CAPSD_MUMIP
ID CAPSD_MUMIP Reviewed; 729 AA.
AC P03137; Q84366;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 3.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Capsid protein VP1;
DE AltName: Full=Coat protein VP1;
OS Murine minute virus (strain MVM prototype) (MVM) (Murine minute virus
OS (strain MVM(p))).
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Quintoviricetes;
OC Piccovirales; Parvoviridae; Parvovirinae; Protoparvovirus.
OX NCBI_TaxID=648235;
OH NCBI_TaxID=10090; Mus musculus (Mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6298737; DOI=10.1093/nar/11.4.999;
RA Astell C.R., Thomson M., Merchlinsky M., Ward D.C.;
RT "The complete DNA sequence of minute virus of mice, an autonomous
RT parvovirus.";
RL Nucleic Acids Res. 11:999-1018(1983).
RN [2]
RP ALTERNATIVE SPLICING.
RX PubMed=3783817; DOI=10.1128/jvi.60.3.1170-1174.1986;
RA Morgan W.R., Ward D.C.;
RT "Three splicing patterns are used to excise the small intron common to all
RT minute virus of mice RNAs.";
RL J. Virol. 60:1170-1174(1986).
RN [3]
RP FUNCTION OF VP1, PHOSPHOLIPASE A2-LIKE REGION, AND NUCLEAR LOCALIZATION
RP SIGNALS.
RX PubMed=16284249; DOI=10.1073/pnas.0508477102;
RA Farr G.A., Zhang L.G., Tattersall P.;
RT "Parvoviral virions deploy a capsid-tethered lipolytic enzyme to breach the
RT endosomal membrane during cell entry.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:17148-17153(2005).
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.
CC {ECO:0000269|PubMed:16284249}.
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=P03137-1; Sequence=Displayed;
CC Name=VP2;
CC IsoId=P03137-2; Sequence=VSP_041135;
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: The capsids of autonomous parvoviruses expose a
CC proportion of VP2 N-terminus and part of that sequence can be cleaved
CC of to form VP3.
CC -!- MISCELLANEOUS: [Isoform VP1]: Minor splicing isoform.
CC -!- MISCELLANEOUS: [Isoform VP2]: Major splicing isoform (approximately 70%
CC of the molecules), produced by deletion of the initiating AUG for VP1
CC and downstream translation of VP2. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the parvoviridae capsid protein family.
CC {ECO:0000305}.
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DR EMBL; V01115; CAA24310.1; ALT_SEQ; Genomic_DNA.
DR EMBL; J02275; AAA67111.1; -; Genomic_DNA.
DR PIR; A03700; VCPV2M.
DR RefSeq; NP_041244.1; NC_001510.1.
DR RefSeq; NP_041245.1; NC_001510.1.
DR PDB; 4ZPY; X-ray; 3.80 A; A=181-729.
DR PDBsum; 4ZPY; -.
DR SMR; P03137; -.
DR GeneID; 1489591; -.
DR GeneID; 1489592; -.
DR KEGG; vg:1489591; -.
DR KEGG; vg:1489592; -.
DR Proteomes; UP000007019; 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 Reference proteome; T=1 icosahedral capsid protein;
KW Viral attachment to host cell; Viral penetration into host cytoplasm;
KW 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_0000039419"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 19..64
FT /note="Phospholipase A2-like"
FT REGION 96..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 130..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..155
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_041135"
FT CONFLICT 385..387
FT /note="MNS -> IP (in Ref. 1; CAA24310)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 729 AA; 80145 MW; CCE2686A003CB6AB CRC64;
MAPPAKRAKR GWVPPGYKYL GPGNSLDQGE PTNPSDAAAK EHDEAYDQYI KSGKNPYLYF
SAADQRFIDQ TKDAKDWGGK VGHYFFRTKR AFAPKLATDS EPGTSGVSRA GKRTRPPAYI
FINQARAKKK LTSSAAQQSS QTMSDGTSQP DSGNAVHSAA RVERAADGPG GSGGGGSGGG
GVGVSTGSYD NQTHYRFLGD GWVEITALAT RLVHLNMPKS ENYCRIRVHN TTDTSVKGNM
AKDDAHEQIW TPWSLVDANA WGVWLQPSDW QYICNTMSQL NLVSLDQEIF NVVLKTVTEQ
DLGGQAIKIY NNDLTACMMV AVDSNNILPY TPAANSMETL GFYPWKPTIA SPYRYYFCVD
RDLSVTYENQ EGTVEHNVMG TPKGMNSQFF TIENTQQITL LRTGDEFATG TYYFDTNSVK
LTHTWQTNRQ LGQPPLLSTF PEADTDAGTL TAQGSRHGTT QMGVNWVSEA IRTRPAQVGF
CQPHNDFEAS RAGPFAAPKV PADITQGVDK EANGSVRYSY GKQHGENWAS HGPAPERYTW
DETSFGSGRD TKDGFIQSAP LVVPPPLNGI LTNANPIGTK NDIHFSNVFN SYGPLTAFSH
PSPVYPQGQI WDKELDLEHK PRLHITAPFV CKNNAPGQML VRLGPNLTDQ YDPNGATLSR
IVTYGTFFWK GKLTMRAKLR ANTTWNPVYQ VSAEDNGNSY MSVTKWLPTA TGNMQSVPLI
TRPVARNTY
