CAPSD_PAVHV
ID CAPSD_PAVHV Reviewed; 781 AA.
AC Q9PZT0; Q90201; Q9PZS9;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Minor capsid protein VP1;
DE EC=3.1.1.4 {ECO:0000269|PubMed:11702787, ECO:0000269|PubMed:23596524};
DE AltName: Full=Coat protein VP1;
GN Name=vp;
OS Human parvovirus B19 (strain HV) (HPV B19).
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Quintoviricetes;
OC Piccovirales; Parvoviridae; Parvovirinae; Erythroparvovirus.
OX NCBI_TaxID=648237;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Gallinella G., Venturoli S.;
RT "B19 genome sequence and structure analysis.";
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM MAJOR CAPSID PROTEIN VP2).
RX PubMed=8922470; DOI=10.1099/0022-1317-77-11-2767;
RA Erdman D.D., Durigon E.L., Wang Q.Y., Anderson L.J.;
RT "Genetic diversity of human parvovirus B19: sequence analysis of the
RT VP1/VP2 gene from multiple isolates.";
RL J. Gen. Virol. 77:2767-2774(1996).
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=1376332; DOI=10.1172/jci115812;
RA Rosenfeld S.J., Yoshimoto K., Kajigaya S., Anderson S., Young N.S.,
RA Field A., Warrener P., Bansal G., Collett M.S.;
RT "Unique region of the minor capsid protein of human parvovirus B19 is
RT exposed on the virion surface.";
RL J. Clin. Invest. 89:2023-2029(1992).
RN [4]
RP FUNCTION.
RX PubMed=8211117; DOI=10.1126/science.8211117;
RA Brown K.E., Anderson S.M., Young N.S.;
RT "Erythrocyte P antigen: cellular receptor for B19 parvovirus.";
RL Science 262:114-117(1993).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=7544049; DOI=10.1006/viro.1995.1418;
RA Kawase M., Momoeda M., Young N.S., Kajigaya S.;
RT "Most of the VP1 unique region of B19 parvovirus is on the capsid
RT surface.";
RL Virology 211:359-366(1995).
RN [6]
RP CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=11702787; DOI=10.1016/s1534-5807(01)00031-4;
RA Zadori Z., Szelei J., Lacoste M.C., Li Y., Gariepy S., Raymond P.,
RA Allaire M., Nabi I.R., Tijssen P.;
RT "A viral phospholipase A2 is required for parvovirus infectivity.";
RL Dev. Cell 1:291-302(2001).
RN [7]
RP FUNCTION.
RX PubMed=12907437; DOI=10.1182/blood-2003-05-1522;
RA Weigel-Kelley K.A., Yoder M.C., Srivastava A.;
RT "Alpha5beta1 integrin as a cellular coreceptor for human parvovirus B19:
RT requirement of functional activation of beta1 integrin for viral entry.";
RL Blood 102:3927-3933(2003).
RN [8]
RP SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-720; PRO-723; ARG-724; LYS-725;
RP ARG-729 AND 723-PRO--LYS-725, FUNCTION, AND NUCLEAR LOCALIZATION SIGNAL.
RX PubMed=12620794; DOI=10.1016/s0042-6822(02)00047-8;
RA Pillet S., Annan Z., Fichelson S., Morinet F.;
RT "Identification of a nonconventional motif necessary for the nuclear import
RT of the human parvovirus B19 major capsid protein (VP2).";
RL Virology 306:25-32(2003).
RN [9]
RP FUNCTION.
RX PubMed=16076874; DOI=10.1182/blood-2005-02-0536;
RA Munakata Y., Saito-Ito T., Kumura-Ishii K., Huang J., Kodera T., Ishii T.,
RA Hirabayashi Y., Koyanagi Y., Sasaki T.;
RT "Ku80 autoantigen as a cellular coreceptor for human parvovirus B19
RT infection.";
RL Blood 106:3449-3456(2005).
RN [10]
RP FUNCTION, AND DOMAIN.
RX PubMed=17020940; DOI=10.1128/jvi.01435-06;
RA Ros C., Gerber M., Kempf C.;
RT "Conformational changes in the VP1-unique region of native human parvovirus
RT B19 lead to exposure of internal sequences that play a role in virus
RT neutralization and infectivity.";
RL J. Virol. 80:12017-12024(2006).
RN [11]
RP CATALYTIC ACTIVITY, AND MUTAGENESIS OF GLU-176.
