CAPSD_HBOC1
ID CAPSD_HBOC1 Reviewed; 671 AA.
AC Q3YPH4; Q3YPH3; U5XGX2;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 23-FEB-2022, entry version 47.
DE RecName: Full=Minor capsid protein VP1;
DE EC=3.1.1.4 {ECO:0000269|PubMed:17981142};
GN Name=VP1;
OS Primate bocaparvovirus 1 (strain Human bocavirus 1 type 1) (HBoV1) (Human
OS bocavirus type 1).
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Quintoviricetes;
OC Piccovirales; Parvoviridae; Parvovirinae; Bocaparvovirus;
OC Primate bocaparvovirus 1.
OX NCBI_TaxID=689403;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORMS MINOR CAPSID
RP PROTEIN VP1 AND MAJOR CAPSID PROTEIN VP3).
RC STRAIN=St2;
RX PubMed=16118271; DOI=10.1073/pnas.0504666102;
RA Allander T., Tammi M.T., Eriksson M., Bjerkner A., Tiveljung-Lindell A.,
RA Andersson B.;
RT "Cloning of a human parvovirus by molecular screening of respiratory tract
RT samples.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:12891-12896(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 122-671.
RA Ursic T., Petrovec M.;
RT "Human bocavirus infection in child with Bronchopulmonary dysplasia.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP DOMAIN, MUTAGENESIS OF PRO-21; HIS-41; ASP-42 AND ASP-63, AND CATALYTIC
RP ACTIVITY.
RX PubMed=17981142; DOI=10.1016/j.bbrc.2007.10.164;
RA Qu X.W., Liu W.P., Qi Z.Y., Duan Z.J., Zheng L.S., Kuang Z.Z., Zhang W.J.,
RA Hou Y.D.;
RT "Phospholipase A2-like activity of human bocavirus VP1 unique region.";
RL Biochem. Biophys. Res. Commun. 365:158-163(2008).
RN [4]
RP SUBUNIT, ALTERNATIVE INITIATION, AND SUBCELLULAR LOCATION.
RX PubMed=19244471; DOI=10.1128/cvi.00470-08;
RA Cecchini S., Negrete A., Virag T., Graham B.S., Cohen J.I., Kotin R.M.;
RT "Evidence of prior exposure to human bocavirus as determined by a
RT retrospective serological study of 404 serum samples from adults in the
RT United States.";
RL Clin. Vaccine Immunol. 16:597-604(2009).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=20457462; DOI=10.1016/j.virol.2010.04.014;
RA Chen A.Y., Cheng F., Lou S., Luo Y., Liu Z., Delwart E., Pintel D., Qiu J.;
RT "Characterization of the gene expression profile of human bocavirus.";
RL Virology 403:145-154(2010).
RN [6]
RP DOMAIN.
RX PubMed=25268969; DOI=10.1371/journal.pone.0107970;
RA Chiu C.C., Shi Y.F., Yang J.J., Hsiao Y.C., Tzang B.S., Hsu T.C.;
RT "Effects of human Parvovirus B19 and Bocavirus VP1 unique region on tight
RT junction of human airway epithelial A549 cells.";
RL PLoS ONE 9:E107970-E107970(2014).
RN [7]
RP ALTERNATIVE INITIATION.
RX PubMed=26912614; DOI=10.1128/jvi.02964-15;
RA Zou W., Cheng F., Shen W., Engelhardt J.F., Yan Z., Qiu J.;
RT "Nonstructural Protein NP1 of Human Bocavirus 1 Plays a Critical Role in
RT the Expression of Viral Capsid Proteins.";
RL J. Virol. 90:4658-4669(2016).
RN [8]
RP STRUCTURE BY ELECTRON MICROSCOPY (2.90 ANGSTROMS) OF 130-671, FUNCTION,
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=28331084; DOI=10.1128/jvi.00261-17;
RA Mietzsch M., Kailasan S., Garrison J., Ilyas M., Chipman P., Kantola K.,
RA Janssen M.E., Spear J., Sousa D., McKenna R., Brown K.,
RA Soderlund-Venermo M., Baker T., Agbandje-McKenna M.;
RT "Structural Insights into Human Bocaparvoviruses.";
RL J. Virol. 91:0-0(2017).
