CAPSD_GMDNV
ID CAPSD_GMDNV Reviewed; 811 AA.
AC Q90125; Q90126; Q90127; Q90128;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 23-FEB-2022, entry version 93.
DE RecName: Full=Capsid protein VP1;
DE AltName: Full=Coat protein VP1;
DE AltName: Full=Structural protein VP1;
GN Name=VP;
OS Galleria mellonella densovirus (GmDNV).
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Quintoviricetes;
OC Piccovirales; Parvoviridae; Densovirinae; Protoambidensovirus;
OC Lepidopteran protoambidensovirus 1.
OX NCBI_TaxID=37138;
OH NCBI_TaxID=7137; Galleria mellonella (Greater wax moth).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Tijssen P.;
RT "Organization and expression of the ambisense genome of densonucleosis
RT virus of Galleria mellonella (GmDNV).";
RL Submitted (NOV-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS) OF 396-811.
RX PubMed=9817847; DOI=10.1016/s0969-2126(98)00136-1;
RA Simpson A.A., Chipman P.R., Baker T.S., Tijssen P., Rossmann M.G.;
RT "The structure of an insect parvovirus (Galleria mellonella densovirus) at
RT 3.7 A resolution.";
RL Structure 6:1355-1367(1998).
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=Q90125-1; Sequence=Displayed;
CC Name=VP2;
CC IsoId=Q90125-2; Sequence=VSP_018950;
CC Name=VP3;
CC IsoId=Q90125-3; Sequence=VSP_018951;
CC Name=VP4;
CC IsoId=Q90125-4; Sequence=VSP_018952;
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L32896; AAA66966.1; -; Genomic_DNA.
DR EMBL; L32896; AAA66964.1; -; Genomic_DNA.
DR EMBL; L32896; AAA66965.1; -; Genomic_DNA.
DR EMBL; L32896; AAA66967.1; -; Genomic_DNA.
DR RefSeq; NP_694830.1; NC_004286.1. [Q90125-1]
DR RefSeq; NP_694831.1; NC_004286.1. [Q90125-2]
DR RefSeq; NP_694832.1; NC_004286.1. [Q90125-3]
DR RefSeq; NP_694833.1; NC_004286.1. [Q90125-4]
DR PDB; 1DNV; X-ray; 3.60 A; A=375-811.
DR PDBsum; 1DNV; -.
DR SMR; Q90125; -.
DR GeneID; 2546231; -.
DR KEGG; vg:2546231; -.
DR EvolutionaryTrace; Q90125; -.
DR Proteomes; UP000202161; Genome.
DR GO; GO:0039615; C:T=1 icosahedral viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0004623; F:phospholipase A2 activity; IEA:InterPro.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0050482; P:arachidonic acid secretion; 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:0006644; P:phospholipid metabolic process; IEA:InterPro.
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 Gene3D; 1.20.90.10; -; 1.
DR InterPro; IPR016184; Capsid/spike_ssDNA_virus.
DR InterPro; IPR003433; Capsid_VP4_densovirus.
DR InterPro; IPR013607; Phospholipase_A2-like.
DR InterPro; IPR036444; PLipase_A2_dom_sf.
DR Pfam; PF02336; Denso_VP4; 1.
DR Pfam; PF08398; Phospholip_A2_4; 1.
DR SUPFAM; SSF88645; SSF88645; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 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..811
FT /note="Capsid protein VP1"
FT /id="PRO_0000039451"
FT REGION 321..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..337
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..374
FT /note="Missing (in isoform VP4)"
FT /evidence="ECO:0000305"
FT /id="VSP_018952"
FT VAR_SEQ 1..323
FT /note="Missing (in isoform VP3)"
FT /evidence="ECO:0000305"
FT /id="VSP_018951"
FT VAR_SEQ 1..276
FT /note="Missing (in isoform VP2)"
FT /evidence="ECO:0000305"
FT /id="VSP_018950"
SQ SEQUENCE 811 AA; 88542 MW; 0A61B09172DF99B5 CRC64;
MSFFKNQLIH RARPGYRIIP ESTVTEDIEL GTIGEETPLL SEGVITAVEE GAIGLPEVAI
GVAGAIGTHA HEWWRDRYAF KSVLTGNYTD LKGNPLKPRN AIPEKIKQLG KKIFQGDFNR
AFPDNLKLET EKEKADLLRY YNHNRRLAGL SEAYPQGKGY AYAKSQKVLE AERRGLTVPG
YKYLGPGNSL NRGQPINQID EDAKEHDEAY DKVKTSQEVS RADNTFVNKA LDHVVNAINF
KETPGNAFGA AIGAIGIGTK QAIEKYSGVI YPSVSGMSRH INPRYINQPN WKDYIAEGNS
KNWVGYSNLP DDFFQEETLS DSPMQEATKR KADSPAVETP AKKGTTGVNV NSQSTDPQNP
SSSGATTDLD VTMAMSLPGT GSGTSSGGGN TQGQDVYIIP RPFSNFGKKL STYTKSHKFM
IFGLANNVIG PTGTGTTAVN RLLTTCLAEI PWQKLPLYMN QSEFDLLPPG SRVVECNVKV
IFRTNRIAFE TSSTVTKQAT LNQISNVQTA IGLNKLGWGI NRAFTAFQSD QPMIPTATTA
PKYEPVTGDT GYRGMIADYY GADSTNDTAF GNAGNYPHHQ VSSFTFLQNY YCMYQQTNQG
TGGWPCLAEH LQQFDSKTVN NQCLIDVTYK PKMGLIKSPL NYKIIGQPTV KGTISVGDNL
VNMRGAVVTN PPEATQNVAE STHNLTRNFP ADLFNIYSDI EKSQVLHKGP WGHENPQIQP
SVHIGIQAVP ALTTGALLIN SSPLNSWTDS MGYIDVMSSC TVMEAQPTHF PFSTEANTNP
GNTIYRINLT PNSLTSAFNG LYGNGATLGN V