RX PubMed=18252260; DOI=10.1016/j.virol.2008.01.002;
RA Filippone C., Zhi N., Wong S., Lu J., Kajigaya S., Gallinella G.,
RA Kakkola L., Soederlund-Venermo M., Young N.S., Brown K.E.;
RT "VP1u phospholipase activity is critical for infectivity of full-length
RT parvovirus B19 genomic clones.";
RL Virology 374:444-452(2008).
RN [12]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=22718826; DOI=10.1128/jvi.01004-12;
RA Quattrocchi S., Ruprecht N., Bonsch C., Bieli S., Zurcher C., Boller K.,
RA Kempf C., Ros C.;
RT "Characterization of the early steps of human parvovirus B19 infection.";
RL J. Virol. 86:9274-9284(2012).
RN [13]
RP CATALYTIC ACTIVITY, AND MUTAGENESIS OF TYR-130; GLY-132; PRO-133; HIS-153;
RP ASP-154; TYR-157; LYS-162; TYR-168; ASP-175; ASP-195 AND ALA-207.
RX PubMed=23596524; DOI=10.1371/journal.pone.0061440;
RA Deng X., Dong Y., Yi Q., Huang Y., Zhao D., Yang Y., Tijssen P., Qiu J.,
RA Liu K., Li Y.;
RT "The determinants for the enzyme activity of human parvovirus B19
RT phospholipase A2 (PLA2) and its influence on cultured cells.";
RL PLoS ONE 8:E61440-E61440(2013).
RN [14]
RP DOMAIN, FUNCTION, AND MUTAGENESIS OF PHE-15; ALA-16; VAL-19; TYR-20;
RP GLN-21; GLN-22; PHE-23; PHE-26; TYR-27 AND LYS-29.
RX PubMed=26927158; DOI=10.3390/v8030061;
RA Leisi R., Di Tommaso C., Kempf C., Ros C.;
RT "The Receptor-Binding Domain in the VP1u Region of Parvovirus B19.";
RL Viruses 8:61-61(2016).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) OF 228-781, DOMAIN, AND SUBUNIT.
RX PubMed=15289612; DOI=10.1073/pnas.0402992101;
RA Kaufmann B., Simpson A.A., Rossmann M.G.;
RT "The structure of human parvovirus B19.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:11628-11633(2004).
CC -!- FUNCTION: Capsid protein self-assembles to form an icosahedral capsid
CC with a T=1 symmetry, about 20 nm in diameter, and consisting of 60
CC copies of two size variants of the capsid proteins, VP1 and VP2, which
CC differ by the presence of an N-terminal extension in the minor protein
CC VP1 (PubMed:15289612). The capsid encapsulates the genomic ssDNA
CC (Probable). Binds to erythroid progenitor cells expressing high levels
CC of P antigen and uses host ITGA5-ITGB1 and XRCC5/Ku80 autoantigen as
CC coreceptors on the cell surface to provide virion attachment to target
CC cell (PubMed:12907437, PubMed:8211117, PubMed:16076874). This
CC attachment induces virion internalization predominantly through
CC clathrin-dependent endocytosis (PubMed:22718826). Binding to the host
CC receptors also induces capsid rearrangements leading to surface
CC exposure of VP1 N-terminus, specifically its phospholipase A2-like
CC region (PubMed:17020940). The additional N-terminal region of isoform
CC Minor capsid protein VP1, called VP1u, may serve as a lipolytic enzyme
CC to breach the endosomal membrane during entry into host cell and might
CC contribute to virus transport to the nucleus (PubMed:11702787).
CC {ECO:0000269|PubMed:11702787, ECO:0000269|PubMed:12907437,
CC ECO:0000269|PubMed:15289612, ECO:0000269|PubMed:16076874,
CC ECO:0000269|PubMed:17020940, ECO:0000269|PubMed:22718826,
CC ECO:0000269|PubMed:8211117, ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-
CC glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4;
CC Evidence={ECO:0000269|PubMed:11702787, ECO:0000269|PubMed:23596524};
CC -!- SUBUNIT: [Isoform Minor capsid protein VP1]: Heteromultimer of isoform
CC Minor capsid protein VP1, isoform Minor capsid protein VP2 and isoform
CC Major capsid protein VP3 (PubMed:15289612).
CC {ECO:0000269|PubMed:15289612}.
