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 08-MAY-2019, entry version 54. DE RecName: Full=Capsid protein {ECO:0000255|HAMAP-Rule:MF_04076}; DE AltName: Full=Core antigen {ECO:0000255|HAMAP-Rule:MF_04076}; DE AltName: Full=Core protein {ECO:0000255|HAMAP-Rule:MF_04076}; DE AltName: Full=HBcAg {ECO:0000255|HAMAP-Rule:MF_04076}; DE AltName: Full=p21.5 {ECO:0000255|HAMAP-Rule:MF_04076}; GN Name=C {ECO:0000255|HAMAP-Rule:MF_04076}; 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 an icosahedral symmetry CC of T=4 and consist of 240 copies of capsid protein, though a CC fraction forms smaller T=3 particles consisting of 180 capsid CC proteins. Entering capsid are transported along microtubules to CC the nucleus. Phosphorylation of the capsid is thought to induce CC exposure of nuclear localization signal in the C-terminal portion CC of the capsid protein that allows binding to the nuclear pore CC complex via the importin (karyopherin-) alpha and beta. Capsids CC are imported in intact form through the nuclear pore into the CC nuclear basket, where it probably binds NUP153. Only capsids that CC contain the mature viral genome can release the viral DNA and CC capsid protein into the nucleoplasm. Immature capsids get stucked CC in the basket. Capsids encapsulate the pre-genomic RNA and the P CC protein. Pre-genomic RNA is reverse transcribed into DNA while the CC capsid is still in the cytoplasm. The capsid can then either be CC directed to the nucleus, providing more genome for transcription, CC or bud through the endoplasmic reticulum to provide new virions. CC {ECO:0000255|HAMAP-Rule:MF_04076}. CC -!- FUNCTION: Encapsidates hepatitis delta genome. {ECO:0000255|HAMAP- CC Rule:MF_04076}. 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. Phosphorylated CC form interacts with host importin alpha; this interaction depends CC on the exposure of the NLS, which itself depends upon genome CC maturation and/or phosphorylation of the capsid protein. Interacts CC with host NUP153. {ECO:0000255|HAMAP-Rule:MF_04076}. CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04076}. CC Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04076}. 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 C or GAPDH. Phosphorylation is critical for pregenomic RNA CC packaging. Protein kinase C phosphorylation is stimulated by HBx CC protein and may play a role in transport of the viral genome to CC the nucleus at the late step during viral replication cycle. CC {ECO:0000255|HAMAP-Rule:MF_04076}. CC -!- SIMILARITY: Belongs to the orthohepadnavirus core antigen family. CC {ECO:0000255|HAMAP-Rule:MF_04076}. 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 SMR; P0C6H6; -. 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-UniRule. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0005198; F:structural molecule activity; IEA:UniProtKB-UniRule. DR GO; GO:0075521; P:microtubule-dependent intracellular transport of viral material towards nucleus; IEA:UniProtKB-UniRule. DR GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-UniRule. DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-UniRule. DR GO; GO:0075732; P:viral penetration into host nucleus; IEA:UniProtKB-UniRule. DR Gene3D; 1.10.4090.10; -; 1. DR HAMAP; MF_04076; HBV_HBEAG; 1. DR InterPro; IPR002006; Hepatitis_core. DR InterPro; IPR036459; Viral_capsid_core_dom_sf_HBV. 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:0000255|HAMAP- FT Rule:MF_04076}. FT MOTIF 158 175 Bipartite nuclear localization signal. FT {ECO:0000255|HAMAP-Rule:MF_04076}. FT MOD_RES 155 155 Phosphoserine; by host. FT {ECO:0000255|HAMAP-Rule:MF_04076}. FT MOD_RES 162 162 Phosphoserine; by host. FT {ECO:0000255|HAMAP-Rule:MF_04076}. FT MOD_RES 170 170 Phosphoserine; by host. FT {ECO:0000255|HAMAP-Rule:MF_04076}. 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 //