CAPSD_PAVHH
ID CAPSD_PAVHH Reviewed; 734 AA.
AC P03136;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 2.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Capsid protein VP1;
DE AltName: Full=Coat protein VP1;
OS Hamster parvovirus H1.
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Quintoviricetes;
OC Piccovirales; Parvoviridae; Parvovirinae; Protoparvovirus.
OX NCBI_TaxID=10799;
OH NCBI_TaxID=36483; Cricetidae sp. (Hamster).
OH NCBI_TaxID=10116; Rattus norvegicus (Rat).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6823009; DOI=10.1128/jvi.45.1.173-184.1983;
RA Rhode S.L. III, Paradiso P.R.;
RT "Parvovirus genome: nucleotide sequence of H-1 and mapping of its genes by
RT hybrid-arrested translation.";
RL J. Virol. 45:173-184(1983).
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=P03136-1; Sequence=Displayed;
CC Name=VP2;
CC IsoId=P03136-2; Sequence=VSP_041140;
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: [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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X01457; CAB57285.1; ALT_SEQ; Genomic_DNA.
DR PIR; A03699; VCPVV2.
DR PDB; 4G0R; X-ray; 2.70 A; A=1-734.
DR PDB; 4GBT; X-ray; 3.20 A; A=1-734.
DR PDBsum; 4G0R; -.
DR PDBsum; 4GBT; -.
DR SMR; P03136; -.
DR Proteomes; UP000007897; 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..734
FT /note="Capsid protein VP1"
FT /id="PRO_0000039431"
FT REGION 1..42
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..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 134..154
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 135..154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 328
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_041140"
FT STRAND 192..198
FT /evidence="ECO:0007829|PDB:4G0R"
FT STRAND 201..215
FT /evidence="ECO:0007829|PDB:4G0R"
FT STRAND 218..221
FT /evidence="ECO:0007829|PDB:4GBT"
FT STRAND 223..227
FT /evidence="ECO:0007829|PDB:4G0R"
FT STRAND 232..235
FT /evidence="ECO:0007829|PDB:4GBT"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:4GBT"
FT HELIX 243..245
FT /evidence="ECO:0007829|PDB:4G0R"
FT STRAND 248..257
FT /evidence="ECO:0007829|PDB:4G0R"
FT HELIX 263..266
FT /evidence="ECO:0007829|PDB:4G0R"
FT HELIX 269..278
FT /evidence="ECO:0007829|PDB:4G0R"
FT STRAND 279..301
FT /evidence="ECO:0007829|PDB:4G0R"
FT STRAND 311..315
FT /evidence="ECO:0007829|PDB:4G0R"
FT STRAND 321..325
FT /evidence="ECO:0007829|PDB:4G0R"
FT HELIX 336..339
FT /evidence="ECO:0007829|PDB:4G0R"
FT STRAND 354..360
FT /evidence="ECO:0007829|PDB:4G0R"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:4G0R"
FT STRAND 381..383
FT /evidence="ECO:0007829|PDB:4G0R"
FT HELIX 388..390
FT /evidence="ECO:0007829|PDB:4G0R"
FT HELIX 396..399
FT /evidence="ECO:0007829|PDB:4G0R"
FT STRAND 403..405
FT /evidence="ECO:0007829|PDB:4G0R"
FT STRAND 426..428
FT /evidence="ECO:0007829|PDB:4GBT"
FT HELIX 432..434
FT /evidence="ECO:0007829|PDB:4G0R"
FT STRAND 441..443
FT /evidence="ECO:0007829|PDB:4GBT"
FT TURN 457..459
FT /evidence="ECO:0007829|PDB:4G0R"
FT TURN 474..476
FT /evidence="ECO:0007829|PDB:4G0R"
FT STRAND 480..484
FT /evidence="ECO:0007829|PDB:4G0R"
FT STRAND 492..495
FT /evidence="ECO:0007829|PDB:4G0R"
FT STRAND 498..501
FT /evidence="ECO:0007829|PDB:4G0R"
FT TURN 510..513
FT /evidence="ECO:0007829|PDB:4G0R"
FT HELIX 516..518
FT /evidence="ECO:0007829|PDB:4G0R"
FT STRAND 521..525
FT /evidence="ECO:0007829|PDB:4G0R"
FT HELIX 527..529
FT /evidence="ECO:0007829|PDB:4G0R"
FT STRAND 541..545
FT /evidence="ECO:0007829|PDB:4G0R"
FT STRAND 550..552
FT /evidence="ECO:0007829|PDB:4GBT"
FT HELIX 556..558
FT /evidence="ECO:0007829|PDB:4G0R"
FT STRAND 560..562
FT /evidence="ECO:0007829|PDB:4GBT"
FT HELIX 572..574
FT /evidence="ECO:0007829|PDB:4G0R"
FT STRAND 575..580
FT /evidence="ECO:0007829|PDB:4GBT"
FT HELIX 590..592
FT /evidence="ECO:0007829|PDB:4G0R"
FT TURN 610..612
FT /evidence="ECO:0007829|PDB:4GBT"
FT STRAND 622..624
FT /evidence="ECO:0007829|PDB:4G0R"
FT STRAND 633..635
FT /evidence="ECO:0007829|PDB:4G0R"
FT STRAND 644..648
FT /evidence="ECO:0007829|PDB:4G0R"
FT STRAND 668..684
FT /evidence="ECO:0007829|PDB:4G0R"
FT HELIX 708..711
FT /evidence="ECO:0007829|PDB:4G0R"
FT STRAND 729..731
FT /evidence="ECO:0007829|PDB:4GBT"
SQ SEQUENCE 734 AA; 81053 MW; 0AA6B088729203F8 CRC64;
MAPPAKRAKR GWVPPGYKYL GPGNSLDQGE PTNPSDAAAK EHDEAYDQYI KSGKNPYLYF
SPADQRFIDQ TKDAKDWGGK VGHYFFRTKR AFAPKLSTDS EPGTSGVSRP GKRTKPPAHI
FVNQARAKKK RASLAAQQRT LTMSDGTETN QPDTGIANAR VERSADGGGS SGGGGSGGGG
IGVSTGTYDN QTTYKFLGDG WVEITAHASR LLHLGMPPSE NYCRVTVHNN QTTGHGTKVK
GNMAYDTHQQ IWTPWSLVDA NAWGVWFQPS DWQFIQNSME SLNLDSLSQE LFNVVVKTVT
EQQGAGQDAI KVYNNDLTAC MMVALDSNNI LPYTPAAQTS ETLGFYPWKP TAPAPYRYYF
FMPRQLSVTS SNSAEGTQIT DTIGEPQALN SQFFTIENTL PITLLRTGDE FTTGTYIFNT
DPLKLTHTWQ TNRHLACLQG ITDLPTSDTA TASLTANGDR FGSTQTQNVN YVTEALRTRP
AQIGFMQPHD NFEANRGGPF KVPVVPLDIT AGEDHDANGA IRFNYGKQHG EDWAKQGAAP
ERYTWDAIDS AAGRDTARCF VQSAPISIPP NQNQILQRED AIAGRTNMHY TNVFNSYGPL
SAFPHPDPIY PNGQIWDKEL DLEHKPRLHV TAPFVCKNNP PGQLFVHLGP NLTDQFDPNS
TTVSRIVTYS TFYWKGILKF KAKLRPNLTW NPVYQATTDS VANSYMNVKK WLPSATGNMH
SDPLICRPVP HMTY