CC -!- FUNCTION: Capsid proteins self-assembles to form an icosahedral capsid
CC with a T=1 symmetry, about 26 nm in diameter, and consisting of 60
CC copies of three size variants of the capsid proteins, VP1, and VP3,
CC which differ by the presence of an N-terminal extension in the minor
CC protein VP1 (Probable). The capsid has a channel at the 5-fold axis and
CC there are densities extending the 5-fold axis into the interior of the
CC capsid (PubMed:28331084). The capsid encapsulates the genomic ssDNA
CC (Probable). Binding to the host receptors also induces capsid
CC rearrangements leading to surface exposure of VP1 N-terminus,
CC specifically its phospholipase A2-like region. The additional N-
CC terminal region of isoform Minor capsid protein VP1, called VP1u, may
CC serve as a lipolytic enzyme to breach the endosomal membrane during
CC entry into host cell and might contribute to virus transport to the
CC nucleus (By similarity). {ECO:0000250|UniProtKB:Q9PZT0,
CC ECO:0000269|PubMed:28331084, ECO:0000305, ECO:0000305|PubMed:28331084}.
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:17981142};
CC -!- SUBUNIT: Heteromultimer of isoform Minor capsid protein VP1, isoform
CC Minor capsid protein VP2 and isoform Major capsid protein VP3
CC (PubMed:19244471). Isoform Major capsid protein VP3 is a homomultimer
CC (PubMed:28331084). Isoform Major capsid protein VP3 is 10 fold more
CC abundant than the minor capsid proteins VP1 and VP2 (PubMed:19244471).
CC {ECO:0000269|PubMed:19244471, ECO:0000269|PubMed:28331084}.
CC -!- SUBCELLULAR LOCATION: [Isoform Minor capsid protein VP1]: Virion
CC {ECO:0000269|PubMed:19244471}. Host nucleus
CC {ECO:0000269|PubMed:20457462}. Host cytoplasm
CC {ECO:0000269|PubMed:20457462}. Note=Slightly detected in the cytoplasm,
CC mainly seen in the nucleus. {ECO:0000269|PubMed:20457462}.
CC -!- SUBCELLULAR LOCATION: [Isoform Minor capsid protein VP2]: Virion
CC {ECO:0000269|PubMed:19244471}.
CC -!- SUBCELLULAR LOCATION: [Isoform Major capsid protein VP3]: Virion
CC {ECO:0000269|PubMed:19244471, ECO:0000269|PubMed:28331084}. Host
CC nucleus {ECO:0000269|PubMed:20457462}. Host cytoplasm
CC {ECO:0000269|PubMed:20457462}. Note=Slightly detected in the cytoplasm,
CC mainly seen in the nucleus. {ECO:0000269|PubMed:20457462}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=3;
CC Comment=The VP-encoding mRNA generates the three capsid proteins.
CC Minor capsid protein VP1 and Major capsid protein VP3 initiate at
CC canonical initiation site, whereas Minor capsid protein VP2 initiates
CC at a GCT codon (PubMed:19244471, PubMed:26912614).
CC {ECO:0000269|PubMed:19244471, ECO:0000269|PubMed:26912614};
CC Name=Minor capsid protein VP1;
CC IsoId=Q3YPH4-1; Sequence=Displayed;
CC Name=Minor capsid protein VP2;
CC IsoId=Q3YPH4-2; Sequence=VSP_059856, VSP_059863;
CC Name=Major capsid protein VP3;
CC IsoId=Q3YPH4-3; Sequence=VSP_059855;
CC -!- DOMAIN: The N-terminus of Isoform Minor capsid protein VP1, VP1u,
CC contains a phospholipase A2-like region (By similarity). VP1u may play
CC a role in the disruption of host tight junctions in the airway tract
CC (PubMed:25268969). {ECO:0000250|UniProtKB:Q9PZT0,
CC ECO:0000269|PubMed:25268969}.
CC -!- DOMAIN: A nuclear localization signal is present in the C-terminus and
CC can be recognized by cellular nuclear import molecules. After assembly,
CC it is hidden because it is on the inner capsid surface.
CC {ECO:0000250|UniProtKB:Q9PZT0}.
CC -!- SIMILARITY: Belongs to the parvoviridae capsid protein family.
CC {ECO:0000305}.
CC -!- CAUTION: Isoform major capsid protein VP3 has former been designated as
CC VP2. {ECO:0000305}.
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DR EMBL; DQ000496; AAY45702.1; -; Genomic_DNA.
