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 08-NOV-2023, entry version 79. 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; OC Erythroparvovirus primate1. 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}. 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; 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; Segment. 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; Parvovirus coat protein VP1/VP2; 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; ssDNA viruses; 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 //