CAPSD_FPV19
ID CAPSD_FPV19 Reviewed; 727 AA.
AC P24840;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Capsid protein VP1;
DE AltName: Full=Coat protein VP1;
OS Feline panleukopenia virus (strain 193) (FPV).
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Quintoviricetes;
OC Piccovirales; Parvoviridae; Parvovirinae; Protoparvovirus.
OX NCBI_TaxID=10787;
OH NCBI_TaxID=9681; Felidae (cat family).
OH NCBI_TaxID=9651; Nasua nasua (Ring-tailed coati).
OH NCBI_TaxID=9654; Procyon lotor (Raccoon).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=193/70;
RX PubMed=2174965; DOI=10.1099/0022-1317-71-11-2747;
RA Martyn J.C., Davidson B.E., Studdert M.J.;
RT "Nucleotide sequence of feline panleukopenia virus: comparison with canine
RT parvovirus identifies host-specific differences.";
RL J. Gen. Virol. 71:2747-2753(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CU-4;
RX PubMed=1647068; DOI=10.1016/0042-6822(91)90132-u;
RA Parrish C.R.;
RT "Mapping specific functions in the capsid structure of canine parvovirus
RT and feline panleukopenia virus using infectious plasmid clones.";
RL Virology 183:195-205(1991).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 144-727.
RX PubMed=8392729; DOI=10.1002/prot.340160204;
RA Agbandje M., McKenna R., Rossmann M.G., Strassheim M.L., Parrish C.R.;
RT "Structure determination of feline panleukopenia virus empty particles.";
RL Proteins 16:155-171(1993).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 180-727.
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).
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 -!- SUBUNIT: Interacts with host TFRC. {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=P24840-1; Sequence=Displayed;
CC Name=VP2;
CC IsoId=P24840-2; Sequence=VSP_041146;
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 (By similarity). {ECO:0000250}.
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. {ECO:0000250}.
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 -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1fpv";
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DR EMBL; X55115; CAA38911.1; -; Genomic_DNA.
DR EMBL; M38246; AAC37928.1; -; Genomic_DNA.
DR EMBL; M38246; AAC37929.1; -; Genomic_DNA.
DR PIR; B36608; VCPVFP.
DR PDB; 1C8E; X-ray; 3.00 A; A=180-727.
DR PDB; 1C8F; X-ray; 3.00 A; A=180-727.
DR PDB; 1C8G; X-ray; 3.00 A; A=180-727.
DR PDB; 1FPV; X-ray; 3.30 A; A=144-727.
DR PDBsum; 1C8E; -.
DR PDBsum; 1C8F; -.
DR PDBsum; 1C8G; -.
DR PDBsum; 1FPV; -.
DR SMR; P24840; -.
DR EvolutionaryTrace; P24840; -.
DR Proteomes; UP000002478; 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; 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 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..727
FT /note="Capsid protein VP1"
FT /id="PRO_0000039441"
FT REGION 1..38
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 /evidence="ECO:0000250"
FT DISULFID 633..637
FT VAR_SEQ 1..143
FT /note="Missing (in isoform VP2)"
FT /evidence="ECO:0000305"
FT /id="VSP_041146"
FT STRAND 192..196
FT /evidence="ECO:0007829|PDB:1C8E"
FT STRAND 198..215
FT /evidence="ECO:0007829|PDB:1C8E"
FT STRAND 223..227
FT /evidence="ECO:0007829|PDB:1C8E"
FT HELIX 230..233
FT /evidence="ECO:0007829|PDB:1C8E"
FT HELIX 239..241
FT /evidence="ECO:0007829|PDB:1C8F"
