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P03146 (CAPSD_HBVD3) Reviewed, UniProtKB/Swiss-Prot

Last modified May 31, 2011. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Capsid protein
Alternative name(s):
Core antigen
Core protein
HBcAg
p21.5
Gene names
Name:C
OrganismHepatitis B virus genotype D subtype ayw (isolate France/Tiollais/1979) (HBV-D) [Complete proteome]
Taxonomic identifier490133 [NCBI]
Taxonomic lineageVirusesRetro-transcribing virusesHepadnaviridaeOrthohepadnavirus
Virus hostPan troglodytes (Chimpanzee) [TaxID: 9598]
Homo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length183 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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 By similarity.

Encapsidates hepatitis delta genome By similarity.

Subunit structure

Homodimerizes, then multimerizes. Interacts with cytosol exposed regions of viral L glycoprotein present in the reticulum-to-Golgi compartment. Interacts with human FLNB By similarity.

Subcellular location

Capsid protein: Virion. Host cytoplasm By similarity.

Post-translational modification

Phosphorylated by host SRPK1, SRPK2, and maybe protein kinase A, 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. Protein kinase A phosphorylation may promote capsid assembly By similarity. Ref.4 Ref.6

Sequence similarities

Belongs to the orthohepadnavirus core antigen family.

Sequence caution

The sequence CAA24706.1 differs from that shown. Reason: Erroneous initiation.

Alternative products

This entry describes 2 isoforms produced by alternative initiation. [Align] [Select]
Isoform Capsid protein (identifier: P03146-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform External core antigen (identifier: P0C573-1)

The sequence of this isoform can be found in the external entry P0C573.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 183183Capsid protein
PRO_0000222315

Regions

Repeat155 – 16171; half-length
Repeat162 – 16982
Repeat170 – 17783
Region155 – 177233 X 8 AA repeats of S-P-R-R-R-[PR]-S-Q
Region177 – 1837RNA binding By similarity
Motif158 – 17518Bipartite nuclear localization signal Potential

Amino acid modifications

Modified residue871Phosphoserine; by host PKA By similarity
Modified residue1551Phosphoserine; by host
Modified residue1621Phosphoserine; by host
Modified residue1701Phosphoserine; by host

Natural variations

Natural variant331T → N in strain: Latvia.
Natural variant801A → I in strain: Latvia.
Natural variant971F → L Frequent mutation in chronic HBV carriers.

Experimental info

Mutagenesis1551S → A: Complete loss of replication. Ref.7
Mutagenesis1621S → A: Complete loss of pregenomic RNA encapsidation and replication. Ref.7
Mutagenesis1701S → A: Partial loss of replication. Ref.7

Sequences

Sequence LengthMass (Da)Tools
Isoform Capsid protein [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: E0D9D9763F24E958

FASTA18321,116
        10         20         30         40         50         60 
MDIDPYKEFG ATVELLSFLP SDFFPSVRDL LDTASALYRE ALESPEHCSP HHTALRQAIL 

        70         80         90        100        110        120 
CWGELMTLAT WVGVNLEDPA SRDLVVSYVN TNMGLKFRQL LWFHISCLTF GRETVIEYLV 

       130        140        150        160        170        180 
SFGVWIRTPP AYRPPNAPIL STLPETTVVR RRGRSPRRRT PSPRRRRSQS PRRRRSQSRE 


SQC 

« Hide

Isoform External core antigen [UniParc].

See P0C573.

References

[1]"Nucleotide sequence of the hepatitis B virus genome (subtype ayw) cloned in E. coli."
Galibert F., Mandart E., Fitoussi F., Tiollais P., Charnay P.
Nature 281:646-650(1979) [PubMed: 399327] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Subtype ayw variant of hepatitis B virus. DNA primary structure analysis."
Bichko V., Pushko P., Dreilina D., Pumpen P., Gren E.Y.
FEBS Lett. 185:208-212(1985) [PubMed: 3996597] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Latvia.
[3]"Evolutionary conservation in the hepatitis B virus core structure: comparison of human and duck cores."
Kenney J.M., von Bonsdorff C.H., Nassal M., Fuller S.D.
Structure 3:1009-1019(1995) [PubMed: 8589996] [Abstract]
Cited for: CAPSID STRUCTURE.
[4]"Phosphorylation of the core protein of hepatitis B virus by a 46-kilodalton serine kinase."
Kau J.H., Ting L.P.
J. Virol. 72:3796-3803(1998) [PubMed: 9557662] [Abstract]
Cited for: PHOSPHORYLATION.
[5]"Subtype-independent immature secretion and subtype-dependent replication deficiency of a highly frequent, naturally occurring mutation of human hepatitis B virus core antigen."
Yuan T.T., Tai P.C., Shih C.
J. Virol. 73:10122-10128(1999) [PubMed: 10559327] [Abstract]
Cited for: NATURALLY OCCURRING MUTATION.
[6]"Identification of SRPK1 and SRPK2 as the major cellular protein kinases phosphorylating hepatitis B virus core protein."
Daub H., Blencke S., Habenberger P., Kurtenbach A., Dennenmoser J., Wissing J., Ullrich A., Cotten M.
J. Virol. 76:8124-8137(2002) [PubMed: 12134018] [Abstract]
Cited for: PHOSPHORYLATION.
[7]"Hepatitis B virus DNA replication is coordinated by core protein serine phosphorylation and HBx expression."
Melegari M., Wolf S.K., Schneider R.J.
J. Virol. 79:9810-9820(2005) [PubMed: 16014942] [Abstract]
Cited for: MUTAGENESIS OF SER-155; SER-162 AND SER-170.
[8]"Envelopment of the hepatitis B virus nucleocapsid."
Bruss V.
Virus Res. 106:199-209(2004) [PubMed: 15567498] [Abstract]
Cited for: REVIEW.
+Additional computationally mapped references.

Web resources

HepSEQ

Hepatitis virus B database

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
V01460 Genomic DNA. Translation: CAA24706.1. Different initiation.
X02496 Genomic DNA. No translation available.

3D structure databases

ProteinModelPortalP03146.
SMRP03146. Positions 1-143.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR002006. Viral_capsid_core_Hepatitis.
[Graphical view]
PfamPF00906. Hepatitis_core. 1 hit.
[Graphical view]
SUPFAMSSF47852. Viral_capsid_core_Hepatitis. 1 hit.
ProtoNetSearch...

Entry information

Entry nameCAPSD_HBVD3
AccessionPrimary (citable) accession number: P03146
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: May 31, 2011
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families