ID CAPSD_HBVC4 Reviewed; 183 AA. AC P0C6H6; DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot. DT 18-MAR-2008, sequence version 1. DT 09-DEC-2015, entry version 36. DE RecName: Full=Capsid protein; DE AltName: Full=Core antigen; DE AltName: Full=Core protein; DE AltName: Full=HBcAg; DE AltName: Full=p21.5; GN Name=C; OS Hepatitis B virus genotype C subtype adr (isolate Korea/Kim/1989) OS (HBV-C). OC Viruses; Retro-transcribing viruses; Hepadnaviridae; OC Orthohepadnavirus. OX NCBI_TaxID=31512; OH NCBI_TaxID=9606; Homo sapiens (Human). OH NCBI_TaxID=9598; Pan troglodytes (Chimpanzee). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2928116; DOI=10.1093/nar/17.5.2124; RA Rho H.M., Kim K., Hyun S.W., Kim Y.S.; RT "The nucleotide sequence and reading frames of a mutant hepatitis B RT virus subtype adr."; RL Nucleic Acids Res. 17:2124-2124(1989). CC -!- FUNCTION: Self assembles to form an icosahedral capsid. Most CC capsid appear to be large particles with a icosahedral symmetry of CC T=4 and consist of 240 copies of capsid protein, though a fraction CC forms smaller T=3 particles consisting of 180 capsid proteins. CC Entering capsid are transported along microtubules to the nucleus. CC Phosphorylation of the capsid is thought to induce exposure of CC nuclear localization signal in the C-terminal portion of the CC capsid protein that allows binding to the nuclear pore complex via CC the importin (karyopherin-) alpha and beta. Capsids are imported CC in intact form through the nuclear pore into the nuclear basket, CC where it probably binds NUP153. Only capsids that contain the CC mature viral genome can release the viral DNA and capsid protein CC into the nucleoplasm. Immature capsids get stucked in the basket. CC Capsids encapsulate the pre-genomic RNA and the P protein. Pre- CC genomic RNA is reverse transcribed into DNA while the capsid is CC still in the cytoplasm. The capsid can then either be directed to CC the nucleus, providing more genome for transcription, or bud CC through the endoplasmic reticulum to provide new virions (By CC similarity). {ECO:0000250}. CC -!- FUNCTION: Encapsidates hepatitis delta genome. {ECO:0000250}. CC -!- SUBUNIT: Homodimerizes, then multimerizes. Interacts with cytosol CC exposed regions of viral L glycoprotein present in the reticulum- CC to-Golgi compartment. Interacts with human FLNB (By similarity). CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Capsid protein: Virion. Host cytoplasm CC {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative initiation; Named isoforms=2; CC Name=Capsid protein; CC IsoId=P0C6H6-1; Sequence=Displayed; CC Name=X-Core fused protein; CC IsoId=Q67863-1; Sequence=External; CC -!- PTM: Phosphorylated by host SRPK1, SRPK2, and maybe protein kinase CC A, protein kinase C or GAPDH. Phosphorylation is critical for CC pregenomic RNA packaging. Protein kinase C phosphorylation is CC stimulated by HBx protein and may play a role in transport of the CC viral genome to the nucleus at the late step during viral CC replication cycle. Protein kinase A phosphorylation may promote CC capsid assembly (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the orthohepadnavirus core antigen family. CC {ECO:0000305}. CC -!- WEB RESOURCE: Name=HepSEQ; Note=Hepatitis virus B database; CC URL="http://www.hpa-bioinformatics.org.uk/HepSEQ-Research/Public/Web_Front/main.php"; 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; X14193; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; P0C6H6; -. DR SMR; P0C6H6; 1-143. DR Proteomes; UP000007924; 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:0009405; P:pathogenesis; IEA:InterPro. 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 InterPro; IPR002006; Viral_capsid_core_Hepatitis. DR Pfam; PF00906; Hepatitis_core; 3. DR SUPFAM; SSF47852; SSF47852; 1. PE 3: Inferred from homology; KW Alternative initiation; Capsid protein; Complete proteome; KW Cytoplasmic inwards viral transport; DNA-binding; Host cytoplasm; KW Host-virus interaction; Microtubular inwards viral transport; KW Phosphoprotein; Repeat; RNA-binding; T=4 icosahedral capsid protein; KW Viral penetration into host nucleus; Virion; KW Virus entry into host cell. FT CHAIN 1 183 Capsid protein. FT /FTId=PRO_0000324365. FT REPEAT 155 160 1; half-length. FT REPEAT 162 168 2. FT REPEAT 170 176 3. FT REGION 155 176 3 X 7 AA repeats of S-P-R-R-R-[PR]-S. FT REGION 177 183 RNA binding. {ECO:0000250}. FT MOTIF 158 175 Bipartite nuclear localization signal. FT {ECO:0000255}. FT MOD_RES 87 87 Phosphoserine; by host PKA. FT {ECO:0000250}. FT MOD_RES 155 155 Phosphoserine; by host. {ECO:0000250}. FT MOD_RES 162 162 Phosphoserine; by host. {ECO:0000250}. FT MOD_RES 170 170 Phosphoserine; by host. {ECO:0000250}. SQ SEQUENCE 183 AA; 21096 MW; ED2DA1DB07FB4829 CRC64; MDIDPYKEFG ASVELLSFLP SDFFPSIRDL LDTASALYRE ALESPEHCSP HHTALRQAIL CWGELMNLAT WVGSNLEDPA SRELVVSYVN VNMGLKIRQL LWFHISCLTF GRETVLEYLV SFGVWIRTPP AYRPPNAPIL STLPETTVVR RRGRSPRRRT PSPRRRRSES PRRRRSQSRE SQC //