VL2_COPV6
ID VL2_COPV6 Reviewed; 513 AA.
AC Q89892;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Minor capsid protein L2 {ECO:0000255|HAMAP-Rule:MF_04003};
GN Name=L2 {ECO:0000255|HAMAP-Rule:MF_04003};
OS Canine oral papillomavirus (strain Y62) (COPV).
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC Lambdapapillomavirus.
OX NCBI_TaxID=766192;
OH NCBI_TaxID=9615; Canis lupus familiaris (Dog) (Canis familiaris).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8091677; DOI=10.1006/viro.1994.1552;
RA Delius H., van Ranst M.A., Jenson A.B., zur Hausen H., Sundberg J.P.;
RT "Canine oral papillomavirus genomic sequence: a unique 1.5-kb intervening
RT sequence between the E2 and L2 open reading frames.";
RL Virology 204:447-452(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Isegawa N., Ohta M., Shirasawa H., Tokita H., Simizu B., Yamaura A.;
RT "Nucleotide sequence of a canine oral papillomavirus containing a long
RT noncoding region.";
RL Int. J. Oncol. 7:155-159(1995).
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; D55633; BAA09502.1; -; Genomic_DNA.
DR EMBL; L22695; AAA61749.1; -; Genomic_DNA.
DR RefSeq; NP_056818.1; NC_001619.1.
DR PRIDE; Q89892; -.
DR GeneID; 1497246; -.
DR KEGG; vg:1497246; -.
DR Proteomes; UP000008788; Genome.
DR Proteomes; UP000097271; 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..513
FT /note="Minor capsid protein L2"
FT /id="PRO_0000133640"
FT REGION 229..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1..9
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04003"
FT MOTIF 504..509
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04003"
FT COMPBIAS 236..262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 18..24
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04003"
SQ SEQUENCE 513 AA; 55883 MW; 36A385C64DB7B545 CRC64;
MALIRKRRAA PQDIYPACKV SNTCPADILN KMEQNTLADK ILKYGSAGVF LGGLGISTGK
GVGGRTGYIP LGGTESGVGV GTRVTTIRPT VPISSVGSPD FIPVDAVDPL GPAVIPPERF
PIAVEDPFTL PPPRFPTAVE EDVIELQPIP GPSSEIPLAG PKITTDAQPA ILEVIPETRP
PKVITRHQYS NPAFEVSITS NSGAGESSAS DHVLVEGFSG GHSIGEHIPL QDLAPSRPSF
SETIEDETAF SSSTPKQGSR SERPKSYYNR RRYQQVQVTD PVFISRPRSL VTFDNPAFDE
SVDLIFERDV AEITAAPHAD FTDITKLTKP AYHRGPSGHV RVSRLGHRAN IKTRSGLTIG
PQSHFYYDVS SIDPAESFEL QALGNVSSAE QTGEAVISSG TGDFEIISLE DSILESYNDE
DLIDVFEDVA RDLHLLVGER RQQPIQVQRY IKPFSFVNEG VHIIHPGSES DFWLPPVTPD
STPAIVIDIL DSSADYYLHP SLIKKRKRKH FFF