DR EMBL; DQ000496; AAY45703.1; -; Genomic_DNA.
DR EMBL; KF385975; AGZ61939.1; -; Genomic_DNA.
DR RefSeq; YP_338088.1; NC_007455.1.
DR RefSeq; YP_338089.1; NC_007455.1.
DR PDB; 5URF; EM; 2.90 A; 1/2/3/4/5/6/7/8/A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V=9-550.
DR PDBsum; 5URF; -.
DR SMR; Q3YPH4; -.
DR DNASU; 3711587; -.
DR DNASU; 3711588; -.
DR GeneID; 3711587; -.
DR GeneID; 3711588; -.
DR KEGG; vg:3711587; -.
DR KEGG; vg:3711588; -.
DR Proteomes; UP000140113; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
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:0004623; F:phospholipase A2 activity; IEA:UniProtKB-EC.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
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 initiation; Capsid protein; Host cytoplasm;
KW Host nucleus; Hydrolase; Lipid degradation; Lipid metabolism;
KW Reference proteome; T=1 icosahedral capsid protein; Virion.
FT CHAIN 1..671
FT /note="Minor capsid protein VP1"
FT /id="PRO_0000445381"
FT REGION 11..66
FT /note="Phospholipase A2-like"
FT /evidence="ECO:0000269|PubMed:17981142"
FT REGION 106..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 614..625
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q9PZT0"
FT COMPBIAS 128..156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..129
FT /note="Missing (in isoform Major capsid protein VP3)"
FT /evidence="ECO:0000269|PubMed:26912614"
FT /id="VSP_059855"
FT VAR_SEQ 1..90
FT /note="Missing (in isoform Minor capsid protein VP2)"
FT /evidence="ECO:0000269|PubMed:26912614"
FT /id="VSP_059856"
FT VAR_SEQ 91
FT /note="V -> M (in isoform Minor capsid protein VP2)"
FT /id="VSP_059863"
FT MUTAGEN 21
FT /note="P->R: Almost complete loss of phospholipase A2-like
FT activity."
FT /evidence="ECO:0000269|PubMed:17981142"
FT MUTAGEN 41
FT /note="H->A: Almost complete loss of phospholipase A2-like
FT activity."
FT /evidence="ECO:0000269|PubMed:17981142"
FT MUTAGEN 42
FT /note="D->N: Almost complete loss of phospholipase A2-like
FT activity."
FT /evidence="ECO:0000269|PubMed:17981142"
FT MUTAGEN 63
FT /note="D->A: Almost complete loss of phospholipase A2-like
FT activity."
FT /evidence="ECO:0000269|PubMed:17981142"
SQ SEQUENCE 671 AA; 75085 MW; DB8766E0DE37DE12 CRC64;
MPPIKRQPRG WVLPGYRYLG PFNPLDNGEP VNNADRAAQL HDHAYSELIK SGKNPYLYFN
KADEKFIDDL KDDWSIGGII GSSFFKIKRA VAPALGNKER AQKRHFYFAN SNKGAKKTKK
SEPKPGTSKM SDTDIQDQQP DTVDAPQNTS GGGTGSIGGG KGSGVGISTG GWVGGSHFSD
KYVVTKNTRQ FITTIQNGHL YKTEAIETTN QSGKSQRCVT TPWTYFNFNQ YSCHFSPQDW
QRLTNEYKRF RPKAMQVKIY NLQIKQILSN GADTTYNNDL TAGVHIFCDG EHAYPNASHP
WDEDVMPDLP YKTWKLFQYG YIPIENELAD LDGNAAGGNA TEKALLYQMP FFLLENSDHQ
VLRTGESTEF TFNFDCEWVN NERAYIPPGL MFNPKVPTRR VQYIRQNGST AASTGRIQPY
SKPTSWMTGP GLLSAQRVGP QSSDTAPFMV CTNPEGTHIN TGAAGFGSGF DPPNGCLAPT
NLEYKLQWYQ TPEGTGNNGN IIANPSLSML RDQLLYKGNQ TTYNLVGDIW MFPNQVWDRF
PITRENPIWC KKPRADKHTI MDPFDGSIAM DHPPGTIFIK MAKIPVPTAS NADSYLNIYC
TGQVSCEIVW EVERYATKNW RPERRHTALG MSLGGESNYT PTYHVDPTGA YIQPTSYDQC
MPVKTNINKV L
