ID   CAPSD_PAVP9             Reviewed;         729 AA.
AC   P33484;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Capsid protein VP1;
DE   AltName: Full=Coat protein VP1;
OS   Porcine parvovirus (strain 90HS) (PPV).
OC   Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Quintoviricetes;
OC   Piccovirales; Parvoviridae; Parvovirinae; Protoparvovirus.
OX   NCBI_TaxID=33725;
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=2750278; DOI=10.1016/0168-1702(89)90088-9;
RA   Sakurai M., Nishimori T., Ushimi C., Nakajima H.;
RT   "Nucleotide sequence of capsid protein gene of porcine parvovirus.";
RL   Virus Res. 13:79-86(1989).
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 receptors. 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 and putative nuclear
CC       localization signal(s). VP1 N-terminus might serve as a lipolytic
CC       enzyme to breach the endosomal membrane during entry into host cell and
CC       might contribute to virus transport to the nucleus (By similarity).
CC       {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=P33484-1; Sequence=Displayed;
CC       Name=VP2;
CC         IsoId=P33484-2; Sequence=VSP_041142;
CC   -!- DOMAIN: The N-terminus of VP1 is sequestered within the mature capsid.
CC       It contains a phospholipase A2-like region and putative nuclear
CC       localization signals.
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.
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   PIR; A60006; A60006.
DR   SMR; P33484; -.
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; Host nucleus; Host-virus interaction;
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..729
FT                   /note="Capsid protein VP1"
FT                   /id="PRO_0000039433"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          18..63
FT                   /note="Phospholipase A2-like"
FT                   /evidence="ECO:0000250"
FT   REGION          94..129
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          163..186
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          437..465
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           4..12
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   BINDING         330
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         1..150
FT                   /note="Missing (in isoform VP2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_041142"
SQ   SEQUENCE   729 AA;  80938 MW;  92538BFF9A0C78E6 CRC64;
     MAPPAKRARG LTLPGYKYLG PGNSLDQGEP TNPSDAAAKE HDEAYDKYIK SGKNPYFYFS
     AADEKFIKET EHAKDYGGKI GHYFFRAKRA FRPKLSETDS PTTSQQPEVR RSPRKHPGSK
     PPGKRPAPRH IFINLAKKKA KGTSNTNSNS MSENVEQHNP INAGTELSAT GNESGGGGGG
     GGGRGAGGVG VSTGSFNNQT EFQYLGEGLV RITAHASRLI HLNMPEHETY KRIHVLNSES
     GVAGQMVQDD AHTQMVTPWS LIDANAWGVW FNPADWQLIS NNMTEINLVS FEQEIFNVVL
     KTITESATSP PTKIYNNDLT ASLMVALDTN NTLPYTPAAP RSETLGFYPW LPTKPTQYRY
     YLSCTRNLNP PTYTGQSQQI TDSIQTGLHS DIMFYTIENA VPIHLLRTGD EFSTGIYHFD
     TKPLKLTHSW QTNRSLGLPP KLLTEPTTEG DQHPGTLPAA NTRKGYHQTM NNSYTEATAI
     RPAQVGYNTP YMNFEYSNGG PFLTPIVPTA DTQYNDDEPN GAIRFTMGYQ HGQLTTSSQE
     LERYTFNPQS KCGRAPKQQF NQQAPLNLEN TNNGTLLPSD PIGGKPNMHF MNTLNTYGPL
     TALNNTAPVF PNGQIWDKEL DTDLKPRLHV TAPFVCKNNP PGQLFVKIAP NLTDDFNADS
     PQQPRIITYS NFWWKGTLTF TAKMRSSNMW NPIQQHTTTA ENIGNYIPTN IGGIKMFPEY
     SQLIPRKLY