CAPSD_PAVCD
ID CAPSD_PAVCD Reviewed; 727 AA.
AC P17455; P30129; Q6LDR5; Q84389;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Capsid protein VP1;
DE AltName: Full=Coat protein VP1;
OS Canine parvovirustype 2 (isolate Dog/United States/CPV-d/1988) (CPV-2).
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Quintoviricetes;
OC Piccovirales; Parvoviridae; Parvovirinae; Protoparvovirus.
OX NCBI_TaxID=10790;
OH NCBI_TaxID=9615; Canis lupus familiaris (Dog) (Canis familiaris).
OH NCBI_TaxID=9685; Felis catus (Cat) (Felis silvestris catus).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3176341; DOI=10.1016/0042-6822(88)90500-4;
RA Parrish C.R., Aquadro C.F., Carmichael L.E.;
RT "Canine host range and a specific epitope map along with variant sequences
RT in the capsid protein gene of canine parvovirus and related feline, mink,
RT and raccoon parvoviruses.";
RL Virology 166:293-307(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 234-727.
RC STRAIN=Y1;
RX PubMed=8207398; DOI=10.1099/0022-1317-75-6-1319;
RA Horiuchi M., Goto H., Ishiguro N., Shinagawa M.;
RT "Mapping of determinants of the host range for canine cells in the genome
RT of canine parvovirus using canine parvovirus/mink enteritis virus chimeric
RT viruses.";
RL J. Gen. Virol. 75:1319-1328(1994).
RN [3]
RP FUNCTION, AND NUCLEAR LOCALIZATION SIGNAL.
RX PubMed=11799183; DOI=10.1128/jvi.76.4.1884-1891.2002;
RA Vihinen-Ranta M., Wang D., Weichert W.S., Parrish C.R.;
RT "The VP1 N-terminal sequence of canine parvovirus affects nuclear transport
RT of capsids and efficient cell infection.";
RL J. Virol. 76:1884-1891(2002).
RN [4]
RP FUNCTION.
RX PubMed=12970411; DOI=10.1128/jvi.77.19.10270-10279.2003;
RA Suikkanen S., Aaltonen T., Nevalainen M., Valilehto O., Lindholm L.,
RA Vuento M., Vihinen-Ranta M.;
RT "Exploitation of microtubule cytoskeleton and dynein during parvoviral
RT traffic toward the nucleus.";
RL J. Virol. 77:10270-10279(2003).
RN [5]
RP FUNCTION, AND INTERACTION WITH CANINE TFRC.
RX PubMed=19656887; DOI=10.1128/jvi.00295-09;
RA Harbison C.E., Lyi S.M., Weichert W.S., Parrish C.R.;
RT "Early steps in cell infection by parvoviruses: host-specific differences
RT in cell receptor binding but similar endosomal trafficking.";
RL J. Virol. 83:10504-10514(2009).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS).
RX PubMed=2006420; DOI=10.1126/science.2006420;
RA Tsao J., Chapman M.S., Agbandje M., Keller W., Smith K., Wu H., Luo M.,
RA Smith T.J., Rossmann M.G., Compans R.W., Parish C.R.;
RT "The three-dimensional structure of canine parvovirus and its functional
RT implications.";
RL Science 251:1456-1464(1991).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS) OF 1-584.
RX PubMed=8918534; DOI=10.1006/viro.1996.0575;
RA Llamas-Saiz A.L., Agbandje-McKenna M., Parker J.S., Wahid A.T.,
RA Parrish C.R., Rossmann M.G.;
RT "Structural analysis of a mutation in canine parvovirus which controls
RT antigenicity and host range.";
RL Virology 225:65-71(1996).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 154-737.
RX PubMed=8969301; DOI=10.1006/jmbi.1996.0657;
RA Xie Q., Chapman M.S.;
RT "Canine parvovirus capsid structure, analyzed at 2.9 A resolution.";
RL J. Mol. Biol. 264:497-520(1996).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS).
RX PubMed=10884355; DOI=10.1006/jmbi.2000.3868;
RA Simpson A.A., Chandrasekar V., Hebert B., Sullivan G.M., Rossmann M.G.,
RA Parrish C.R.;
RT "Host range and variability of calcium binding by surface loops in the
RT capsids of canine and feline parvoviruses.";
RL J. Mol. Biol. 300:597-610(2000).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 37-737.
RX PubMed=14581558; DOI=10.1128/jvi.77.22.12211-12221.2003;
RA Govindasamy L., Hueffer K., Parrish C.R., Agbandje-McKenna M.;
RT "Structures of host range-controlling regions of the capsids of canine and
RT feline parvoviruses and mutants.";
RL J. Virol. 77:12211-12221(2003).
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 receptor TFRC. This
CC attachment induces virion internalization predominantly through
CC clathrin-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 nuclear localization
CC signal(s). VP1 N-terminus might serve as a lipolytic enzyme to breach
CC the endosomal membrane during entry into host cell (By similarity).
