CAPSD_HBOC4
ID CAPSD_HBOC4 Reviewed; 670 AA.
AC C5IY46; C5IY47;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 23-FEB-2022, entry version 40.
DE RecName: Full=Minor capsid protein VP1;
DE EC=3.1.1.4 {ECO:0000250|UniProtKB:Q3YPH4};
GN Name=VP1;
OS Human bocavirus 4 (HBoV4) (Human bocavirus type 4).
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Quintoviricetes;
OC Piccovirales; Parvoviridae; Parvovirinae; Bocaparvovirus;
OC Primate bocaparvovirus 2.
OX NCBI_TaxID=1511883;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HBoV4-NI-385;
RX PubMed=20415538; DOI=10.1086/652416;
RA Kapoor A., Simmonds P., Slikas E., Li L., Bodhidatta L., Sethabutr O.,
RA Triki H., Bahri O., Oderinde B.S., Baba M.M., Bukbuk D.N., Besser J.,
RA Bartkus J., Delwart E.;
RT "Human bocaviruses are highly diverse, dispersed, recombination prone, and
RT prevalent in enteric infections.";
RL J. Infect. Dis. 201:1633-1643(2010).
RN [2]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.00 ANGSTROMS), FUNCTION, SUBUNIT, AND
RP 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. 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 (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|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: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 (PubMed:28331084). Heteromultimer of isoform Minor capsid
CC protein VP1, isoform Minor capsid protein VP2 and isoform Major capsid
CC protein VP3 (By similarity). {ECO:0000250|UniProtKB:Q3YPH4,
CC ECO:0000269|PubMed:28331084}.
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:0000269|PubMed:28331084}. 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 (By similarity). {ECO:0000250|UniProtKB:Q3YPH4};
CC Name=Minor capsid protein VP1;
CC IsoId=C5IY46-1; Sequence=Displayed;
CC Name=Minor capsid protein VP2;
CC IsoId=C5IY46-2; Sequence=VSP_059862, VSP_059866;
CC Name=Major capsid protein VP3;
CC IsoId=C5IY46-3; Sequence=VSP_059861;
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: [Isoform Minor capsid protein VP1]: A nuclear localization
CC signal is present in the C-terminus and can be recognized by cellular
CC nuclear import molecules. After assembly, it is hidden because it is on
CC the inner capsid surface. {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}.
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; FJ973561; ACR15782.1; -; Genomic_DNA.
DR EMBL; FJ973561; ACR15781.1; -; Genomic_DNA.
DR RefSeq; YP_002916062.1; NC_012729.2. [C5IY46-1]
DR RefSeq; YP_002916063.1; NC_012729.2. [C5IY46-3]
DR PDB; 5US9; EM; 3.00 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=130-670.
DR PDBsum; 5US9; -.
DR SMR; C5IY46; -.
DR DNASU; 7922603; -.
DR GeneID; 7922602; -.
DR GeneID; 7922603; -.
DR KEGG; vg:7922602; -.
DR KEGG; vg:7922603; -.
DR Proteomes; UP000106086; 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..670
FT /note="Minor capsid protein VP1"
FT /id="PRO_0000445384"
FT REGION 11..66
FT /note="Phospholipase A2-like"
FT /evidence="ECO:0000250|UniProtKB:Q3YPH4"
FT REGION 106..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 613..624
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_059861"
FT VAR_SEQ 1..90
FT /note="Missing (in isoform Minor capsid protein VP2)"
FT /id="VSP_059862"
FT VAR_SEQ 91
FT /note="V -> M (in isoform Minor capsid protein VP2)"
FT /id="VSP_059866"
SQ SEQUENCE 670 AA; 75402 MW; 68842D0CB8C9A281 CRC64;
MPPIKRQPGG WVLPGYKYLG PFNPLENGEP VNKADRAAQA HDKSYSELIK SGKNPYLYFN
KADEKFIDDL KDDWSLGGII GSSFFKLKRA VAPALGNKER AQKRHFYFAN SNKGAKKTKN
NEPKPGTSKM SENEIQDQQP SDSMDGQRGG GGGATGSVGG GKGSGVGIST GGWVGGSYFT
DSYVITKNTR QFLVKIQNNH QYKTELISPS TSQGKSQRCV STPWSYFNFN QYSSHFSPQD
WQRLTNEYKR FRPKGMHVKI YNLQIKQILS NGADTTYNND LTAGVHIFCD GEHAYPNATH
PWDEDVMPEL PYQTWYLFQY GYIPVIHELA EMEDSNAVEK AICLQIPFFM LENSDHEVLR
TGESTEFTFN FDCEWINNER AYIPPGLMFN PLVPTRRAQY IRRNNNPQTA ESTSRIAPYA
KPTSWMTGPG LLSAQRVGPA TSDTGAWMVA VKPENASIDT GMSGIGSGFD PPQGSLAPTN
LEYKIQWYQT PQGTNNNGNI ISNQPLSMLR DQALFRGNQT TYNLCSDVWM FPNQIWDRYP
ITRENPIWCK KPRSDKHTTI DPFDGSLAMD HPPGTIFIKM AKIPVPSNNN ADSYLNIYCT
GQVSCEIVWE VERYATKNWR PERRHTTFGL GIGGADNLNP TYHVDKNGTY IQPTTWDMCF
PVKTNINKVL
