X_HBVA6
ID X_HBVA6 Reviewed; 154 AA.
AC Q91C38;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 23-FEB-2022, entry version 62.
DE RecName: Full=Protein X {ECO:0000255|HAMAP-Rule:MF_04074};
DE AltName: Full=HBx {ECO:0000255|HAMAP-Rule:MF_04074};
DE AltName: Full=Peptide X {ECO:0000255|HAMAP-Rule:MF_04074};
DE AltName: Full=pX {ECO:0000255|HAMAP-Rule:MF_04074};
GN Name=X {ECO:0000255|HAMAP-Rule:MF_04074};
OS Hepatitis B virus genotype A1 subtype adw2 (isolate South Africa/84/2001)
OS (HBV-A).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Blubervirales; Hepadnaviridae; Orthohepadnavirus.
OX NCBI_TaxID=489454;
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9598; Pan troglodytes (Chimpanzee).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11596083; DOI=10.1002/jmv.2062.abs;
RA Owiredu W.K., Kramvis A., Kew M.C.;
RT "Molecular analysis of hepatitis B virus genomes isolated from black
RT African patients with fulminant hepatitis B.";
RL J. Med. Virol. 65:485-492(2001).
RN [2]
RP REVIEW.
RX PubMed=15542625; DOI=10.1128/jvi.78.23.12725-12734.2004;
RA Bouchard M.J., Schneider R.J.;
RT "The enigmatic X gene of hepatitis B virus.";
RL J. Virol. 78:12725-12734(2004).
RN [3]
RP REVIEW.
RX PubMed=16984372; DOI=10.1111/j.1349-7006.2006.00299.x;
RA Tang H., Oishi N., Kaneko S., Murakami S.;
RT "Molecular functions and biological roles of hepatitis B virus x protein.";
RL Cancer Sci. 97:977-983(2006).
CC -!- FUNCTION: Multifunctional protein that plays a role in silencing host
CC antiviral defenses and promoting viral transcription. Does not seem to
CC be essential for HBV infection. May be directly involved in development
CC of cirrhosis and liver cancer (hepatocellular carcinoma). Most of
CC cytosolic activities involve modulation of cytosolic calcium. The
CC effect on apoptosis is controversial depending on the cell types in
CC which the studies have been conducted. May induce apoptosis by
CC localizing in mitochondria and causing loss of mitochondrial membrane
CC potential. May also modulate apoptosis by binding host CFLAR, a key
CC regulator of the death-inducing signaling complex (DISC). Promotes
CC viral transcription by using the host E3 ubiquitin ligase DDB1 to
CC target the SMC5-SMC6 complex to proteasomal degradation. This host
CC complex would otherwise bind to viral episomal DNA, and prevents its
CC transcription. Moderately stimulates transcription of many different
CC viral and cellular transcription elements. Promoters and enhancers
CC stimulated by HBx contain DNA binding sites for NF-kappa-B, AP-1, AP-2,
CC c-EBP, ATF/CREB, or the calcium-activated factor NF-AT.
CC {ECO:0000255|HAMAP-Rule:MF_04074}.
CC -!- SUBUNIT: May form homodimer. May interact with host CEBPA, CFLAR,
CC CREB1, DDB1, E4F1, HBXIP, HSPD1/HSP60, NFKBIA, POLR2E and SMAD4.
CC Interacts with host SMC5-SMC6 complex and induces its degradation.
CC {ECO:0000255|HAMAP-Rule:MF_04074}.
CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04074}.
CC Host nucleus {ECO:0000255|HAMAP-Rule:MF_04074}. Host mitochondrion
CC {ECO:0000255|HAMAP-Rule:MF_04074}. Note=Mainly cytoplasmic as only a
CC fraction is detected in the nucleus. In cytoplasm, a minor fraction
CC associates with mitochondria or proteasomes. {ECO:0000255|HAMAP-
CC Rule:MF_04074}.
CC -!- PTM: A fraction may be phosphorylated in insect cells and HepG2 cells,
CC a human hepatoblastoma cell line. Phosphorylated in vitro by host
CC protein kinase C or mitogen-activated protein kinase. N-acetylated in
CC insect cells. {ECO:0000255|HAMAP-Rule:MF_04074}.
CC -!- SIMILARITY: Belongs to the orthohepadnavirus protein X family.
CC {ECO:0000255|HAMAP-Rule:MF_04074}.
CC -!- CAUTION: Transcriptional activities should be taken with a grain of
CC salt. As of 2007, all studies demonstrating in vivo interaction between
CC protein X and transcriptional components were performed with
CC significant overexpression of both proteins and in the absence of viral
CC infection.
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DR EMBL; AF297625; AAK97201.1; -; Genomic_DNA.
DR SMR; Q91C38; -.
DR Proteomes; UP000007909; Genome.
DR GO; GO:0033650; C:host cell mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0039652; P:induction by virus of host NF-kappaB cascade; IEA:UniProtKB-UniRule.
DR GO; GO:0039592; P:suppression by virus of G2/M transition of host mitotic cell cycle; IEA:UniProtKB-UniRule.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR GO; GO:0019079; P:viral genome replication; IEA:UniProtKB-UniRule.
DR HAMAP; MF_04074; HBV_X; 1.
DR InterPro; IPR000236; Transactivation_prot_X.
DR Pfam; PF00739; X; 1.
PE 3: Inferred from homology;
KW Activation of host NF-kappa-B by virus; Activator; Apoptosis;
KW Host cytoplasm; Host G2/M cell cycle arrest by virus; Host mitochondrion;
KW Host nucleus; Host-virus interaction;
KW Modulation of host cell cycle by virus; Transcription;
KW Transcription regulation.
FT CHAIN 1..154
FT /note="Protein X"
FT /id="PRO_0000319895"
FT REGION 68..117
FT /note="Mitochondrial targeting sequence"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04074"
SQ SEQUENCE 154 AA; 16593 MW; 8E561143CA7F8292 CRC64;
MAARLYCQLD SSRDVLCLRP VGAESRGRPL AGPLGALSSP SPSAVPSDHG AHLSLRGLPV
CAFSSAGPCA LRFTSARCME TTVNAHQILP KVLHKRTLGL PAMSTTDLEA YFKDCVFKDW
EELGEEIRLK VFVLGGCRHK LVFAPSSCNF FTSA
