CAPSD_PAVHU
ID CAPSD_PAVHU Reviewed; 781 AA.
AC P07299;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Minor capsid protein VP1;
DE EC=3.1.1.4;
DE AltName: Full=Coat protein VP1;
OS Human parvovirus B19 (isolate AU) (HPV B19).
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Quintoviricetes;
OC Piccovirales; Parvoviridae; Parvovirinae; Erythroparvovirus.
OX NCBI_TaxID=648238;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3701931; DOI=10.1128/jvi.58.3.921-936.1986;
RA Shade R.O., Blundell M.C., Cotmore S.F., Tattersall P., Astell C.R.;
RT "Nucleotide sequence and genome organization of human parvovirus B19
RT isolated from the serum of a child during aplastic crisis.";
RL J. Virol. 58:921-936(1986).
RN [2]
RP FUNCTION, AND INTERACTION WITH INTEGRIN HETERODIMER ITGAV/ITGB1.
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 [3]
RP FUNCTION, AND INTERACTION WITH THE HOST GLOBOSIDE RECEPTOR.
RX PubMed=20826697; DOI=10.1128/jvi.01143-10;
RA Boensch C., Zuercher C., Lieby P., Kempf C., Ros C.;
RT "The globoside receptor triggers structural changes in the B19 virus capsid
RT that facilitate virus internalization.";
RL J. Virol. 84:11737-11746(2010).
RN [4]
RP REVIEW.
RX PubMed=20631151; DOI=10.1128/jvi.00684-10;
RA Servant-Delmas A., Lefrere J.J., Morinet F., Pillet S.;
RT "Advances in human B19 erythrovirus biology.";
RL J. Virol. 84:9658-9665(2010).
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. The capsid encapsulates the genomic ssDNA. Binds to erythroid
CC progenitor cells expressing high levels of P antigen and uses host
CC ITGA5-ITGB1 and XRCC5/Ku80 autoantigen as coreceptors on the cell
CC surface to provide virion attachment to target cell. This attachment
CC induces virion internalization predominantly through clathrin-dependent
CC endocytosis. 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. {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:Q9PZT0};
CC -!- SUBUNIT: [Isoform Minor capsid protein VP1]: Heteromultimer of isoform
CC Minor capsid protein VP1 and isoform Major capsid protein VP2.
CC {ECO:0000250|UniProtKB:Q9PZT0}.
CC -!- SUBUNIT: [Isoform Major capsid protein VP2]: Heteromultimer of isoform
CC Minor capsid protein VP1 and isoform Major capsid protein VP2. 20 fold
CC more abundant than the minor capsid protein VP1.
CC {ECO:0000250|UniProtKB:Q9PZT0}.
CC -!- SUBCELLULAR LOCATION: [Isoform Minor capsid protein VP1]: Virion
CC {ECO:0000250|UniProtKB:Q9PZT0}. Host nucleus
CC {ECO:0000250|UniProtKB:Q9PZT0}. Host cytoplasm
CC {ECO:0000250|UniProtKB:Q9PZT0}.
CC -!- SUBCELLULAR LOCATION: [Isoform Major capsid protein VP2]: Virion
CC {ECO:0000250|UniProtKB:Q9PZT0}. Host nucleus
CC {ECO:0000250|UniProtKB:Q9PZT0}. Host cytoplasm
CC {ECO:0000250|UniProtKB:Q9PZT0}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Minor capsid protein VP1;
CC IsoId=P07299-1; Sequence=Displayed;
CC Name=Major capsid protein VP2;
CC IsoId=P07299-2; Sequence=VSP_059854;
CC -!- DOMAIN: [Isoform Minor capsid protein VP1]: The N-terminus of VP1,
CC VP1u, contains a phospholipase A2-like region. VP1u is necessary and
CC sufficient for host cell binding and internalization.
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 -!- MISCELLANEOUS: [Isoform Minor capsid protein VP1]: Minor splicing
CC isoform. {ECO:0000250|UniProtKB:Q9PZT0}.
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:0000250|UniProtKB:Q9PZT0}.
CC -!- SIMILARITY: Belongs to the parvoviridae capsid protein family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1s58";
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DR EMBL; M13178; AAA66867.1; -; Genomic_DNA.
DR PIR; A24299; VCPV19.
DR SMR; P07299; -.
DR ABCD; P07299; 2 sequenced antibodies.
DR Proteomes; UP000008027; 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 1: Evidence at protein level;
KW 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 T=1 icosahedral capsid protein; Viral attachment to host cell;
KW Viral penetration into host cytoplasm; 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_0000222459"
FT REGION 5..80
FT /note="Binding to the host cell receptor and
FT internalization"
FT /evidence="ECO:0000250|UniProtKB:Q9PZT0"
FT REGION 77..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 130..175
FT /note="Phospholipase A2-like"
FT REGION 524..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 761..781
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 720..730
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q9PZT0"
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 /id="VSP_059854"
SQ SEQUENCE 781 AA; 86015 MW; 8C6254DBD0576B07 CRC64;
MSKKSGKWWE SDDKFAKAVY QQFVEFYEKV TGTDLELIQI LKDHYNISLD NPLENPSSLF
DLVARIKNNL KNSPDLYSHH FQSHGQLSDH PHALSSSSSH AEPRGENAVL SSEDLHKPGQ
VSVQLPGTNY VGPGNELQAG PPQSAVDSAA RIHDFRYSQL AKLGINPYTH WTVADEELLK
NIKNETGFQA QVVKDYFTLK GAAAPVAHFQ GSLPEVPAYN ASEKYPSMTS VNSAEASTGA
GGGGSNSVKS MWSEGATFSA NSVTCTFSRQ FLIPYDPEHH YKVFSPAASS CHNASGKEAK
VCTISPIMGY STPWRYLDFN ALNLFFSPLE FQHLIENYGS IAPDALTVTI SEIAVKDVTD
KTGGGVQVTD STTGRLCMLV DHEYKYPYVL GQGQDTLAPE LPIWVYFPPQ YAYLTVGDVN
TQGISGDSKK LASEESAFYV LEHSSFQLLG TGGTASMSYK FPPVPPENLE GCSQHFYEMY
NPLYGSRLGV PDTLGGDPKF RSLTHEDHAI QPQNFMPGPL VNSVSTKEGD SSNTGAGKAL
TGLSTGTSQN TRISLRPGPV SQPYHHWDTD KYVTGINAIS HGQTTYGNAE DKEYQQGVGR
FPNEKEQLKQ LQGLNMHTYF PNKGTQQYTD QIERPLMVGS VWNRRALHYE SQLWSKIPNL
DDSFKTQFAA LGGWGLHQPP PQIFLKILPQ SGPIGGIKSM GITTLVQYAV GIMTVTMTFK
LGPRKATGRW NPQPGVYPPH AAGHLPYVLY DPTATDAKQH HRHGYEKPEE LWTAKSRVHP
L