CC -!- SUBUNIT: [Isoform Major capsid protein VP2]: Heteromultimer of isoform
CC Minor capsid protein VP1, isoform Minor capsid protein VP2 and isoform
CC Major capsid protein VP3 (PubMed:15289612). 20 fold more abundant than
CC the minor capsid protein VP1 (PubMed:15289612).
CC {ECO:0000269|PubMed:15289612}.
CC -!- SUBCELLULAR LOCATION: [Isoform Minor capsid protein VP1]: Virion
CC {ECO:0000269|PubMed:1376332, ECO:0000269|PubMed:7544049}. Host nucleus
CC {ECO:0000269|PubMed:12620794}. Host cytoplasm.
CC -!- SUBCELLULAR LOCATION: [Isoform Major capsid protein VP2]: Virion
CC {ECO:0000269|PubMed:15289612}. Host nucleus
CC {ECO:0000269|PubMed:12620794}. Host cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Minor capsid protein VP1;
CC IsoId=Q9PZT0-1; Sequence=Displayed;
CC Name=Major capsid protein VP2;
CC IsoId=Q9PZT0-2; Sequence=VSP_054247;
CC -!- DOMAIN: The N-terminus of Isoform Minor capsid protein VP1, VP1u,
CC contains a phospholipase A2-like region (PubMed:17020940). VP1u is
CC necessary and sufficient for host cell binding and internalization
CC (PubMed:26927158). {ECO:0000269|PubMed:17020940,
CC ECO:0000269|PubMed:26927158}.
CC -!- DOMAIN: A nuclear localization signal is present in the C-terminus and
CC can be recognized by cellular nuclear import molecules
CC (PubMed:15289612). After assembly, it is hidden because it is on the
CC inner capsid surface (PubMed:15289612). {ECO:0000269|PubMed:15289612,
CC ECO:0000303|PubMed:15289612}.
CC -!- MISCELLANEOUS: [Isoform Minor capsid protein VP1]: Minor splicing
CC isoform. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform Major capsid protein VP2]: Major splicing
CC isoform produced by deletion of the initiating AUG for VP1 and
CC downstream translation of VP2. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the parvoviridae capsid protein family.
CC {ECO:0000305}.
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DR EMBL; AF162273; AAD46614.1; -; Genomic_DNA.
DR EMBL; AF162273; AAD46615.1; -; Genomic_DNA.
DR EMBL; U53595; AAB47453.1; -; Genomic_DNA.
DR RefSeq; YP_004928148.1; NC_000883.2.
DR PDB; 1S58; X-ray; 3.50 A; A=1-554.
DR PDBsum; 1S58; -.
DR SMR; Q9PZT0; -.
DR ABCD; Q9PZT0; 2 sequenced antibodies.
DR GeneID; 11293627; -.
DR KEGG; vg:11293627; -.
DR Proteomes; UP000006624; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; IDA:UniProtKB.
DR GO; GO:0039615; C:T=1 icosahedral viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0019028; C:viral capsid; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004623; F:phospholipase A2 activity; IDA:UniProtKB.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IDA:UniProtKB.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0075521; P:microtubule-dependent intracellular transport of viral material towards nucleus; IEA:UniProtKB-KW.
DR GO; GO:0039665; P:permeabilization of host organelle membrane involved in viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0046813; P:receptor-mediated virion attachment to host cell; IDA:UniProtKB.
DR GO; GO:0099008; P:viral entry via permeabilization of inner membrane; IEA:UniProtKB-KW.
DR GO; GO:0075732; P:viral penetration into host nucleus; IDA:UniProtKB.
DR Gene3D; 2.170.30.10; -; 1.
DR InterPro; IPR016184; Capsid/spike_ssDNA_virus.
DR InterPro; IPR001403; Parvovirus_coat.
DR InterPro; IPR013607; Phospholipase_A2-like.
DR InterPro; IPR036952; VP1/VP2.
DR Pfam; PF00740; Parvo_coat; 1.
DR Pfam; PF08398; Phospholip_A2_4; 1.
DR SUPFAM; SSF88645; SSF88645; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Capsid protein;
KW Clathrin-mediated endocytosis of virus by host;
KW Cytoplasmic inwards viral transport; Host cytoplasm; Host nucleus;
KW Host-virus interaction; Hydrolase; Lipid degradation; Lipid metabolism;
KW Magnesium; Metal-binding; Microtubular inwards viral transport;
KW Reference proteome; T=1 icosahedral capsid protein;
KW Viral attachment to host cell; Viral penetration into host cytoplasm;
KW Viral penetration into host nucleus;
KW Viral penetration via permeabilization of host membrane; Virion;
KW Virus endocytosis by host; Virus entry into host cell.
