ID   CAPSD_AADNV             Reviewed;         355 AA.
AC   Q90187;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1999, sequence version 2.
DT   02-JUN-2021, entry version 73.
DE   RecName: Full=Capsid protein VP1/VP2;
DE   AltName: Full=Coat protein VP1/VP2;
GN   Name=VP;
OS   Aedes albopictus densovirus (isolate Boublik/1994) (AalDNV).
OC   Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Quintoviricetes;
OC   Piccovirales; Parvoviridae; Hamaparvovirinae; Brevihamaparvovirus;
OC   Dipteran brevihamaparvovirus 1.
OX   NCBI_TaxID=648330;
OH   NCBI_TaxID=7160; Aedes albopictus (Asian tiger mosquito) (Stegomyia albopicta).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8178459; DOI=10.1006/viro.1994.1239;
RA   Boublik Y., Jousset F.X., Bergoin M.;
RT   "Complete nucleotide sequence and genomic organization of the Aedes
RT   albopictus parvovirus (AaPV) pathogenic for Aedes aegypti larvae.";
RL   Virology 200:752-763(1994).
RN   [2]
RP   FUNCTION.
RC   STRAIN=Aedes albopictus C6/36 cell densovirus;
RX   PubMed=17393085; DOI=10.1007/s11427-007-2036-3;
RA   Cheng L., Chen S., Zhou Z.H., Zhang J.;
RT   "Structure comparisons of Aedes albopictus densovirus with other
RT   parvoviruses.";
RL   Sci. China, Ser. C, Life Sci. 50:70-74(2007).
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       ECO:0000269|PubMed:17393085}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative initiation; Named isoforms=2;
CC       Name=VP1;
CC         IsoId=Q90187-1; Sequence=Displayed;
CC       Name=VP2;
CC         IsoId=Q90187-2; Sequence=Not described;
CC   -!- SIMILARITY: Belongs to the parvoviridae capsid protein family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA52901.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; X74945; CAA52901.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_694829.3; NC_004285.1.
DR   GeneID; 955418; -.
DR   KEGG; vg:955418; -.
DR   Proteomes; UP000008472; Genome.
DR   GO; GO:0039615; C:T=1 icosahedral viral capsid; IEA:UniProtKB-KW.
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.
PE   3: Inferred from homology;
KW   Alternative initiation; Capsid protein;
KW   Clathrin-mediated endocytosis of virus by host; Host-virus interaction;
KW   Reference proteome; T=1 icosahedral capsid protein;
KW   Viral attachment to host cell; 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..355
FT                   /note="Capsid protein VP1/VP2"
FT                   /id="PRO_0000039443"
FT   REGION          1..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..23
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   355 AA;  40942 MW;  F662F6F56CD2A7F1 CRC64;
     MADSTTMEHD GRGTKRKREA DGGSGQGVGK GNSNAVKEGY GPNITEMVPR NIFNKGNHTI
     YHVVKTQKYL DFNYVTNQNP YIIPYQTAGF WGSMWDQTDI GNNQSINIMK ALNAVALGVT
     WIKGEITFEV YSVTRQRLLT GTTNQTTWDF ETSQNMFIAD ADREPENFNL ETVAATGPLA
     QQTTQTLLFN SHNDRYTKYE LPQRNQYTRE INFQQLTNNY MWRPLDISKE TNFRSLIPMS
     EGVYTKSENL RQTEFTYETT TYATSGATTR QTLFRNRTSY PRMHIAQPQV PDETGFMKFR
     YQVRMSTKLH LNFHMYPDYA TNNNLEYMHR QTILLPQVAE TNGIVACMPY EINTQ