HBEAG_HBVD3
ID HBEAG_HBVD3 Reviewed; 212 AA.
AC P0C573;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=External core antigen {ECO:0000255|HAMAP-Rule:MF_04076};
DE AltName: Full=HBeAg {ECO:0000255|HAMAP-Rule:MF_04076};
DE AltName: Full=Precore protein {ECO:0000255|HAMAP-Rule:MF_04076};
DE AltName: Full=p25 {ECO:0000255|HAMAP-Rule:MF_04076};
DE Flags: Precursor;
GN Name=C {ECO:0000255|HAMAP-Rule:MF_04076};
OS Hepatitis B virus genotype D subtype ayw (isolate France/Tiollais/1979)
OS (HBV-D).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Blubervirales; Hepadnaviridae; Orthohepadnavirus;
OC hepatitis B virus genotype D.
OX NCBI_TaxID=490133;
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9598; Pan troglodytes (Chimpanzee).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=399327; DOI=10.1038/281646a0;
RA Galibert F., Mandart E., Fitoussi F., Tiollais P., Charnay P.;
RT "Nucleotide sequence of the hepatitis B virus genome (subtype ayw) cloned
RT in E. coli.";
RL Nature 281:646-650(1979).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Latvia;
RX PubMed=3996597; DOI=10.1016/0014-5793(85)80771-7;
RA Bichko V., Pushko P., Dreilina D., Pumpen P., Gren E.Y.;
RT "Subtype ayw variant of hepatitis B virus. DNA primary structure
RT analysis.";
RL FEBS Lett. 185:208-212(1985).
RN [3]
RP CLEAVAGE BY HOST FURIN, AND MUTAGENESIS OF ARG-180; ARG-183; ARG-186;
RP ARG-188; ARG-193; ARG-196; ARG-201 AND ARG-204.
RX PubMed=17881438; DOI=10.1128/jvi.00846-07;
RA Nassal M., Leifer I., Wingert I., Dallmeier K., Prinz S., Vorreiter J.;
RT "A structural model for duck hepatitis B virus core protein derived by
RT extensive mutagenesis.";
RL J. Virol. 81:13218-13229(2007).
CC -!- FUNCTION: May regulate immune response to the intracellular capsid in
CC acting as a T-cell tolerogen, by having an immunoregulatory effect
CC which prevents destruction of infected cells by cytotoxic T-cells. This
CC immune regulation may predispose to chronicity during perinatal
CC infections and prevent severe liver injury during adult infections.
CC {ECO:0000255|HAMAP-Rule:MF_04076}.
CC -!- SUBUNIT: Homodimerizes. {ECO:0000255|HAMAP-Rule:MF_04076}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000255|HAMAP-Rule:MF_04076}. Host
CC nucleus {ECO:0000255|HAMAP-Rule:MF_04076}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=External core antigen;
CC IsoId=P0C573-1; Sequence=Displayed;
CC Name=Capsid protein;
CC IsoId=P03146-1; Sequence=External;
CC -!- PTM: Phosphorylated. {ECO:0000255|HAMAP-Rule:MF_04076}.
CC -!- PTM: Cleaved by host furin. {ECO:0000255|HAMAP-Rule:MF_04076}.
CC -!- SIMILARITY: Belongs to the orthohepadnavirus precore antigen family.
CC {ECO:0000255|HAMAP-Rule:MF_04076}.
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DR EMBL; V01460; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X02496; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR SMR; P0C573; -.
DR ABCD; P0C573; 2 sequenced antibodies.
DR Proteomes; UP000007930; Genome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-UniRule.
DR GO; GO:0042025; C:host cell nucleus; 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: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; IPR013195; Hepatitis_B_virus_capsid_N.
DR InterPro; IPR002006; Hepatitis_core.
DR InterPro; IPR036459; Viral_capsid_core_dom_sf_HBV.
DR Pfam; PF08290; Hep_core_N; 1.
DR Pfam; PF00906; Hepatitis_core; 3.
DR SUPFAM; SSF47852; SSF47852; 1.
PE 1: Evidence at protein level;
KW Alternative initiation; Disulfide bond; Host nucleus;
KW Host-virus interaction; Reference proteome; Repeat; Secreted; Signal;
KW Viral immunoevasion.
FT SIGNAL 1..19
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04076"
FT CHAIN 20..212
FT /note="External core antigen"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04076"
FT /id="PRO_0000324724"
FT PROPEP 184..212
FT /id="PRO_0000324725"
FT REPEAT 184..190
FT /note="1; half-length"
FT REPEAT 191..198
FT /note="2"
FT REPEAT 199..206
FT /note="3"
FT REGION 25..27
FT /note="HBEAG"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04076"
FT REGION 165..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 184..206
FT /note="3 X 8 AA repeats of S-P-R-R-R-R-S-Q"
FT COMPBIAS 181..202
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 183..184
FT /note="Cleavage; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04076"
FT DISULFID 77
FT /note="Interchain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04076"
FT DISULFID 90
FT /note="Interchain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04076"
FT MUTAGEN 180
FT /note="R->G: Complete loss of cleavage."
FT /evidence="ECO:0000269|PubMed:17881438"
FT MUTAGEN 183
FT /note="R->G: Complete loss of cleavage."
FT /evidence="ECO:0000269|PubMed:17881438"
FT MUTAGEN 186
FT /note="R->G: No effect on cleavage."
FT /evidence="ECO:0000269|PubMed:17881438"
FT MUTAGEN 188
FT /note="R->G: No effect on cleavage."
FT /evidence="ECO:0000269|PubMed:17881438"
FT MUTAGEN 193
FT /note="R->G: No effect on cleavage."
FT /evidence="ECO:0000269|PubMed:17881438"
FT MUTAGEN 196
FT /note="R->G: No effect on cleavage."
FT /evidence="ECO:0000269|PubMed:17881438"
FT MUTAGEN 201
FT /note="R->G: No effect on cleavage."
FT /evidence="ECO:0000269|PubMed:17881438"
FT MUTAGEN 204
FT /note="R->G: No effect on cleavage."
FT /evidence="ECO:0000269|PubMed:17881438"
SQ SEQUENCE 212 AA; 24350 MW; D3016A4E8B05A1B8 CRC64;
MQLFHLCLII SCSCPTVQAS KLCLGWLWGM DIDPYKEFGA TVELLSFLPS DFFPSVRDLL
DTASALYREA LESPEHCSPH HTALRQAILC WGELMTLATW VGVNLEDPAS RDLVVSYVNT
NMGLKFRQLL WFHISCLTFG RETVIEYLVS FGVWIRTPPA YRPPNAPILS TLPETTVVRR
RGRSPRRRTP SPRRRRSQSP RRRRSQSRES QC