FT CHAIN 1..781
FT /note="Minor capsid protein VP1"
FT /id="PRO_0000428714"
FT REGION 5..80
FT /note="Binding to the host cell receptor and
FT internalization"
FT /evidence="ECO:0000269|PubMed:26927158"
FT REGION 77..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 123..181
FT /note="Phospholipase A2-like"
FT /evidence="ECO:0000269|PubMed:11702787,
FT ECO:0000269|PubMed:18252260"
FT REGION 524..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 720..730
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:12620794,
FT ECO:0000303|PubMed:15289612"
FT COMPBIAS 77..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..557
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..227
FT /note="Missing (in isoform Major capsid protein VP2)"
FT /evidence="ECO:0000305"
FT /id="VSP_054247"
FT MUTAGEN 15
FT /note="F->C: 50% loss of virus internalization into the
FT host cell."
FT /evidence="ECO:0000269|PubMed:26927158"
FT MUTAGEN 15
FT /note="F->W: 70% loss of virus internalization into the
FT host cell."
FT /evidence="ECO:0000269|PubMed:26927158"
FT MUTAGEN 16
FT /note="A->S: Almost complete loss of virus internalization
FT into the host cell."
FT /evidence="ECO:0000269|PubMed:26927158"
FT MUTAGEN 19
FT /note="V->A: 70% loss of virus internalization into the
FT host cell."
FT /evidence="ECO:0000269|PubMed:26927158"
FT MUTAGEN 19
FT /note="V->S: 70% loss of virus internalization into the
FT host cell."
FT /evidence="ECO:0000269|PubMed:26927158"
FT MUTAGEN 20
FT /note="Y->C: 70% loss of virus internalization into the
FT host cell."
FT /evidence="ECO:0000269|PubMed:26927158"
FT MUTAGEN 20
FT /note="Y->W: Almost complete loss of virus internalization
FT into the host cell."
FT /evidence="ECO:0000269|PubMed:26927158"
FT MUTAGEN 21
FT /note="Q->A: 80% loss of virus internalization into the
FT host cell."
FT /evidence="ECO:0000269|PubMed:26927158"
FT MUTAGEN 21
FT /note="Q->P: 50% loss of virus internalization into the
FT host cell."
FT /evidence="ECO:0000269|PubMed:26927158"
FT MUTAGEN 22
FT /note="Q->A: 30% loss of virus internalization into the
FT host cell."
FT /evidence="ECO:0000269|PubMed:26927158"
FT MUTAGEN 22
FT /note="Q->P: 10% loss of virus internalization into the
FT host cell."
FT /evidence="ECO:0000269|PubMed:26927158"
FT MUTAGEN 23
FT /note="F->S: 60% loss of virus internalization into the
FT host cell."
FT /evidence="ECO:0000269|PubMed:26927158"
FT MUTAGEN 26
FT /note="F->S: 70% loss of virus internalization into the
FT host cell."
FT /evidence="ECO:0000269|PubMed:26927158"
FT MUTAGEN 27
FT /note="Y->C: 30% loss of virus internalization into the
FT host cell."
FT /evidence="ECO:0000269|PubMed:26927158"
FT MUTAGEN 27
FT /note="Y->W: 70% loss of virus internalization into the
FT host cell."
FT /evidence="ECO:0000269|PubMed:26927158"
FT MUTAGEN 29
FT /note="K->A: Almost complete loss of virus internalization
FT into the host cell."
FT /evidence="ECO:0000269|PubMed:26927158"
FT MUTAGEN 130
FT /note="Y->A: Very low levels of phospholipase A2-like
FT activity."
FT /evidence="ECO:0000269|PubMed:23596524"
FT MUTAGEN 132
FT /note="G->A: Complete loss of phospholipase A2-like
FT activity."
FT /evidence="ECO:0000269|PubMed:23596524"
FT MUTAGEN 133
FT /note="P->R: No effect on phospholipase A2-like activity."
FT /evidence="ECO:0000269|PubMed:23596524"
FT MUTAGEN 153
FT /note="H->A: Very low levels of phospholipase A2-like
FT activity."
FT /evidence="ECO:0000269|PubMed:23596524"
FT MUTAGEN 154
FT /note="D->A: Complete loss of phospholipase A2-like
FT activity."