CC Intracytoplasmic transport involves microtubules and interaction
CC between capsid proteins and host dynein. Exposure of nuclear
CC localization signal probably allows nuclear import of capsids.
CC {ECO:0000250, ECO:0000269|PubMed:11799183, ECO:0000269|PubMed:12970411,
CC ECO:0000269|PubMed:19656887}.
CC -!- SUBUNIT: Interacts with host TFRC. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Virion. Host nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=VP1;
CC IsoId=P17455-1; Sequence=Displayed;
CC Name=VP2;
CC IsoId=P17455-2; Sequence=VSP_041137;
CC -!- DOMAIN: The N-terminus of VP1 is sequestered within the mature capsid.
CC It contains a phospholipase A2-like region and nuclear localization
CC signals that might be exposed by capsid modifications during virus
CC entry.
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 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA47158.1; Type=Erroneous gene model prediction; 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=1p5w";
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral empty
CC capsid structure;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=2cas";
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=4dpv";
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral empty
CC capsid structure at pH 5,5;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1c8h";
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DR EMBL; M23255; AAA47158.1; ALT_SEQ; Genomic_DNA.
DR EMBL; M23255; AAA47159.1; -; Genomic_DNA.
DR EMBL; D26081; BAA05075.1; -; Genomic_DNA.
DR PIR; A31163; VCPVCD.
DR PDB; 1C8D; X-ray; 3.00 A; A=144-727.
DR PDB; 1C8H; X-ray; 3.50 A; A=144-727.
DR PDB; 1IJS; X-ray; 3.25 A; P=144-727.
DR PDB; 1P5W; X-ray; 3.30 A; A=180-727.
DR PDB; 1P5Y; X-ray; 3.20 A; A=180-727.
DR PDB; 4DPV; X-ray; 2.90 A; Z=144-727.
DR PDBsum; 1C8D; -.
DR PDBsum; 1C8H; -.
DR PDBsum; 1IJS; -.
DR PDBsum; 1P5W; -.
DR PDBsum; 1P5Y; -.
DR PDBsum; 4DPV; -.
DR SMR; P17455; -.
DR ABCD; P17455; 9 sequenced antibodies.
DR EvolutionaryTrace; P17455; -.
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:0098671; P:adhesion receptor-mediated virion attachment to host cell; IEA:UniProtKB-KW.
DR GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
DR GO; GO:0098670; P:entry receptor-mediated virion attachment to 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 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; Disulfide bond; Host nucleus;
KW Host-virus interaction; Magnesium; Metal-binding;
KW Microtubular inwards viral transport; T=1 icosahedral capsid protein;
KW Viral attachment to host adhesion receptor; Viral attachment to host cell;
KW Viral attachment to host entry receptor;
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..727
FT /note="Capsid protein VP1"
FT /id="PRO_0000039425"
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 95..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 141..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 4..13
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT BINDING 323
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT DISULFID 633..637
FT VAR_SEQ 1..143
FT /note="Missing (in isoform VP2)"
FT /evidence="ECO:0000305"
FT /id="VSP_041137"
FT VARIANT 244
FT /note="I -> T (in strain: Y1)"
FT STRAND 192..196
FT /evidence="ECO:0007829|PDB:4DPV"
FT STRAND 200..215
FT /evidence="ECO:0007829|PDB:4DPV"
FT STRAND 223..227
FT /evidence="ECO:0007829|PDB:4DPV"
FT HELIX 230..234
