CAPSD_MUMIM
ID CAPSD_MUMIM Reviewed; 729 AA.
AC P07302; Q9WMH2; Q9WMH3;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Capsid protein VP1;
DE AltName: Full=Coat protein VP1;
OS Murine minute virus (strain MVMi) (MVM) (Murine parvovirus).
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Quintoviricetes;
OC Piccovirales; Parvoviridae; Parvovirinae; Protoparvovirus.
OX NCBI_TaxID=10795;
OH NCBI_TaxID=10090; Mus musculus (Mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3502703; DOI=10.1128/jvi.57.2.656-669.1986;
RA Astell C.R., Gardiner E.M., Tattersall P.;
RT "DNA sequence of the lymphotropic variant of minute virus of mice, MVM(i),
RT and comparison with the DNA sequence of the fibrotropic prototype strain.";
RL J. Virol. 57:656-669(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3855242; DOI=10.1093/nar/13.10.3617;
RA Sahli R., McMaster G.K., Hirt B.;
RT "DNA sequence comparison between two tissue-specific variants of the
RT autonomous parvovirus, minute virus of mice.";
RL Nucleic Acids Res. 13:3617-3633(1985).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 132-718.
RX PubMed=15299974; DOI=10.1107/s0907444996010566;
RA Llamas-Saiz A.L., Agbandje-Mckenna M., Wikoff W.R., Bratton J.,
RA Tattersall P., Rossmann M.G.;
RT "Structure determination of Minute virus of mice.";
RL Acta Crystallogr. D 53:93-100(1997).
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=P07302-1; Sequence=Displayed;
CC Name=VP2;
CC IsoId=P07302-2; Sequence=VSP_041134;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA69569.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB46507.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB46508.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1mvm";
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DR EMBL; X02481; CAB46507.1; ALT_SEQ; Genomic_DNA.
DR EMBL; X02481; CAB46508.1; ALT_INIT; Genomic_DNA.
DR EMBL; M12032; AAA69569.1; ALT_SEQ; Genomic_DNA.
DR PIR; B23008; VCPVIM.
DR PDB; 1MVM; X-ray; 3.50 A; A=143-729.
DR PDB; 1Z1C; X-ray; 3.50 A; A=143-729.
DR PDB; 2XGK; X-ray; 4.20 A; A=143-729.
DR PDBsum; 1MVM; -.
DR PDBsum; 1Z1C; -.
DR PDBsum; 2XGK; -.
DR SMR; P07302; -.
DR EvolutionaryTrace; P07302; -.
DR Proteomes; UP000007783; Genome.
DR Proteomes; UP000104537; 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_0000039417"
FT REGION 1..39
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 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..154
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_041134"
FT CONFLICT 155
FT /note="A -> G (in Ref. 2; CAB46507/CAB46508)"
FT /evidence="ECO:0000305"
FT STRAND 193..197
FT /evidence="ECO:0007829|PDB:1MVM"
FT STRAND 199..215
FT /evidence="ECO:0007829|PDB:1MVM"
FT STRAND 219..222
FT /evidence="ECO:0007829|PDB:1Z1C"
FT STRAND 224..228
FT /evidence="ECO:0007829|PDB:1MVM"
FT STRAND 233..238
FT /evidence="ECO:0007829|PDB:1MVM"
FT STRAND 246..256
