ID   CAPSD_PAVC              Reviewed;         584 AA.
AC   P61826;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2004, sequence version 1.
DT   02-SEP-2026, entry version 79.
DE   RecName: Full=Capsid protein VP2;
DE   AltName: Full=Coat protein VP2;
OS   Canine parvovirus type 2 (CPV-2).
OC   Viruses; Floreoviria; Shotokuvirae; Cossaviricota; Quintoviricetes;
OC   Piccovirales; Parvoviridae; Parvovirinae; Protoparvovirus;
OC   Protoparvovirus carnivoran1.
OX   NCBI_TaxID=10788;
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].
RC   STRAIN=Isolate CPV2b-India;
RA   Gupta P.K., Rai A., Rai N., Raut A.A., Chauhan S.;
RT   "Cloning of VP2 gene of canine parvovirus in a mammalian expression vector
RT   for use as DNA vaccine.";
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
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=VP2;
CC         IsoId=P61826-1; Sequence=Displayed;
CC       Name=VP1;
CC         IsoId=P61826-2; Sequence=Not described;
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 VP2]: Major splicing isoform produced by
CC       deletion of the initiating AUG for VP1 and downstream translation of
CC       VP2.
CC   -!- MISCELLANEOUS: [Isoform VP1]: Minor splicing isoform. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the parvoviridae capsid protein family.
CC       {ECO:0000305}.
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DR   EMBL; AJ698134; CAG27358.1; -; Genomic_DNA.
DR   SMR; P61826; -.
DR   ABCD; P61826; 1 sequenced antibody.
DR   GO; GO:0043657; C:host cell; IEA:GOC.
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:0098671; P:adhesion receptor-mediated virion attachment to host cell; IEA:UniProtKB-KW.
DR   GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
DR   GO; GO:0098670; P:entry receptor-mediated virion attachment to 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:0140267; P:symbiont entry into host cell via permeabilization of host membrane; IEA:UniProtKB-KW.
DR   GO; GO:0075732; P:viral penetration into host nucleus; IEA:UniProtKB-KW.
DR   Gene3D; 2.170.30.10; Parvovirus coat protein VP1/VP2; 1.
DR   InterPro; IPR016184; Capsid/spike_ssDNA_virus.
DR   InterPro; IPR001403; Parvovirus_coat.
DR   InterPro; IPR036952; VP1/VP2.
DR   Pfam; PF00740; VP1_2; 1.
DR   SUPFAM; SSF88645; ssDNA viruses; 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 adhesion receptor; Viral attachment to host cell;
KW   Viral attachment to host entry receptor;
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..584
FT                   /note="Capsid protein VP2"
FT                   /id="PRO_0000222457"
FT   REGION          1..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..40
FT                   /note="Gly residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         180
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   DISULFID        490..494
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   584 AA;  64705 MW;  C2B77AB02436FBDA CRC64;
     MSDGAVQPDG GQPAVRNERA TGSGNGSGGG GGGGSGGVGI STGTFNNQTE FKFLENGWVE
     ITANSSRLVH LNMPESENYR RVVVNNMDKT AVNGNMALDD IHVQIVTPWS LVDANAWGVW
     FNPGDWQLIV NTMSELHLVS FEQEIFNVVL KTVSESATQP PTKVYNNDLT ASLMVALDSN
     NTMPFTPAAM RSETLGFYPW KPTIPTPWRY YFQWDRTLVP SHTGTSGTPT NIYHGTDPDD
     VQFYTIENSV PVHLLRTGDE FATGTFFFDC KPCRLTHTWQ TNRALGLPPF LNSLPQSEGA
     TNFGDIGVQQ DKRRGVTQMG NTNYITEATI MRPAEVGYSA PYYSFEASTQ GPFKTPIAAG
     RGGAQTYENQ AADGDPRYAF GRQHGQKTTT TGETPDRITY IAHHDTGRYP EGDWIQNINF
     NLPVTNDNVL LPTDPIGGKT GINYTNIFNT YGPLTALNNV PPVYPNGQIW DKEFDTDLKP
     RPHVNAPFVC QHNCPGQLFV KVAPNLTNEY DPDASANMSR IVTYSHFWWK GKLVFKAKLR
     ASHTWNPIQQ MSINVDNQFN YVPSNIGGMK IVYEKSQLAP RKLY
//