CAPSD_JDNVP
ID CAPSD_JDNVP Reviewed; 810 AA.
AC Q90053;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 23-FEB-2022, entry version 86.
DE RecName: Full=Capsid protein VP1;
DE AltName: Full=Coat protein VP1;
DE AltName: Full=Structural protein VP1;
GN Name=VP;
OS Junonia coenia densovirus (isolate pBRJ/1990) (JcDNV).
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Quintoviricetes;
OC Piccovirales; Parvoviridae; Densovirinae; Ambidensovirus.
OX NCBI_TaxID=648250;
OH NCBI_TaxID=7088; Lepidoptera (butterflies and moths).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1413502; DOI=10.1016/0042-6822(92)90182-o;
RA Dumas B., Jourdan M., Pascaud A.M., Bergoin M.;
RT "Complete nucleotide sequence of the cloned infectious genome of Junonia
RT coenia densovirus reveals an organization unique among parvoviruses.";
RL Virology 191:202-222(1992).
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 protein which differ in the N-
CC terminus. The capsid encapsulates the genomic ssDNA. Capsid proteins
CC are responsible for the attachment to host cell receptors. This
CC attachment induces virion internalization predominantly through
CC clathrin-dependent 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=Q90053-1; Sequence=Displayed;
CC Name=VP2;
CC IsoId=Q90053-2; Sequence=VSP_018953;
CC Name=VP3;
CC IsoId=Q90053-3; Sequence=VSP_018954;
CC Name=VP4;
CC IsoId=Q90053-4; Sequence=VSP_018955;
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DR EMBL; S47266; AAB23698.1; -; Genomic_DNA.
DR PIR; A44054; A44054.
DR RefSeq; NP_694823.1; NC_004284.1.
DR GeneID; 955412; -.
DR KEGG; vg:955412; -.
DR Proteomes; UP000008294; 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 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..810
FT /note="Capsid protein VP1"
FT /id="PRO_0000039455"
FT REGION 305..394
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 345..369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..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_018955"
FT VAR_SEQ 1..322
FT /note="Missing (in isoform VP3)"
FT /evidence="ECO:0000305"
FT /id="VSP_018954"
FT VAR_SEQ 1..277
FT /note="Missing (in isoform VP2)"
FT /evidence="ECO:0000305"
FT /id="VSP_018953"
SQ SEQUENCE 810 AA; 87896 MW; 0D618F04ADD04DE4 CRC64;
MSFYTAGLIH RARPGYRIIP ESTATEDIEL GAIGEETPLL SEGAVTAVEE SAAVGLPELG
AGLAGAIGTH ADVLYRNRNV FKSVLTGNYT DLKGNPLKQR NAISEKTKQL GRGIFQGDFN
RAFPDDLKLE TEQEKKDLLR YYNHNRRLAG LSEAYPQGKG YAYAKSQKVL EAERRGLTVP
GYKYLGPGNS LNRGQPTNQI DEDAKEHDEA YDKAKTSQEV SQADNTFVNK ALDHIVNAIN
LKETPGNAFG AAIGAIGIGT KQAIEKHSGV IYPSVSGMSR QINSKYLNSW HDWIEQNKHN
NFEGIQLPED FYTEEQTLSD SPMSEGTKRK ADTPVEEGPS KKGAHNAPHN SQGTDPQNPS
SSGATTSXDV EMAMSLPGTG SGTSSGGGNT SGQEVYVIPR PFSNFGKKLS TYTKSHKFMI
FGLANNVIGP TGTGTTAVNR LITTCLAEIP WQKLPLYMNQ SEFDLLPPGS RVVECNVKVI
FRTNRIAFET SSTATKQATL NQISNLQTAV GLNKLGWGID RSFTAFQSDQ PMIPTATSAP
KYEPITGTTG YRGMIADYYG ADSTNDAAFG NAGNYPHHQV GSFTFIQNYY CMYQQTNQGT
GGWPCLAEHL QQFDSKTVNN QCLIDVTYKP KMGLIKPPLN YKIIGQPTAK GTISVGDNLV
NMRGAVVINP PEATQSVTES THNLTRNFPA NLFNIYSDIE KSQILHKGPW GHENPQIQPS
VHIGIQAVPA LTTGALLVNS SPLNSWTDSM GYIDVMSSCT VMESQPTHFP FSTDANTNPG
NTIYRINLTP NSLTSAFNGL YGNGATLGNV