FT /evidence="ECO:0007829|PDB:1MVM"
FT TURN 262..264
FT /evidence="ECO:0007829|PDB:1MVM"
FT HELIX 267..276
FT /evidence="ECO:0007829|PDB:1MVM"
FT STRAND 277..280
FT /evidence="ECO:0007829|PDB:1MVM"
FT STRAND 285..300
FT /evidence="ECO:0007829|PDB:1MVM"
FT STRAND 302..305
FT /evidence="ECO:0007829|PDB:1MVM"
FT STRAND 307..312
FT /evidence="ECO:0007829|PDB:1MVM"
FT STRAND 320..323
FT /evidence="ECO:0007829|PDB:1MVM"
FT HELIX 333..336
FT /evidence="ECO:0007829|PDB:1MVM"
FT STRAND 351..356
FT /evidence="ECO:0007829|PDB:1MVM"
FT HELIX 384..386
FT /evidence="ECO:0007829|PDB:1Z1C"
FT HELIX 392..395
FT /evidence="ECO:0007829|PDB:1MVM"
FT STRAND 399..401
FT /evidence="ECO:0007829|PDB:1Z1C"
FT STRAND 406..408
FT /evidence="ECO:0007829|PDB:1Z1C"
FT STRAND 428..432
FT /evidence="ECO:0007829|PDB:1MVM"
FT STRAND 442..445
FT /evidence="ECO:0007829|PDB:1MVM"
FT HELIX 453..455
FT /evidence="ECO:0007829|PDB:1MVM"
FT STRAND 461..466
FT /evidence="ECO:0007829|PDB:1MVM"
FT TURN 469..471
FT /evidence="ECO:0007829|PDB:1MVM"
FT STRAND 475..479
FT /evidence="ECO:0007829|PDB:1MVM"
FT STRAND 490..492
FT /evidence="ECO:0007829|PDB:1MVM"
FT STRAND 493..496
FT /evidence="ECO:0007829|PDB:1Z1C"
FT TURN 505..507
FT /evidence="ECO:0007829|PDB:1MVM"
FT TURN 510..514
FT /evidence="ECO:0007829|PDB:1MVM"
FT STRAND 516..518
FT /evidence="ECO:0007829|PDB:1Z1C"
FT STRAND 538..540
FT /evidence="ECO:0007829|PDB:1Z1C"
FT HELIX 545..547
FT /evidence="ECO:0007829|PDB:1MVM"
FT STRAND 551..553
FT /evidence="ECO:0007829|PDB:1MVM"
FT STRAND 573..575
FT /evidence="ECO:0007829|PDB:1MVM"
FT STRAND 577..579
FT /evidence="ECO:0007829|PDB:1MVM"
FT TURN 586..588
FT /evidence="ECO:0007829|PDB:1MVM"
FT STRAND 605..607
FT /evidence="ECO:0007829|PDB:1MVM"
FT STRAND 628..630
FT /evidence="ECO:0007829|PDB:1Z1C"
FT STRAND 638..641
FT /evidence="ECO:0007829|PDB:1MVM"
FT STRAND 653..657
FT /evidence="ECO:0007829|PDB:1Z1C"
FT STRAND 663..679
FT /evidence="ECO:0007829|PDB:1MVM"
FT STRAND 694..702
FT /evidence="ECO:0007829|PDB:1MVM"
FT HELIX 703..705
FT /evidence="ECO:0007829|PDB:1MVM"
SQ SEQUENCE 729 AA; 80236 MW; 14F7CF9BB135717F CRC64;
MAPPAKRAKR GWVPPGYKYL GPGNSLDQGE PTNPSDAAAK EHDEAYDQYI KSGKNPYLYF
SAADQRFIDQ TKDAKDWGGK VGHYFFRTKR AFAPKLATDS EPGTSGVSRA GKRTRPPAYI
FINQARAKKK LTSSAAQQSS QTMSDGTSQP DGGNAVHSAA RVERAADGPG GSGGGGSGGG
GVGVSTGSYD NQTHYRFLGD GWVEITALAT RLVHLNMPKS ENYCRIRVHN TTDTSVKGNM
AKDDAHEQIW TPWSLVDANA WGVWLQPSDW QYICNTMSQL NLVSLDQEIF NVVLKTVTEQ
DSGGQAIKIY NNDLTACMMV AVDSNNILPY TPAANSMETL GFYPWKPTIA SPYRYYFCVD
RDLSVTYENQ EGTIEHNVMG TPKGMNSQFF TIENTQQITL LRTGDEFATG TYYFDTNPVK
LTHTWQTNRQ LGQPPLLSTF PEADTDAGTL TAQGSRHGAT QMEVNWVSEA IRTRPAQVGF
CQPHNDFEAS RAGPFAAPKV PADVTQGVDR EANGSVRYSY GKQHGENWAA HGPAPERYTW
DETNFGSGRD TRDGFIQSAP LVVPPPLNGI LTNANPIGTK NDIHFSNVFN SYGPLTAFSH
PSPVYPQGQI WDKELDLEHK PRLHITAPFV CKNNAPGQML VRLGPNLTDQ YDPNGATLSR
IVTYGTFFWK GKLTMRAKLR ANTTWNPVYQ VSVEDNGNSY MSVTKWLPTA TGNMQSVPLI
TRPVARNTY
