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CAPSD_DSDNV
ID   CAPSD_DSDNV             Reviewed;         809 AA.
AC   O71155; O92824;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   23-FEB-2022, entry version 80.
DE   RecName: Full=Capsid protein VP1;
DE   AltName: Full=Coat protein VP1;
DE   AltName: Full=Structural protein VP1;
GN   Name=VP;
OS   Diatraea saccharalis densovirus (DsDNV).
OC   Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Quintoviricetes;
OC   Piccovirales; Parvoviridae; Densovirinae; unclassified Densovirinae.
OX   NCBI_TaxID=72003;
OH   NCBI_TaxID=40085; Diatraea saccharalis (sugarcane borer).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Boublik Y., Kouassi K.N., Cavallaro C., Bergoin M.;
RT   "Complete nucleotide sequence and genome organization of an infectious
RT   clone of Diatraea saccharalis densovirus (DsDNV).";
RL   Submitted (DEC-1997) 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 size variants of the capsid proteins, which differ in the N-
CC       terminushe 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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative initiation; Named isoforms=4;
CC       Name=VP1;
CC         IsoId=O71155-1; Sequence=Displayed;
CC       Name=VP2;
CC         IsoId=O71155-2; Sequence=VSP_018947;
CC       Name=VP3;
CC         IsoId=O71155-3; Sequence=VSP_018948;
CC       Name=VP4;
CC         IsoId=O71155-4; Sequence=VSP_018949;
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.
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DR   EMBL; AF036333; AAC18002.1; -; Genomic_DNA.
DR   EMBL; AF036333; AAC18001.1; -; Genomic_DNA.
DR   RefSeq; NP_046815.1; NC_001899.1. [O71155-1]
DR   RefSeq; NP_046816.1; NC_001899.1. [O71155-2]
DR   SMR; O71155; -.
DR   GeneID; 1449602; -.
DR   GeneID; 1449606; -.
DR   KEGG; vg:1449602; -.
DR   KEGG; vg:1449606; -.
DR   Proteomes; UP000007205; Genome.
DR   GO; GO:0039615; C:T=1 icosahedral viral capsid; 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: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:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR   InterPro; IPR016184; Capsid/spike_ssDNA_virus.
DR   InterPro; IPR003433; Capsid_VP4_densovirus.
DR   InterPro; IPR013607; Phospholipase_A2-like.
DR   Pfam; PF02336; Denso_VP4; 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; Host-virus interaction;
KW   T=1 icosahedral capsid protein; Viral attachment to host cell;
KW   Viral penetration into host cytoplasm;
KW   Viral penetration via permeabilization of host membrane; Virion;
KW   Virus endocytosis by host; Virus entry into host cell.
FT   CHAIN           1..809
FT                   /note="Capsid protein VP1"
FT                   /id="PRO_0000039447"
FT   REGION          315..366
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          373..392
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        325..343
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        344..366
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        376..392
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..373
FT                   /note="Missing (in isoform VP4)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_018949"
FT   VAR_SEQ         1..322
FT                   /note="Missing (in isoform VP3)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_018948"
FT   VAR_SEQ         1..277
FT                   /note="Missing (in isoform VP2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_018947"
SQ   SEQUENCE   809 AA;  87961 MW;  B07D809018C1C140 CRC64;
     MSFYARALTH RARPGYRIIP ENTVTEDIEL GAIGEETPLL SEGIITAAEE TAAVGLPELG
     VGAVGAVGTH ADVLYRNRNA FKSVLTGNYT DLKGNPLKQR NAISEKTKQL GKQIFQGDFN
     RAFPDNLKLE TEQEKTDLLR YYNHNRRLAG LSEAYPQGKG YAYAKSQKVL EAEKRGLTVP
     GYKYLGPGNS LNRGPPTNEI DADAKEHDEA YSQSKTAQEV SKADNTFVNK ALDHVVNAIN
     LKESPSNTVG AIIGATGIGT KQAIEKHTGV IYPSVSGMSR EINPKYLNSW SDWIKENKPN
     NFAGIQLPED FYTEEQTLSD SPMSESTKRK ADTPAEETPS KKGAHNTDSS SQSADPQNPS
     SSGATTDLDV TMAMSLPGTG SGTSSGGGNT TGQEIYEIPR PFTNFGKKLS TYTKSHKFMI
     FGLANNVIAE TGTTGNLHRL LTTCLAEIPW QKIPLYMNQS EFDLLPPGSR IVECNVKVIF
     RSNRIAFETS STATKQATLN QISNLQTAVG LNKLGWGIDR SFTAFQSDQP MIPTASAPPK
     YASVSGANGY RGMIADYYGA DSNNDIAFGN AGNYPHHQVG SFTFLQNYYC MYIQTERGTG
     GWPCLAEHFQ QYDSKTVNNQ CLLDVSYKPQ MGMIKPPLNY NIIGFPTNKG AISIGENLTA
     MRSANVSGPE IATQQVSETS NNRIHNFPAT FFDIYADIEK SQRLNKGPWG FEHPQIQPSI
     HIGMQAVPAL TTGALLVNSS PLNSWTDSMG YVDVIASCTV MESQPTHFPY ATSANTNPGN
     TVYRNNINVN SLTSAFNGLY GNAATLGSL
 
 
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