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Capsid protein VP1 (Coat protein VP1)

 CAPSD_PAVC7             Reviewed;         727 AA.
P04863;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
31-MAY-2011, sequence version 3.
25-OCT-2017, entry version 88.
RecName: Full=Capsid protein VP1;
AltName: Full=Coat protein VP1;
Canine parvovirus type 2 (strain Dog/United States/780929/-) (CPV-2).
Viruses; ssDNA viruses; Parvoviridae; Parvovirinae; Protoparvovirus.
NCBI_TaxID=10789;
NCBI_TaxID=9615; Canis lupus familiaris (Dog) (Canis familiaris).
NCBI_TaxID=9685; Felis catus (Cat) (Felis silvestris catus).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3989914;
Rhode S.L. III;
"Nucleotide sequence of the coat protein gene of canine parvovirus.";
J. Virol. 54:630-633(1985).
[2]
SEQUENCE REVISION.
Rhode S.L. III;
Submitted (JUL-1989) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 228-473.
PubMed=3942033; DOI=10.1016/0042-6822(86)90408-3;
Parrish C.R., Carmichael L.E.;
"Characterization and recombination mapping of an antigenic and host
range mutation of canine parvovirus.";
Virology 148:121-132(1986).
-!- FUNCTION: Capsid protein self-assembles to form an icosahedral
capsid with a T=1 symmetry, about 22 nm in diameter, and
consisting of 60 copies of two size variants of the capsid
proteins, VP1 and VP2, which differ by the presence of an N-
terminal extension in the minor protein VP1. The capsid
encapsulates the genomic ssDNA. Capsid proteins are responsible
for the attachment to host cell receptor TFRC. This attachment
induces virion internalization predominantly through clathrin-
endocytosis. Binding to the host receptors also induces capsid
rearrangements leading to surface exposure of VP1 N-terminus,
specifically its phospholipase A2-like region and nuclear
localization signal(s). VP1 N-terminus might serve as a lipolytic
enzyme to breach the endosomal membrane during entry into host
cell. Intracytoplasmic transport involves microtubules and
interaction between capsid proteins and host dynein. Exposure of
nuclear localization signal probably allows nuclear import of
capsids (By similarity). {ECO:0000250}.
-!- SUBUNIT: Interacts with host TFRC. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Virion {ECO:0000250}. Host nucleus
{ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=VP1;
IsoId=P04863-1; Sequence=Displayed;
Note=Minor splicing isoform.;
Name=VP2;
IsoId=P04863-2; Sequence=VSP_041136;
Note=Major splicing isoform produced by deletion of the
initiating AUG for VP1 and downstream translation of VP2.;
-!- DOMAIN: The N-terminus of VP1 is sequestered within the mature
capsid. It contains a phospholipase A2-like region and nuclear
localization signals that might be exposed by capsid modifications
during virus entry (By similarity). {ECO:0000250}.
-!- MISCELLANEOUS: The capsids of autonomous parvoviruses expose a
proportion of VP2 N-terminus and part of that sequence can be
cleaved of to form VP3. {ECO:0000250}.
-!- SIMILARITY: Belongs to the parvoviridae capsid protein family.
{ECO:0000305}.
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EMBL; M10989; AAA47149.1; -; Genomic_DNA.
EMBL; M11871; AAA47147.1; -; Genomic_DNA.
PIR; A03702; VCPVCN.
SMR; P04863; -.
PRIDE; P04863; -.
GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
GO; GO:0039615; C:T=1 icosahedral viral capsid; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
GO; GO:0075521; P:microtubule-dependent intracellular transport of viral material towards nucleus; IEA:UniProtKB-KW.
GO; GO:0039665; P:permeabilization of host organelle membrane involved in viral entry into host cell; IEA:UniProtKB-KW.
GO; GO:0099008; P:viral entry via permeabilization of inner membrane; IEA:UniProtKB-KW.
GO; GO:0075732; P:viral penetration into host nucleus; IEA:UniProtKB-KW.
GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
Gene3D; 2.170.30.10; -; 1.
InterPro; IPR016184; Capsid/spike_ssDNA_virus.
InterPro; IPR001403; Parvovirus_coat.
InterPro; IPR013607; Parvovirus_coat_VP1_N.
InterPro; IPR036952; VP1/VP2.
Pfam; PF00740; Parvo_coat; 1.
Pfam; PF08398; Parvo_coat_N; 1.
SUPFAM; SSF88645; SSF88645; 1.
3: Inferred from homology;
Alternative splicing; Capsid protein;
Clathrin-mediated endocytosis of virus by host;
Cytoplasmic inwards viral transport; Disulfide bond; Host nucleus;
Host-virus interaction; Magnesium; Metal-binding;
Microtubular inwards viral transport; T=1 icosahedral capsid protein;
Viral attachment to host cell; Viral penetration into host cytoplasm;
Viral penetration into host nucleus;
Viral penetration via permeabilization of host membrane; Virion;
Virus endocytosis by host; Virus entry into host cell.
CHAIN 1 727 Capsid protein VP1.
/FTId=PRO_0000039423.
REGION 19 64 Phospholipase A2-like. {ECO:0000250}.
MOTIF 4 13 Nuclear localization signal.
{ECO:0000255}.
COMPBIAS 165 182 Gly-rich.
METAL 323 323 Magnesium 1. {ECO:0000250}.
DISULFID 633 637 {ECO:0000250}.
VAR_SEQ 1 143 Missing (in isoform VP2). {ECO:0000305}.
/FTId=VSP_041136.
CONFLICT 414 414 K -> R (in Ref. 3; AAA47147).
{ECO:0000305}.
CONFLICT 443 444 AT -> DI (in Ref. 3; AAA47147).
{ECO:0000305}.
CONFLICT 452 452 P -> Q (in Ref. 3; AAA47147).
{ECO:0000305}.
CONFLICT 456 456 K -> R (in Ref. 3; AAA47147).
{ECO:0000305}.
CONFLICT 459 459 V -> I (in Ref. 3; AAA47147).
{ECO:0000305}.
SEQUENCE 727 AA; 80290 MW; 26D12418B199BBC6 CRC64;
MAPPAKRARR GLVPPGYKYL GPGKSLDQGE PTNPSDAAAK EHDEAYAAYL RSGKNPYLYF
SPADQRFIDQ TKDAKDWGGK IGHYFFRAKK AIAPVLTDTP DHPSTSRPTK PTKRSKPPPH
IFINLAKKKK AGAGQVKRDN LAPMSDGAVQ PDGGQPAVRN ERATGSGNGS GGGGGGGSGG
VGISTGTFNN QTEFKFLENG WVEITANSSR LVHLNMPESE KDRRVVVNNM DKTAVNGNMA
LDDIHAQIVT PWSLVDANAW GVWFNPGDWQ LIVNTMSELH LVSFEQEIFN VVLKTVSESA
TQPPTKVYNN DLTASLMVAL DSNNTMPFTP AAMRSETLGF YPWKPTIPTP WRYYFQWDRT
LIPSHTGTSG TPTNIYHGTD PDDVQFYTIE NSVPVHLLRT GDEFATGTFF FDCKPCRLTH
TWQTNRALGL PPFLNSLPQS EGATNFGDIG VPQDKKRGVT QMGNTNYITE ATIMRPAEVG
YSAPYYSFEA STQGPFKTPI AAGRGGAQTD ENQAADGNPR YAFGRQHGKK TTTTGETPER
FTYIAHQDTG RYPEGDWIQN INFNLPVTND NVLLPIDPIG GKTGINYTNI FNTYGPLTAL
NNVPPVYPNG QIWDKEFDTD LKPRLHVNAP FVCQNNCPGQ LFVKLAPNLT NEYDPDASAN
MSRIVTYSDF WWKGKLVFKA KLRASHTWNP IQQMSINVDN QFNYVPSNIG GMKIVYEKSQ
LAPRKLY


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