FT /evidence="ECO:0007829|PDB:4DPV"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:1P5W"
FT HELIX 239..241
FT /evidence="ECO:0007829|PDB:4DPV"
FT STRAND 245..254
FT /evidence="ECO:0007829|PDB:4DPV"
FT HELIX 260..263
FT /evidence="ECO:0007829|PDB:4DPV"
FT HELIX 266..275
FT /evidence="ECO:0007829|PDB:4DPV"
FT STRAND 276..297
FT /evidence="ECO:0007829|PDB:4DPV"
FT TURN 302..304
FT /evidence="ECO:0007829|PDB:1C8D"
FT STRAND 307..310
FT /evidence="ECO:0007829|PDB:4DPV"
FT STRAND 316..320
FT /evidence="ECO:0007829|PDB:4DPV"
FT HELIX 331..334
FT /evidence="ECO:0007829|PDB:4DPV"
FT STRAND 349..355
FT /evidence="ECO:0007829|PDB:4DPV"
FT STRAND 358..361
FT /evidence="ECO:0007829|PDB:4DPV"
FT STRAND 374..378
FT /evidence="ECO:0007829|PDB:4DPV"
FT HELIX 381..383
FT /evidence="ECO:0007829|PDB:4DPV"
FT HELIX 389..392
FT /evidence="ECO:0007829|PDB:4DPV"
FT STRAND 396..398
FT /evidence="ECO:0007829|PDB:4DPV"
FT STRAND 404..410
FT /evidence="ECO:0007829|PDB:1C8H"
FT STRAND 416..418
FT /evidence="ECO:0007829|PDB:1P5Y"
FT STRAND 419..421
FT /evidence="ECO:0007829|PDB:4DPV"
FT HELIX 425..427
FT /evidence="ECO:0007829|PDB:4DPV"
FT STRAND 440..442
FT /evidence="ECO:0007829|PDB:1C8D"
FT TURN 453..455
FT /evidence="ECO:0007829|PDB:4DPV"
FT TURN 470..472
FT /evidence="ECO:0007829|PDB:4DPV"
FT STRAND 476..480
FT /evidence="ECO:0007829|PDB:4DPV"
FT STRAND 488..491
FT /evidence="ECO:0007829|PDB:4DPV"
FT STRAND 494..497
FT /evidence="ECO:0007829|PDB:4DPV"
FT TURN 507..512
FT /evidence="ECO:0007829|PDB:4DPV"
FT HELIX 513..516
FT /evidence="ECO:0007829|PDB:1C8D"
FT STRAND 520..523
FT /evidence="ECO:0007829|PDB:4DPV"
FT HELIX 525..527
FT /evidence="ECO:0007829|PDB:4DPV"
FT STRAND 539..542
FT /evidence="ECO:0007829|PDB:4DPV"
FT HELIX 553..555
FT /evidence="ECO:0007829|PDB:4DPV"
FT HELIX 569..571
FT /evidence="ECO:0007829|PDB:4DPV"
FT STRAND 575..577
FT /evidence="ECO:0007829|PDB:4DPV"
FT STRAND 579..581
FT /evidence="ECO:0007829|PDB:1IJS"
FT STRAND 582..586
FT /evidence="ECO:0007829|PDB:1P5W"
FT HELIX 587..589
FT /evidence="ECO:0007829|PDB:4DPV"
FT STRAND 613..615
FT /evidence="ECO:0007829|PDB:4DPV"
FT STRAND 619..621
FT /evidence="ECO:0007829|PDB:4DPV"
FT STRAND 630..635
FT /evidence="ECO:0007829|PDB:4DPV"
FT STRAND 641..645
FT /evidence="ECO:0007829|PDB:4DPV"
FT STRAND 657..659
FT /evidence="ECO:0007829|PDB:4DPV"
FT STRAND 666..682
FT /evidence="ECO:0007829|PDB:4DPV"
FT STRAND 687..689
FT /evidence="ECO:0007829|PDB:4DPV"
FT TURN 698..700
FT /evidence="ECO:0007829|PDB:4DPV"
FT HELIX 701..704
FT /evidence="ECO:0007829|PDB:4DPV"
FT STRAND 717..719
FT /evidence="ECO:0007829|PDB:1C8D"
FT STRAND 722..724
FT /evidence="ECO:0007829|PDB:4DPV"
SQ SEQUENCE 727 AA; 80343 MW; 115F3E1A79098EBE CRC64;
MAPPAKRARR GLVPPGYKYL GPGNSLDQGE PTNPSDAAAK EHDEAYAAYL RSGKNPYLYF
SPADQRFIDQ TKDAKDWGGK IGHYFFRAKK AIAPVLTDTP DHPSTSRPTK PTKRSKPPPH
IFINLAKKKK AGAGQVKRDN LAPMSDGAVQ PDGGQPAVRN ERATGSGNGS GGGGGGGSGG
VGISTGTFNN QTEFKFLENG WVEITANSSR LVHLNMPESE NYRRVVVNNM DKTAVNGNMA
LDDIHAQIVT PWSLVDANAW GVWFNPGDWQ LIVNTMSELH LVSFEQEIFN VVLKTVSESA
TQPPTKVYNN DLTASLMVAL DSNNTMPFTP AAMRSETLGF YPWKPTIPTP WRYYFQWDRT
LIPSHTGTSG TPTNIYHGTD PDDVQFYTIE NSVPVHLLRT GDEFATGTFF FDCKPCRLTH
TWQTNRALGL PPFLNSLPQS EGATNFGDIG VQQDKRRGVT QMGNTNYITE ATIMRPAEVG
YSAPYYSFEA STQGPFKTPI AAGRGGAQTD ENQAADGNPR YAFGRQHGQK TTTTGETPER
FTYIAHQDTG RYPEGDWIQN INFNLPVTND NVLLPTDPIG GKTGINYTNI FNTYGPLTAL
NNVPPVYPNG QIWDKEFDTD LKPRLHVNAP FVCQNNCPGQ LFVKVAPNLT NEYDPDASAN
MSRIVTYSDF WWKGKLVFKA KLRASHTWNP IQQMSINVDN QFNYVPSNIG GMKIVYEKSQ
LAPRKLY
