKRIPLFF TDVAA
 
 
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