LHDAG_HDVU2
ID LHDAG_HDVU2 Reviewed; 214 AA.
AC P0C6M5;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 1.
DT 29-SEP-2021, entry version 49.
DE RecName: Full=Large delta antigen;
DE Short=L-HDAg;
DE AltName: Full=p27;
DE Flags: Precursor;
OS Hepatitis delta virus genotype I (isolate US-2) (HDV).
OC Viruses; Ribozyviria; Kolmioviridae; Deltavirus.
OX NCBI_TaxID=261991;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND RNA EDITING.
RX PubMed=8415646; DOI=10.1073/pnas.90.19.9016;
RA Casey J.L., Brown T.L., Colan E.J., Wignall F.S., Gerin J.L.;
RT "A genotype of hepatitis D virus that occurs in northern South America.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:9016-9020(1993).
RN [2]
RP RNA EDITING.
RX PubMed=7494266; DOI=10.1128/jvi.69.12.7593-7600.1995;
RA Casey J.L., Gerin J.L.;
RT "Hepatitis D virus RNA editing: specific modification of adenosine in the
RT antigenomic RNA.";
RL J. Virol. 69:7593-7600(1995).
RN [3]
RP RNA EDITING.
RX PubMed=9528763; DOI=10.1128/mcb.18.4.1919;
RA Polson A.G., Ley H.L. III, Bass B.L., Casey J.L.;
RT "Hepatitis delta virus RNA editing is highly specific for the amber/W site
RT and is suppressed by hepatitis delta antigen.";
RL Mol. Cell. Biol. 18:1919-1926(1998).
RN [4]
RP REVIEW.
RX PubMed=16402678;
RA Husa P., Linhartova A., Nemecek V., Husova L.;
RT "Hepatitis D.";
RL Acta Virol. 49:219-225(2005).
RN [5]
RP REVIEW.
RX PubMed=16903222; DOI=10.1007/3-540-29802-9_5;
RA Huang W.H., Chen C.W., Wu H.L., Chen P.J.;
RT "Post-translational modification of delta antigen of hepatitis D virus.";
RL Curr. Top. Microbiol. Immunol. 307:91-112(2006).
CC -!- FUNCTION: Following virus entry into host cell, provides nuclear import
CC of HDV RNPs thanks to its nuclear localization signal. Needs co-
CC infection with hepatitis B virus to provide surface proteins, otherwise
CC there is no packaging or budding. Packages the HDV ribonucleoprotein in
CC hepatitis B virus empty particles. Interacts with both HDV genomic RNA
CC and cytoplasmic tail of HBsAg. May inhibit viral RNA replication (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Homooctamer. Interacts with HBV HBsAg. May interact
CC with clathrin to induce virion budding (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Virion. Host nucleus, host nucleolus.
CC Note=isoprenylated in the cytoplasm, and translocates in the nucleus
CC possibly after phosphorylation. Translocates after to nuclear speckle,
CC then to the ER membrane where interaction with Hepatitis B virus
CC antigene takes place (By similarity). {ECO:0000250}.
CC -!- PTM: Prenylated by host farnesyl-transferase in the cytoplasm prior to
CC nucleus translocation. {ECO:0000250}.
CC -!- PTM: Phosphorylated at serines by host CK2 and other kinases.
CC phosphorylation does not seem to be important for its function (By
CC similarity). {ECO:0000250}.
CC -!- RNA EDITING: Modified_positions=196 {ECO:0000269|PubMed:7494266,
CC ECO:0000269|PubMed:8415646, ECO:0000269|PubMed:9528763}; Note=Partially
CC edited. RNA editing at this position occurs on the antigenomic strand
CC and consists of a conversion of A to G catalyzed by the cellular enzyme
CC ADAR1. The unedited RNA version gives rise to the small delta antigen
CC (AC Q81835), which ends with a nonsense codon at position 196. In the
CC edited version, this amber codon is modified to a tryptophan codon and
CC gives rise to the large delta antigen protein. S-HDAg suppresses
CC editing of non-replicating antigenomic RNA, thereby regulating the
CC extent of editing (By similarity). {ECO:0000250};
CC -!- MISCELLANEOUS: This strain belongs to the genotype I found in North
CC America, Europe, Africa, East and West Asia and the South Pacific.
CC -!- SIMILARITY: Belongs to the hepatitis delta antigen family.
CC {ECO:0000305}.
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DR EMBL; L22066; AAB02593.1; -; Genomic_RNA.
DR SMR; P0C6M5; -.
DR Proteomes; UP000008235; Genome.
DR GO; GO:0044196; C:host cell nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
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 Gene3D; 4.10.220.40; -; 1.
DR InterPro; IPR027403; Delta_antigen_N.
DR InterPro; IPR037517; HDAG_dom.
DR InterPro; IPR002506; HDV_ag.
DR Pfam; PF01517; HDV_ag; 1.
DR SUPFAM; SSF58108; SSF58108; 1.
DR PROSITE; PS51838; HDAG; 1.
PE 3: Inferred from homology;
KW Acetylation; Host nucleus; Lipoprotein; Methylation; Phosphoprotein;
KW Prenylation; RNA editing; RNA-binding; Viral penetration into host nucleus;
KW Virion; Virus entry into host cell.
FT CHAIN 1..211
FT /note="Large delta antigen"
FT /id="PRO_0000038150"
FT PROPEP 212..214
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:P29996"
FT /id="PRO_0000396677"
FT DOMAIN 20..195
FT /note="HDAg"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01183"
FT REGION 12..60
FT /note="Dimerization"
FT /evidence="ECO:0000255"
FT REGION 52..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 97..107
FT /note="RNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01183"
FT REGION 130..195
FT /note="RNAPII-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01183"
FT REGION 136..146
FT /note="RNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01183"
FT MOTIF 66..75
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:P29996"
FT COMPBIAS 57..103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..146
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000250|UniProtKB:P29996"
FT MOD_RES 13
FT /note="Omega-N-methylated arginine; by host"
FT /evidence="ECO:0000250|UniProtKB:P0C6L3"
FT MOD_RES 72
FT /note="N6-acetyllysine; by host"
FT /evidence="ECO:0000250|UniProtKB:P0C6L3"
FT MOD_RES 123
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000250|UniProtKB:P29996"
FT MOD_RES 177
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000250|UniProtKB:P29996"
FT MOD_RES 211
FT /note="Cysteine methyl ester; by host"
FT /evidence="ECO:0000250|UniProtKB:P29996"
FT LIPID 211
FT /note="S-farnesyl cysteine; by host"
FT /evidence="ECO:0000250|UniProtKB:P29996"
SQ SEQUENCE 214 AA; 24245 MW; 83CA09F1EC1E7FF6 CRC64;
MSRSESKKNR GGREEILEQW VGARKKLEEL ERDLRKIKKK IKKLEEENPW LGNIKGILGK
KDREGEGAPP AKRARADQME VDSGPRKRPF RGEFTDKERR DHRRRKALEN KRKQLSSGGK
SLSKEEEEEL RKLTEEDERR ERRVAGPRVG GVNPLEGGTR GAPGGGFVPS MQGVPESPFA
RTGEGLDVRG NQGFPWDILF PADPPFSPQS CRPQ