FT /evidence="ECO:0000269|PubMed:23596524"
FT MUTAGEN 157
FT /note="Y->F: Very low levels of phospholipase A2-like
FT activity."
FT /evidence="ECO:0000269|PubMed:23596524"
FT MUTAGEN 162
FT /note="K->R: Very low levels of phospholipase A2-like
FT activity."
FT /evidence="ECO:0000269|PubMed:23596524"
FT MUTAGEN 168
FT /note="Y->F: Complete loss of phospholipase A2-like
FT activity."
FT /evidence="ECO:0000269|PubMed:23596524"
FT MUTAGEN 175
FT /note="D->A: Very low levels of phospholipase A2-like
FT activity."
FT /evidence="ECO:0000269|PubMed:23596524"
FT MUTAGEN 176
FT /note="E->K: 80% loss of infectivity."
FT /evidence="ECO:0000269|PubMed:18252260"
FT MUTAGEN 195
FT /note="D->A: 10% increased phospholipase A2-like activity."
FT /evidence="ECO:0000269|PubMed:23596524"
FT MUTAGEN 207
FT /note="A->Y: No effect on phospholipase A2-like activity."
FT /evidence="ECO:0000269|PubMed:23596524"
FT MUTAGEN 720
FT /note="K->A: Host nucleocytoplasmic localization."
FT /evidence="ECO:0000269|PubMed:12620794"
FT MUTAGEN 723..725
FT /note="PRK->AAA: Host cytoplasmic localization."
FT /evidence="ECO:0000269|PubMed:12620794"
FT MUTAGEN 723
FT /note="P->A: Host nucleocytoplasmic localization."
FT /evidence="ECO:0000269|PubMed:12620794"
FT MUTAGEN 724
FT /note="R->A: Host nucleocytoplasmic localization."
FT /evidence="ECO:0000269|PubMed:12620794"
FT MUTAGEN 725
FT /note="K->A: Host nucleocytoplasmic localization."
FT /evidence="ECO:0000269|PubMed:12620794"
FT MUTAGEN 729
FT /note="R->A: Host nucleocytoplasmic localization."
FT /evidence="ECO:0000269|PubMed:12620794"
FT CONFLICT 377
FT /note="S -> C (in Ref. 2; AAB47453)"
FT /evidence="ECO:0000305"
FT CONFLICT 574
FT /note="P -> T (in Ref. 2; AAB47453)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 781 AA; 86020 MW; 225DF1EDC68B841F CRC64;
MSKESGKWWE SDDKFAKAVY QQFVEFYEKV TGTDLELIQI LKDHYNISLD NPLENPSSLF
DLVARIKNNL KNSPDLYSHH FQSHGQLSDH PHALSSSSSH AEPRGENAVL SSEDLHKPGQ
VSVQLPGTNY VGPGNELQAG PPQSAVDSAA RIHDFRYSQL AKLGINPYTH WTVADEELLK
NIKNETGFQA QVVKDYFTLK GAAAPVAHFQ GSLPEVPAYN ASEKYPSMTS VNSAEASTGA
GGGGSNPVKS MWSEGATFSA NSVTCTFSRQ FLIPYDPEHH YKVFSPAASS CHNASGKEAK
VCTISPIMGY STPWRYLDFN ALNLFFSPLE FQHLIENYGS IAPDALTVTI SEIAVKDVTD
KTGGGVQVTD STTGRLSMLV DHEYKYPYVL GQGQDTLAPE LPIWVYFPPQ YAYLTVGDVN
TQGISGDSKK LASEESAFYV LEHSSFQLLG TGGTATMSYK FPPVPPENLE GCSQHFYEMY
NPLYGSRLGV PDTLGGDPKF RSLTHEDHAI QPQNFMPGPL VNSVSTKEGD SSNTGAGKAL
TGLSTGTSQN TRISLRPGPV SQPYHHWDTD KYVPGINAIS HGQTTYGNAE DKEYQQGVGR
FPNEKEQLKQ LQGLNMHTYF PNKGTQQYTD QIERPLMVGS VWNRRALHYE SQLWSKIPNL
DDSFKTQFAA LGGWGLHQPP PQIFLKILPQ SGPIGGIKSM GITTLVQYAV GIMTVTMTFK
LGPRKATGRW NPQPGVYPPH AAGHLPYVLY DPTATDAKQH HRHGYEKPEE LWTAKSRVHP
L
