CAPSD_HBOC3
ID CAPSD_HBOC3 Reviewed; 668 AA.
AC C1IWT2; C1IWT3;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 23-FEB-2022, entry version 37.
DE RecName: Full=Minor capsid protein VP1;
DE EC=3.1.1.4 {ECO:0000250|UniProtKB:Q3YPH4};
GN Name=VP1;
OS Human bocavirus 3 (HBoV3) (Adelavirus W471).
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Quintoviricetes;
OC Piccovirales; Parvoviridae; Parvovirinae; Bocaparvovirus;
OC Primate bocaparvovirus 1.
OX NCBI_TaxID=638313;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W471, and W855;
RA Arthur J.L., Higgins G.D., Davidson G.P., Givney R.C., Ratcliff R.M.;
RT "A Novel Bocavirus Associated with Acute Gastroenteritis in Australian
RT Children.";
RL PLoS Pathog. 5:E1000391-E1000391(2009).
RN [2]
RP STRUCTURE BY ELECTRON MICROSCOPY (2.80 ANGSTROMS).
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. The capsid has a channel at the 5-fold axis and there are
CC densities extending the 5-fold axis into the interior of the capsid.
CC The capsid encapsulates the genomic ssDNA (By similarity). Binding to
CC the host receptors also induces capsid rearrangements leading to
CC surface exposure of VP1 N-terminus, specifically its phospholipase A2-
CC like region. The additional N-terminal region of isoform Minor capsid
CC protein VP1, called VP1u, may serve as a lipolytic enzyme to breach the
CC endosomal membrane during entry into host cell and might contribute to
CC virus transport to the nucleus (By similarity).
CC {ECO:0000250|UniProtKB:Q3YPH4, ECO:0000250|UniProtKB:Q9PZT0}.
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:0000250|UniProtKB:Q3YPH4};
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 (By similarity).
CC {ECO:0000250|UniProtKB:Q3YPH4}.
CC -!- SUBUNIT: [Isoform Minor capsid protein VP2]: Heteromultimer of isoform
CC Minor capsid protein VP1, isoform Minor capsid protein VP2 and isoform
CC Major capsid protein VP3 (By similarity).
CC {ECO:0000250|UniProtKB:Q3YPH4}.
CC -!- SUBUNIT: [Isoform Major capsid protein VP3]: Homomultimer (By
CC similarity). 10 fold more abundant than the minor capsid proteins VP1
CC and VP2 (By similarity). Heteromultimer of isoform Minor capsid protein
CC VP1, isoform Minor capsid protein VP2 and isoform Major capsid protein
CC VP3 (By similarity). {ECO:0000250|UniProtKB:Q3YPH4}.
CC -!- SUBCELLULAR LOCATION: [Isoform Minor capsid protein VP1]: Virion
CC {ECO:0000250|UniProtKB:Q3YPH4}. Host nucleus
CC {ECO:0000250|UniProtKB:Q3YPH4}. Host cytoplasm
CC {ECO:0000250|UniProtKB:Q3YPH4}. Note=Slightly detected in the
CC cytoplasm, mainly seen in the nucleus. {ECO:0000250|UniProtKB:Q3YPH4}.
CC -!- SUBCELLULAR LOCATION: [Isoform Minor capsid protein VP2]: Virion
CC {ECO:0000250|UniProtKB:Q3YPH4}.
CC -!- SUBCELLULAR LOCATION: [Isoform Major capsid protein VP3]: Virion
CC {ECO:0000250|UniProtKB:Q3YPH4}. Host nucleus
CC {ECO:0000250|UniProtKB:Q3YPH4}. Host cytoplasm
CC {ECO:0000250|UniProtKB:Q3YPH4}. Note=Slightly detected in the
CC cytoplasm, mainly seen in the nucleus. {ECO:0000250|UniProtKB:Q3YPH4}.