FT STRAND 245..254
FT /evidence="ECO:0007829|PDB:1C8E"
FT HELIX 260..263
FT /evidence="ECO:0007829|PDB:1C8E"
FT HELIX 266..275
FT /evidence="ECO:0007829|PDB:1C8E"
FT STRAND 276..297
FT /evidence="ECO:0007829|PDB:1C8E"
FT TURN 302..304
FT /evidence="ECO:0007829|PDB:1C8E"
FT STRAND 307..310
FT /evidence="ECO:0007829|PDB:1C8E"
FT STRAND 316..321
FT /evidence="ECO:0007829|PDB:1C8E"
FT HELIX 331..334
FT /evidence="ECO:0007829|PDB:1C8E"
FT STRAND 349..354
FT /evidence="ECO:0007829|PDB:1C8E"
FT STRAND 358..361
FT /evidence="ECO:0007829|PDB:1C8E"
FT STRAND 374..378
FT /evidence="ECO:0007829|PDB:1C8E"
FT HELIX 381..383
FT /evidence="ECO:0007829|PDB:1C8E"
FT HELIX 389..392
FT /evidence="ECO:0007829|PDB:1C8E"
FT STRAND 395..398
FT /evidence="ECO:0007829|PDB:1C8E"
FT STRAND 416..418
FT /evidence="ECO:0007829|PDB:1C8E"
FT HELIX 425..427
FT /evidence="ECO:0007829|PDB:1C8E"
FT HELIX 453..455
FT /evidence="ECO:0007829|PDB:1C8G"
FT TURN 470..472
FT /evidence="ECO:0007829|PDB:1C8E"
FT STRAND 476..480
FT /evidence="ECO:0007829|PDB:1C8E"
FT STRAND 488..491
FT /evidence="ECO:0007829|PDB:1C8E"
FT STRAND 494..497
FT /evidence="ECO:0007829|PDB:1C8E"
FT TURN 510..512
FT /evidence="ECO:0007829|PDB:1C8G"
FT TURN 513..517
FT /evidence="ECO:0007829|PDB:1C8F"
FT STRAND 520..523
FT /evidence="ECO:0007829|PDB:1C8E"
FT TURN 525..528
FT /evidence="ECO:0007829|PDB:1C8G"
FT STRAND 539..542
FT /evidence="ECO:0007829|PDB:1C8E"
FT STRAND 547..549
FT /evidence="ECO:0007829|PDB:1C8E"
FT HELIX 553..555
FT /evidence="ECO:0007829|PDB:1C8E"
FT HELIX 569..571
FT /evidence="ECO:0007829|PDB:1C8E"
FT STRAND 575..577
FT /evidence="ECO:0007829|PDB:1C8E"
FT STRAND 579..581
FT /evidence="ECO:0007829|PDB:1FPV"
FT STRAND 582..584
FT /evidence="ECO:0007829|PDB:1C8F"
FT HELIX 587..590
FT /evidence="ECO:0007829|PDB:1C8E"
FT STRAND 613..615
FT /evidence="ECO:0007829|PDB:1C8E"
FT STRAND 619..621
FT /evidence="ECO:0007829|PDB:1C8E"
FT STRAND 630..635
FT /evidence="ECO:0007829|PDB:1C8E"
FT STRAND 640..645
FT /evidence="ECO:0007829|PDB:1C8E"
FT STRAND 655..657
FT /evidence="ECO:0007829|PDB:1C8F"
FT STRAND 666..682
FT /evidence="ECO:0007829|PDB:1C8E"
FT STRAND 687..689
FT /evidence="ECO:0007829|PDB:1C8E"
FT TURN 698..700
FT /evidence="ECO:0007829|PDB:1C8E"
FT HELIX 701..703
FT /evidence="ECO:0007829|PDB:1C8E"
FT STRAND 717..719
FT /evidence="ECO:0007829|PDB:1C8G"
FT STRAND 722..724
FT /evidence="ECO:0007829|PDB:1C8G"
SQ SEQUENCE 727 AA; 80386 MW; 648596C09B621FF5 CRC64;
MAPPAKRARR GLVPPGYKYL GPGNSLDQGE PTNPSDAAAK EHDEAYAAYL RSGKNPYLYF
SPADQRFIDQ TKDAKDWGGK IGHYFFRAKK AIAPVLTDTP DHPSTSRPTK PTKRSKPPPH
IFINLAKKKK AGAGQVKRDN LAPMSDGAVQ PDGGQPAVRN ERATGSGNGS GGGGGGGSGG
VGISTGTFNN QTEFKFLENG WVEITANSSR LVHLNMPESE NYKRVVVNNM DKTAVKGNMA
LDDIHVQIVT PWSLVDANAW GVWFNPGDWQ LIVNTMSELH LVSFEQEIFN VVLKTVSESA
TQPPTKVYNN DLTASLMVAL DSNNTMPFTP AAMRSETLGF YPWKPTIPTP WRYYFQWDRT
LIPSHTGTSG TPTNVYHGTD PDDVQFYTIE NSVPVHLLRT GDEFATGTFF FDCKPCRLTH
TWQTNRALGL PPFLNSLPQS EGATNFGDIG VQQDKRRGVT QMGNTDYITE ATIMRPAEVG
YSAPYYSFEA STQGPFKTPI AAGRGGAQTD ENQAADGDPR YAFGRQHGQK TTTTGETPER
FTYIAHQDTG RYPEGDWIQN INFNLPVTND NVLLPTDPIG GKTGINYTNI FNTYGPLTAL
NNVPPVYPNG QIWDKEFDTD LKPRLHVNAP FVCQNNCPGQ LFVKVAPNLT NEYDPDASAN
MSRIVTYSDF WWKGKLVFKA KLRASHTWNP IQQMSINVDN QFNYVPNNIG AMKIVYEKSQ
LAPRKLY
