CAPSD_PAVC7
ID CAPSD_PAVC7 Reviewed; 727 AA.
AC P04863;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 3.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Capsid protein VP1;
DE AltName: Full=Coat protein VP1;
OS Canine parvovirus type 2 (strain Dog/United States/780929/-) (CPV-2).
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Quintoviricetes;
OC Piccovirales; Parvoviridae; Parvovirinae; Protoparvovirus.
OX NCBI_TaxID=10789;
OH NCBI_TaxID=9615; Canis lupus familiaris (Dog) (Canis familiaris).
OH NCBI_TaxID=9685; Felis catus (Cat) (Felis silvestris catus).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3989914; DOI=10.1128/jvi.54.2.630-633.1985;
RA Rhode S.L. III;
RT "Nucleotide sequence of the coat protein gene of canine parvovirus.";
RL J. Virol. 54:630-633(1985).
RN [2]
RP SEQUENCE REVISION.
RA Rhode S.L. III;
RL Submitted (JUL-1989) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 228-473.
RX PubMed=3942033; DOI=10.1016/0042-6822(86)90408-3;
RA Parrish C.R., Carmichael L.E.;
RT "Characterization and recombination mapping of an antigenic and host range
RT mutation of canine parvovirus.";
RL Virology 148:121-132(1986).
CC -!- FUNCTION: Capsid protein self-assembles to form an icosahedral capsid
CC with a T=1 symmetry, about 22 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. Capsid proteins are
CC responsible for the attachment to host cell receptor TFRC. This
CC attachment induces virion internalization predominantly through
CC clathrin-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 and nuclear localization
CC signal(s). VP1 N-terminus might serve as a lipolytic enzyme to breach
CC the endosomal membrane during entry into host cell. Intracytoplasmic
CC transport involves microtubules and interaction between capsid proteins
CC and host dynein. Exposure of nuclear localization signal probably
CC allows nuclear import of capsids (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with host TFRC. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000250}. Host nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=VP1;
CC IsoId=P04863-1; Sequence=Displayed;
CC Name=VP2;
CC IsoId=P04863-2; Sequence=VSP_041136;
CC -!- DOMAIN: The N-terminus of VP1 is sequestered within the mature capsid.
CC It contains a phospholipase A2-like region and nuclear localization
CC signals that might be exposed by capsid modifications during virus
CC entry (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: The capsids of autonomous parvoviruses expose a
CC proportion of VP2 N-terminus and part of that sequence can be cleaved
CC of to form VP3. {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform VP1]: Minor splicing isoform.
CC -!- MISCELLANEOUS: [Isoform VP2]: Major splicing isoform produced by
CC deletion of the initiating AUG for VP1 and downstream translation of
CC VP2. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the parvoviridae capsid protein family.
CC {ECO:0000305}.
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DR EMBL; M10989; AAA47149.1; -; Genomic_DNA.
DR EMBL; M11871; AAA47147.1; -; Genomic_DNA.
DR PIR; A03702; VCPVCN.
DR SMR; P04863; -.
DR PRIDE; P04863; -.
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: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: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 splicing; Capsid protein;
KW Clathrin-mediated endocytosis of virus by host;
KW Cytoplasmic inwards viral transport; Disulfide bond; Host nucleus;
KW Host-virus interaction; Magnesium; Metal-binding;
KW Microtubular inwards viral transport; 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..727
FT /note="Capsid protein VP1"
FT /id="PRO_0000039423"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 19..64
FT /note="Phospholipase A2-like"
FT /evidence="ECO:0000250"
FT REGION 95..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 141..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 503..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 4..13
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT BINDING 323
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT DISULFID 633..637
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..143
FT /note="Missing (in isoform VP2)"
FT /evidence="ECO:0000305"
FT /id="VSP_041136"
FT CONFLICT 414
FT /note="K -> R (in Ref. 3; AAA47147)"
FT /evidence="ECO:0000305"
FT CONFLICT 443..444
FT /note="AT -> DI (in Ref. 3; AAA47147)"
FT /evidence="ECO:0000305"
FT CONFLICT 452
FT /note="P -> Q (in Ref. 3; AAA47147)"
FT /evidence="ECO:0000305"
FT CONFLICT 456
FT /note="K -> R (in Ref. 3; AAA47147)"
FT /evidence="ECO:0000305"
FT CONFLICT 459
FT /note="V -> I (in Ref. 3; AAA47147)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 727 AA; 80290 MW; 26D12418B199BBC6 CRC64;
MAPPAKRARR GLVPPGYKYL GPGKSLDQGE PTNPSDAAAK EHDEAYAAYL RSGKNPYLYF
SPADQRFIDQ TKDAKDWGGK IGHYFFRAKK AIAPVLTDTP DHPSTSRPTK PTKRSKPPPH
IFINLAKKKK AGAGQVKRDN LAPMSDGAVQ PDGGQPAVRN ERATGSGNGS GGGGGGGSGG
VGISTGTFNN QTEFKFLENG WVEITANSSR LVHLNMPESE KDRRVVVNNM DKTAVNGNMA
LDDIHAQIVT PWSLVDANAW GVWFNPGDWQ LIVNTMSELH LVSFEQEIFN VVLKTVSESA
TQPPTKVYNN DLTASLMVAL DSNNTMPFTP AAMRSETLGF YPWKPTIPTP WRYYFQWDRT
LIPSHTGTSG TPTNIYHGTD PDDVQFYTIE NSVPVHLLRT GDEFATGTFF FDCKPCRLTH
TWQTNRALGL PPFLNSLPQS EGATNFGDIG VPQDKKRGVT QMGNTNYITE ATIMRPAEVG
YSAPYYSFEA STQGPFKTPI AAGRGGAQTD ENQAADGNPR YAFGRQHGKK TTTTGETPER
FTYIAHQDTG RYPEGDWIQN INFNLPVTND NVLLPIDPIG GKTGINYTNI FNTYGPLTAL
NNVPPVYPNG QIWDKEFDTD LKPRLHVNAP FVCQNNCPGQ LFVKLAPNLT NEYDPDASAN
MSRIVTYSDF WWKGKLVFKA KLRASHTWNP IQQMSINVDN QFNYVPSNIG GMKIVYEKSQ
LAPRKLY
