CAPSD_FPV
ID CAPSD_FPV Reviewed; 727 AA.
AC P04864; Q65112;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Capsid protein VP1;
DE AltName: Full=Coat protein VP1;
OS Feline panleukopenia virus (FPV).
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Quintoviricetes;
OC Piccovirales; Parvoviridae; Parvovirinae; Protoparvovirus.
OX NCBI_TaxID=10786;
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].
RX PubMed=2991581; DOI=10.1128/jvi.55.3.574-582.1985;
RA Carlson J., Rushlow K., Maxwell I., Maxwell F., Winston S., Hahn W.;
RT "Cloning and sequence of DNA encoding structural proteins of the autonomous
RT parvovirus feline panleukopenia virus.";
RL J. Virol. 55:574-582(1985).
RN [2]
RP FUNCTION, AND INTERACTION WITH FELINE 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).
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-dependent endocytosis. Binding to the host receptors also
CC induces capsid rearrangements leading to surface exposure of VP1 N-
CC terminus (By similarity). {ECO:0000250, ECO:0000269|PubMed:19656887}.
CC -!- SUBUNIT: Interacts with host TFRC. {ECO:0000269|PubMed:19656887}.
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=P04864-1; Sequence=Displayed;
CC Name=VP2;
CC IsoId=P04864-2; Sequence=VSP_041145;
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 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}.
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DR EMBL; M10824; AAA47161.1; -; Genomic_DNA.
DR EMBL; M10824; AAA47162.1; -; Genomic_DNA.
DR PIR; A03701; VCPV1F.
DR SMR; P04864; -.
DR ABCD; P04864; 7 sequenced antibodies.
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 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_0000039439"
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..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 507..536
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 /evidence="ECO:0000250"
FT VAR_SEQ 1..143
FT /note="Missing (in isoform VP2)"
FT /evidence="ECO:0000305"
FT /id="VSP_041145"
SQ SEQUENCE 727 AA; 80344 MW; 77E0F6FE554C0C6E CRC64;
MAPPAKRARR GLVPPGYKYL GPGNSLDQGE PTNPSDAAAK EHDEAYAAYL RSGKNPYLYF
SPADQRFIDQ TKDATDWGGK IGHYFFRAKK AIAPVLTDTP DHPSTSRPTK PTKRSKPPPH
IFINLAKKKK AGAGQVKRDN QAPMSDGAVQ PDGGQPAVRN ERATGSGNGS GGGGGGGSGG
VGISTGTFNN QTEFKFLENG WVEITANSSR LVHLNMPESE NYKRVVVNNM DKTAVKGNMA
LDDTHVQIVT PWSLVDANAW GVWFNPGDWQ LIVNTMSELH LVSFEQEIFN VVLKTVSESA
TQPPTKVYNN DLTASLMVAL DSNNTMPFTP AAMRSETLGF YPWKPTIPTP WRYYFQWDRT
LIPSHTGTSG TPTNIYHGTD PDDVQFYTIE NSVPVHLLRT GDEFATGTFF FDCKPCRLTH
TWQTNRALGL PPFLNSLPQS EGATNFGDIG VQQDKRRGVT QMGNTDYITE ATIMRPAEVG
YSAPYYSFEA STQGPFKIPI AAGRGGAQTD ENQAADGDPR YAFGRQHGQK TTTTGETPER
FTYIAHQDTG RYPAGDWIQN INFNLPVTND NVLLPTDPIG GKTGINYTNI FNTYGPLTAL
NNVPPVYPNG QIWDKEFDTD LKPRLHVNAP FVCQNNCPGQ LFVKVAPNLT NEYDPDASAN
MSRIVTYSDF WWKGKLVFKA KLRASHTWNP IQQMSINVDN QFNYLPNNIG AMKIVYEKSQ
LAPRKLY
