CAPSD_PAVL3
ID CAPSD_PAVL3 Reviewed; 729 AA.
AC P36310;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Capsid protein VP1;
DE AltName: Full=Coat protein VP1;
OS Parvovirus LuIII.
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Quintoviricetes;
OC Piccovirales; Parvoviridae; Parvovirinae; Protoparvovirus.
OX NCBI_TaxID=35339;
OH NCBI_TaxID=9989; Rodentia.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8517025; DOI=10.1006/viro.1993.1040;
RA Diffoot N., Chen K.C., Bates R.C., Lederma M.;
RT "The complete nucleotide sequence of parvovirus LuIII and localization of a
RT unique sequence possibly responsible for its encapsidation pattern.";
RL Virology 192:339-345(1993).
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=P36310-1; Sequence=Displayed;
CC Name=VP2;
CC IsoId=P36310-2; Sequence=VSP_041141;
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: [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 EMBL; M81888; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; B44276; B44276.
DR PDB; 6B9Q; EM; 3.17 A; 1/2/3/4/5/6/7/8/A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V=143-729.
DR PDBsum; 6B9Q; -.
DR SMR; P36310; -.
DR Proteomes; UP000007898; Genome.
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 1: Evidence at protein level;
KW 3D-structure; 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_0000222460"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 19..64
FT /note="Phospholipase A2-like"
FT /evidence="ECO:0000250"
FT REGION 95..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 4..13
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 130..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 325
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..142
FT /note="Missing (in isoform VP2)"
FT /evidence="ECO:0000305"
FT /id="VSP_041141"
SQ SEQUENCE 729 AA; 81125 MW; 56A59A50E5BCDE43 CRC64;
MAPPAKRAKR GWVPPGYKYL GPGNSLNQGE PTNPSDAAAK EHDEAYDQYI KSGKNPYLYF
SPADQRFIDQ TKDAKDWGGK VGHYFFRTKR AFAPKLSTDS EPGTSGVSTA GKRTKPPAHI
FINQARAKKK RTSLAAQQRT QTMSDGTDQS DSGNAVQSAA RVERAADGPG GSGGGGSGGG
GVGVSTGSYD NQTHYKFLGD GWVEITAYST RMVHLNMPKS ENYCRVRVHN TNDTGTASHM
AMDDAHEQIW TPWSLVDANA WGVWFQPSDW QYISNNMIHI NLHSLDQELF NVVIKTVTEQ
NTGAEAIKVY NNDLTAAMMV ALDSNNILPY TPAIDNQETL GFYPWKPTIP SPYRYYFSCD
RNLSVTYKDE AGTITDTMGL ASGLNSQFFT IENTQRINLL RTGDEYATGT YYFDTEPIRL
THTWQTNRHL GQPPQITELP SSDTANATLT ARGYRSGLTQ IQGRNDVTEA TRVRPAQVGF
CQPHDNFETS RAGPFKVPVV PADITQGLDH DANGSLRYTY DKQHGQSWAS QNNKDRYTWD
AVNYDSGRWT NNCFIQSVPF TSEPNANQIL TNRDNLAGKT DIHFTNAFNS YGPLTAFPHP
APIYPQGQIW DKELDLEHKP RLHTQAPFVC KNNAPGQLLV RLAPNLTDQY DPNSSNLSRI
VTYGTFFWKG KLTLKAKMRP NATWNPVFQI SATNQGTNDY MSIERWLPTA TGNITNVPLL
SRPVARNTY
