CAPSD_PAVBP
ID CAPSD_PAVBP Reviewed; 673 AA.
AC P07297; Q84374;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 23-FEB-2022, entry version 97.
DE RecName: Full=Minor capsid protein VP1;
DE EC=3.1.1.4 {ECO:0000250|UniProtKB:Q3YPH4};
OS Bovine parvovirus (isolate pAT153/1986) (BPV).
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Quintoviricetes;
OC Piccovirales; Parvoviridae; Parvovirinae; Bocaparvovirus.
OX NCBI_TaxID=648243;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3783814; DOI=10.1128/jvi.60.3.1085-1097.1986;
RA Chen K.C., Shull B.C., Moses E.A., Lederman M., Stout E.R., Bates R.C.;
RT "Complete nucleotide sequence and genome organization of bovine
RT parvovirus.";
RL J. Virol. 60:1085-1097(1986).
RN [2]
RP FUNCTION.
RX PubMed=20810750; DOI=10.1099/vir.0.024133-0;
RA Dudleenamjil E., Lin C.Y., Dredge D., Murray B.K., Robison R.A.,
RA Johnson F.B.;
RT "Bovine parvovirus uses clathrin-mediated endocytosis for cell entry.";
RL J. Gen. Virol. 91:3032-3041(2010).
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 (By similarity). {ECO:0000250|UniProtKB:Q3YPH4};
CC Name=Minor capsid protein VP1;
CC IsoId=P07297-1; Sequence=Displayed;
CC Name=Minor capsid protein VP2;
CC IsoId=P07297-2; Sequence=VSP_059853, VSP_059867;
CC Name=Major capsid protein VP3;
CC IsoId=P07297-3; Sequence=VSP_059852;
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}.
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DR EMBL; M14363; AAB59848.1; -; Genomic_DNA.
DR EMBL; M14363; AAB59849.1; -; Genomic_DNA.
DR PIR; A26104; VCPVB5.
DR RefSeq; NP_041404.1; NC_001540.1.
DR RefSeq; NP_041406.1; NC_001540.1.
DR SMR; P07297; -.
DR GeneID; 1489584; -.
DR GeneID; 1489585; -.
DR KEGG; vg:1489584; -.
DR KEGG; vg:1489585; -.
DR Proteomes; UP000007022; 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:0046872; F:metal ion binding; 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:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
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:0099008; P:viral entry via permeabilization of inner membrane; IEA:UniProtKB-KW.
DR GO; GO:0075732; P:viral penetration into host nucleus; IEA:UniProtKB-KW.
DR GO; GO:0019062; P:virion attachment to host cell; 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 3: Inferred from homology;
KW Alternative initiation; 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..673
FT /note="Minor capsid protein VP1"
FT /id="PRO_0000039421"
FT REGION 13..68
FT /note="Phospholipase A2-like"
FT /evidence="ECO:0000250|UniProtKB:Q3YPH4"
FT REGION 118..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 623..634
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q9PZT0"
FT COMPBIAS 127..148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..137
FT /note="Missing (in isoform Major capsid protein VP3)"
FT /id="VSP_059852"
FT VAR_SEQ 1..91
FT /note="Missing (in isoform Minor capsid protein VP2)"
FT /id="VSP_059853"
FT VAR_SEQ 92
FT /note="A -> M (in isoform Minor capsid protein VP2)"
FT /id="VSP_059867"
SQ SEQUENCE 673 AA; 75103 MW; 5F244642B2214831 CRC64;
MPPTNKANSK KGLTLPGYNY LGPFNSLFAG APVNKADAAA RKHDFGYSDL LKEGKNPYLY
FNTHDQNLID ELKDDTSFGG KLARGVFQIK KALAPALPGT SKGGDRALKR KLYFARSNKG
AKKANREPAP STSNQQNMEV SNDIPNDEAG NQPIELATRS VVGSGSVGGG GRGGSGVGYS
TGGWTGGTIF SENIVVTKNT RQFICDIKNG HLYKSEVLNT GDTAHRQYAI TTPWSYFNFN
QYSSHFSPND WQHLVNDYER FRPKAMIVRV YNLQIKQIMT DGAMGTVYNN DLTAGMHIFC
DGDHRYPYVQ HPWDDQCMPE LPNSIWELPQ YAYIPAPISV VDNNTTNTVE EHLLKGVPLY
MLENSDHEVL RNGRIYRIYI QLWRLRMDRK QHHIQHASDD VQSTGQKQKN LLIQRTKQPN
KQRFQNAALR TSNWMSGPGI ARGTHNATLQ TQSAGALVTM VTNGADVSGV RAVRVGYSTD
PIYGGQQPES DLLRLRYSAS AAEGQQNPIL ENAARHTFTR EARTKLITGS NGADGDYKEW
WMLPNQMWDS APISRYNPIW VKVPRVNRKT LLDTQDGSIP MSHPPGTIFI KLARIPVPGN
GDSFLNIYVT GQVSCEVVWE VEKRGTKNWR PEYMHSATNM SVDAYTINNA GVYAGAVQNA
DVMQTRFNHH KVL
