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Capsid protein (Core antigen) (Core protein) (HBcAg) (p21.5)
A0A144HXY0_HBV Unreviewed; 183 AA.
A0A144HXY0;
08-JUN-2016, integrated into UniProtKB/TrEMBL.
08-JUN-2016, sequence version 1.
13-FEB-2019, entry version 14.
RecName: Full=Capsid protein {ECO:0000256|HAMAP-Rule:MF_04076};
AltName: Full=Core antigen {ECO:0000256|HAMAP-Rule:MF_04076};
AltName: Full=Core protein {ECO:0000256|HAMAP-Rule:MF_04076};
AltName: Full=HBcAg {ECO:0000256|HAMAP-Rule:MF_04076};
AltName: Full=p21.5 {ECO:0000256|HAMAP-Rule:MF_04076};
Name=C {ECO:0000256|HAMAP-Rule:MF_04076, ECO:0000313|EMBL:AMS75088.1};
Hepatitis B virus (HBV).
Viruses; Retro-transcribing viruses; Hepadnaviridae;
Orthohepadnavirus.
NCBI_TaxID=10407 {ECO:0000313|EMBL:AMS75088.1, ECO:0000313|Proteomes:UP000159686};
NCBI_TaxID=9606; Homo sapiens (Human).
NCBI_TaxID=9598; Pan troglodytes (Chimpanzee).
[1] {ECO:0000313|EMBL:AMS75088.1, ECO:0000313|Proteomes:UP000159686}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=IND-DIB-RMRC-2052 {ECO:0000313|EMBL:AMS75088.1};
Borkakoty B.;
"Circulation of genotype-I hepatitis B virus in Dibang Valley,
Arunachal Pradesh.";
Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Encapsidates hepatitis delta genome. {ECO:0000256|HAMAP-
Rule:MF_04076}.
-!- FUNCTION: Self assembles to form an icosahedral capsid. Most
capsid appear to be large particles with a icosahedral symmetry of
T=4 and consist of 240 copies of capsid protein, though a fraction
forms smaller T=3 particles consisting of 180 capsid proteins.
Entering capsid are transported along microtubules to the nucleus.
Phosphorylation of the capsid is thought to induce exposure of
nuclear localization signal in the C-terminal portion of the
capsid protein that allows binding to the nuclear pore complex via
the importin (karyopherin-) alpha and beta. Capsids are imported
in intact form through the nuclear pore into the nuclear basket,
where it probably binds NUP153. Only capsids that contain the
mature viral genome can release the viral DNA and capsid protein
into the nucleoplasm. Immature capsids get stucked in the basket.
Capsids encapsulate the pre-genomic RNA and the P protein. Pre-
genomic RNA is reverse transcribed into DNA while the capsid is
still in the cytoplasm. The capsid can then either be directed to
the nucleus, providing more genome for transcription, or bud
through the endoplasmic reticulum to provide new virions.
{ECO:0000256|HAMAP-Rule:MF_04076}.
-!- SUBUNIT: Homodimerizes, then multimerizes. Interacts with cytosol
exposed regions of viral L glycoprotein present in the reticulum-
to-Golgi compartment. Interacts with human FLNB. Phosphorylated
form interacts with host importin alpha; this interaction depends
on the exposure of the NLS, which itself depends upon genome
maturation and/or phosphorylation of the capsid protein. Interacts
with host NUP153. {ECO:0000256|HAMAP-Rule:MF_04076}.
-!- SUBCELLULAR LOCATION: Virion {ECO:0000256|HAMAP-Rule:MF_04076}.
Host cytoplasm {ECO:0000256|HAMAP-Rule:MF_04076}.
-!- PTM: Phosphorylated by host SRPK1, SRPK2, and maybe protein kinase
C or GAPDH. Phosphorylation is critical for pregenomic RNA
packaging. Protein kinase C phosphorylation is stimulated by HBx
protein and may play a role in transport of the viral genome to
the nucleus at the late step during viral replication cycle.
{ECO:0000256|HAMAP-Rule:MF_04076}.
-!- SIMILARITY: Belongs to the orthohepadnavirus core antigen family.
{ECO:0000256|HAMAP-Rule:MF_04076}.
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EMBL; KU950741; AMS75088.1; -; Genomic_DNA.
Proteomes; UP000159686; Genome.
GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0039619; C:T=4 icosahedral viral capsid; IEA:UniProtKB-UniRule.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
GO; GO:0005198; F:structural molecule activity; IEA:UniProtKB-UniRule.
GO; GO:0075521; P:microtubule-dependent intracellular transport of viral material towards nucleus; IEA:UniProtKB-UniRule.
GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-UniRule.
GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-UniRule.
GO; GO:0075732; P:viral penetration into host nucleus; IEA:UniProtKB-UniRule.
Gene3D; 1.10.4090.10; -; 1.
HAMAP; MF_04076; HBV_HBEAG; 1.
InterPro; IPR002006; Hepatitis_core.
InterPro; IPR036459; Viral_capsid_core_dom_sf_HBV.
Pfam; PF00906; Hepatitis_core; 3.
SUPFAM; SSF47852; SSF47852; 1.
3: Inferred from homology;
Capsid protein {ECO:0000256|HAMAP-Rule:MF_04076};
Complete proteome {ECO:0000313|Proteomes:UP000159686};
Cytoplasmic inwards viral transport {ECO:0000256|HAMAP-Rule:MF_04076};
DNA-binding {ECO:0000256|HAMAP-Rule:MF_04076};
Host cytoplasm {ECO:0000256|HAMAP-Rule:MF_04076};
Host-virus interaction {ECO:0000256|HAMAP-Rule:MF_04076};
Microtubular inwards viral transport {ECO:0000256|HAMAP-
Rule:MF_04076}; Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_04076};
Repeat {ECO:0000256|HAMAP-Rule:MF_04076,
ECO:0000256|SAAS:SAAS00779256};
RNA-binding {ECO:0000256|HAMAP-Rule:MF_04076};
T=4 icosahedral capsid protein {ECO:0000256|HAMAP-Rule:MF_04076};
Viral penetration into host nucleus {ECO:0000256|HAMAP-Rule:MF_04076};
Virion {ECO:0000256|HAMAP-Rule:MF_04076};
Virus entry into host cell {ECO:0000256|HAMAP-Rule:MF_04076}.
REGION 177 183 RNA binding. {ECO:0000256|HAMAP-
Rule:MF_04076}.
MOTIF 158 175 Bipartite nuclear localization signal.
{ECO:0000256|HAMAP-Rule:MF_04076}.
MOD_RES 155 155 Phosphoserine; by host.
{ECO:0000256|HAMAP-Rule:MF_04076}.
MOD_RES 162 162 Phosphoserine; by host.
{ECO:0000256|HAMAP-Rule:MF_04076}.
MOD_RES 170 170 Phosphoserine; by host.
{ECO:0000256|HAMAP-Rule:MF_04076}.
SEQUENCE 183 AA; 21046 MW; 5A7294EA8EE61460 CRC64;
MDIDPYKEFG ASVELLSFLP SDFFPSIRDL LDTASALYRE ALESPEHCSP HHTALRQAVL
CWGELMTLAT WVGSNLEDPA SRDLVVSYVN VNMGLKIRQL LWFHISCLTF GRETVLEYLV
SFGVWIRTPP AYRPSNAPIL STLPETCVVR RRGRSPRRRT PSPRRRRSQS PRRRRSQSRE
SQC
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Pathways :
WP1049: G Protein Signaling Pathways
WP114: Core lipid-linked oligosaccharide biosynthesis
WP1165: G Protein Signaling Pathways
WP1371: G Protein Signaling Pathways
WP1438: Influenza A virus infection
WP1493: Carbon assimilation C4 pathway
WP1502: Mitochondrial biogenesis
WP1531: Vitamin D synthesis
WP1566: Citrate cycle (TCA cycle)
WP1613: 1,4-Dichlorobenzene degradation
WP1616: ABC transporters
WP1624: Bacterial secretion system
WP1625: Base excision repair
WP1644: DNA replication
WP1650: Fluorobenzoate degradation
WP1654: gamma-Hexachlorocyclohexane degradation
WP1657: Glycerolipid metabolism
WP1659: Glycine, serine and threonine metabolism
WP1661: Glyoxylate and dicarboxylate metabolism
WP1663: Homologous recombination
WP1665: Limonene and pinene degradation
WP1672: Mismatch repair
WP1673: Naphthalene and anthracene degradation
WP1675: Nitrogen metabolism
WP1676: Non-homologous end-joining
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