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. {ECO:0000250|UniProtKB:Q3YPH4};
CC Name=Minor capsid protein VP1;
CC IsoId=C1IWT2-1; Sequence=Displayed;
CC Name=Minor capsid protein VP2;
CC IsoId=C1IWT2-2; Sequence=VSP_059860, VSP_059865;
CC Name=Major capsid protein VP3;
CC IsoId=C1IWT2-3; Sequence=VSP_059859;
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 (By similarity). {ECO:0000250|UniProtKB:Q3YPH4,
CC ECO:0000250|UniProtKB:Q9PZT0}.
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; EU918736; ACH81929.1; -; Genomic_DNA.
DR EMBL; FJ948861; ACR43454.1; -; Genomic_DNA.
DR EMBL; EU918736; ACH81930.1; -; Genomic_DNA.
DR EMBL; FJ948861; ACR43455.1; -; Genomic_DNA.
DR RefSeq; YP_002808456.1; NC_012564.1. [C1IWT2-1]
DR RefSeq; YP_002808457.1; NC_012564.1. [C1IWT2-3]
DR PDB; 5US7; EM; 2.80 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/W/X/Y/Z/a/b/c/d/e/f/g/h/i/j/k/l/m/n/o/p/q/r/s/t/u/v/w/x/y/z=130-668.
DR PDBsum; 5US7; -.
DR SMR; C1IWT2; -.
DR DNASU; 7768238; -.
DR GeneID; 7768238; -.
DR GeneID; 7768239; -.
DR KEGG; vg:7768238; -.
DR KEGG; vg:7768239; -.
DR Proteomes; UP000128541; Genome.
DR Proteomes; UP000163519; 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: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 T=1 icosahedral capsid protein; Virion.
FT CHAIN 1..668
FT /note="Minor capsid protein VP1"
FT /id="PRO_0000445383"
FT REGION 11..66
FT /note="Phospholipase A2-like"
FT /evidence="ECO:0000250|UniProtKB:Q3YPH4"
FT REGION 107..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 611..622
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q9PZT0"
FT COMPBIAS 124..145
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 /id="VSP_059859"
FT VAR_SEQ 1..90
FT /note="Missing (in isoform Minor capsid protein VP2)"
FT /id="VSP_059860"
FT VAR_SEQ 91
FT /note="V -> M (in isoform Minor capsid protein VP2)"
FT /id="VSP_059865"
SQ SEQUENCE 668 AA; 74850 MW; B8D95EEA29EA37E5 CRC64;
MPPIKRQPGG WVLPGYKYLG PFNPLDNGEP VNKADRAAQS HDKSYSELIK SGKNPYLYFN
KADEKFIDDL KNDWSLGGII GSSFFKLKRA VAPALGNKER AQKRHFYFAN SNKGAKKSKN
NEPKPSTSKM SENEIQDQQP SEPNDGQRGG GGGATGSVGG GKGSGVGIST GGWVGGSYFT
DSYVITKNTR QFLVKIQNNH QYKTESIIPS NGGGKSQRCV STPWSYFNFN QYSSHFSPQD
WQRLTNEYKR FRPKGMHVKI YNLQIKQILS NGADVTYNND LTAGVHIFCD GEHAYPNATH
PWDEDVMPEL PYQTWYLFQY GYIPTIHELA EMEDSNAVEK AIALQIPFFM LENSDHEVLR
TGESAEFNFN FDCEWINNER AFIPPGLMFN PLVPTRRAQY IRRNGNTQAS TSRVQPYAKP
TSWMTGPGLL SAQRVGPAAS DTAAWMVGVD PEGANINSGR AGVSSGFDPP AGSLRPTDLE
YKVQWYQTPA GTNNDGNIIS NPPLSMLRDQ TLYRGNQTTY NLCSDVWMFP NQIWDRYPVT
RENPIWCKQP RSDKHTTIDP FDGSIAMDHP PGTIFIKMAK IPVPSNNNAD SYLNIYCTGQ
VSCEIVWEVE RYATKNWRPE RRHTALGLGI GGADEINPTY HVDKNGAYIQ PTTWDMCFPV
KTNINKVL
