CAPSD_DHBV1
ID CAPSD_DHBV1 Reviewed; 262 AA.
AC P0C6J7;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 1.
DT 29-SEP-2021, entry version 54.
DE RecName: Full=Capsid protein;
DE AltName: Full=Core antigen;
DE AltName: Full=Core protein;
DE AltName: Full=HBcAg;
GN Name=C;
OS Duck hepatitis B virus (strain United States/DHBV-16) (DHBV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Blubervirales; Hepadnaviridae; Avihepadnavirus.
OX NCBI_TaxID=489543;
OH NCBI_TaxID=8835; Anas (ducks).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6699938; DOI=10.1128/jvi.49.3.782-792.1984;
RA Mandart E., Kay A., Galibert F.;
RT "Nucleotide sequence of a cloned duck hepatitis B virus genome: comparison
RT with woodchuck and human hepatitis B virus sequences.";
RL J. Virol. 49:782-792(1984).
CC -!- FUNCTION: Self assembles to form an icosahedral capsid. Most capsid
CC appear to be large particles with an icosahedral symmetry of T=4 and
CC consist of 240 copies of capsid protein, though a fraction forms
CC smaller T=3 particles consisting of 180 capsid proteins. Entering
CC capsid are transported along microtubules to the nucleus.
CC Phosphorylation of the capsid is thought to induce exposure of nuclear
CC localization signal in the C-terminal portion of the capsid protein
CC that allows binding to the nuclear pore complex via the importin
CC (karyopherin-) alpha and beta. Capsids are imported in intact form
CC through the nuclear pore into the nuclear basket, where it probably
CC binds NUP153. Only capsids that contain the mature viral genome can
CC release the viral DNA and capsid protein into the nucleoplasm. Immature
CC capsids get stucked in the basket. Capsids encapsulate the pre-genomic
CC RNA and the P protein. Pre-genomic RNA is reverse transcribed into DNA
CC while the capsid is still in the cytoplasm. The capsid can then either
CC be directed to the nucleus, providing more genome for transcription, or
CC bud through the endoplasmic reticulum to provide new virions (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimerizes, then multimerizes. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein]: Virion
CC {ECO:0000250|UniProtKB:P03148}. Host cytoplasm
CC {ECO:0000250|UniProtKB:P03148}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=Capsid protein;
CC IsoId=P0C6J7-1; Sequence=Displayed;
CC Name=External core antigen;
CC IsoId=P03154-1; Sequence=External;
CC -!- SIMILARITY: Belongs to the avihepadnavirus core antigen family.
CC {ECO:0000305}.
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DR EMBL; K01834; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PDB; 6YGH; EM; 3.70 A; A/B/C/D/E/H=1-262.
DR PDB; 6YGI; EM; 3.00 A; A/B/C/D/E/H=1-77, A/B/C/D/E/H=123-262.
DR PDBsum; 6YGH; -.
DR PDBsum; 6YGI; -.
DR SMR; P0C6J7; -.
DR Proteomes; UP000180685; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0039619; C:T=4 icosahedral viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0075521; P:microtubule-dependent intracellular transport of viral material towards nucleus; IEA:UniProtKB-KW.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0075732; P:viral penetration into host nucleus; IEA:UniProtKB-KW.
DR Gene3D; 1.10.4090.10; -; 2.
DR InterPro; IPR002006; Hepatitis_core.
DR InterPro; IPR036459; Viral_capsid_core_dom_sf_HBV.
DR Pfam; PF00906; Hepatitis_core; 1.
DR SUPFAM; SSF47852; SSF47852; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative initiation; Capsid protein;
KW Cytoplasmic inwards viral transport; DNA-binding; Host cytoplasm;
KW Host-virus interaction; Microtubular inwards viral transport;
KW Phosphoprotein; RNA-binding; T=4 icosahedral capsid protein;
KW Viral penetration into host nucleus; Virion; Virus entry into host cell.
FT CHAIN 1..262
FT /note="Capsid protein"
FT /id="PRO_0000324344"
FT REGION 183..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 254..260
FT /note="RNA binding"
FT /evidence="ECO:0000250"
FT MOTIF 215..233
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 206..220
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..235
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 232
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000250"
FT MOD_RES 245
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000250"
FT HELIX 3..9
FT /evidence="ECO:0007829|PDB:6YGI"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:6YGI"
FT STRAND 17..20
FT /evidence="ECO:0007829|PDB:6YGI"
FT HELIX 23..39
FT /evidence="ECO:0007829|PDB:6YGI"
FT HELIX 45..77
FT /evidence="ECO:0007829|PDB:6YGI"
FT HELIX 123..155
FT /evidence="ECO:0007829|PDB:6YGI"
FT HELIX 158..173
FT /evidence="ECO:0007829|PDB:6YGI"
SQ SEQUENCE 262 AA; 30284 MW; DF6A37E9E9AA2584 CRC64;
MDINASRALA NVYDLPDDFF PKIDDLVRDA KDALEPYWKS DSIKKHVLIA THFVDLIEDF
WQTTQGMHEI AESLRAVIPP TTTPVPPGYL IQHEEAEEIP LGDLFKHQEE RIVSFQPDYP
ITARIHAHLK AYAKINEESL DRARRLLWWH YNCLLWGEAQ VTNYISRLRT WLSTPEKYRG
RDAPTIEAIT RPIQVAQGGR KTTTGTRKPR GLEPRRRKVK TTVVYGRRRS KSRERRAPTP
QRAGSPLPRS SSSHHRSPSP RK
