LHDAG_HDVP1
ID LHDAG_HDVP1 Reviewed; 214 AA.
AC P0C6M3;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 1.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=Large delta antigen;
DE Short=L-HDAg;
DE AltName: Full=p27;
DE Flags: Precursor;
OS Hepatitis delta virus genotype III (isolate Peru-1) (HDV).
OC Viruses; Ribozyviria; Kolmioviridae; Deltavirus.
OX NCBI_TaxID=261996;
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=12829818; DOI=10.1128/jvi.77.14.7786-7795.2003;
RA Cheng Q., Jayan G.C., Casey J.L.;
RT "Differential inhibition of RNA editing in hepatitis delta virus genotype
RT III by the short and long forms of hepatitis delta antigen.";
RL J. Virol. 77:7786-7795(2003).
RN [3]
RP ISOPRENYLATION AT CYS-211, AND ANTIVIRAL AGENTS.
RX PubMed=12239323; DOI=10.1128/jvi.76.20.10465-10472.2002;
RA Bordier B.B., Marion P.L., Ohashi K., Kay M.A., Greenberg H.B., Casey J.L.,
RA Glenn J.S.;
RT "A prenylation inhibitor prevents production of infectious hepatitis delta
RT virus particles.";
RL J. Virol. 76:10465-10472(2002).
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:12829818,
CC ECO:0000269|PubMed:8415646}; Note=Partially edited. RNA editing at this
CC position occurs on the antigenomic strand and consists of a conversion
CC of A to G catalyzed by the cellular enzyme ADAR1. The unedited RNA
CC version gives rise to the small delta antigen (AC Q81842), which ends
CC with a nonsense codon at position 196. In the edited version, this
CC amber codon is modified to a tryptophan codon and gives rise to the
CC large delta antigen protein. S-HDAg suppresses editing of non-
CC replicating antigenomic RNA, thereby regulating the extent of editing
CC (By similarity). {ECO:0000250};
CC -!- MISCELLANEOUS: This strain belongs to the genotype III found only among
CC cases in South America and which causes a more severe form of infection
CC than genotypes I and II.
CC -!- SIMILARITY: Belongs to the hepatitis delta antigen family.
CC {ECO:0000305}.
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DR EMBL; L22063; AAB02595.1; -; Genomic_RNA.
DR SMR; P0C6M3; -.
DR Proteomes; UP000008110; 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 1: Evidence at protein level;
KW Acetylation; Host nucleus; Lipoprotein; Methylation; Phosphoprotein;
KW Prenylation; Reference proteome; RNA editing; RNA-binding;
KW Viral penetration into host nucleus; Virion; Virus entry into host cell.
FT CHAIN 1..211
FT /note="Large delta antigen"
FT /id="PRO_0000038142"
FT PROPEP 212..214
FT /note="Removed in mature form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000396795"
FT DOMAIN 20..194
FT /note="HDAg"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01183"
FT REGION 12..59
FT /note="Dimerization"
FT /evidence="ECO:0000255"
FT REGION 58..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 96..106
FT /note="RNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01183"
FT REGION 129..194
FT /note="RNAPII-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01183"
FT REGION 135..145
FT /note="RNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01183"
FT MOTIF 65..74
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:P29996"
FT COMPBIAS 58..103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..145
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 71
FT /note="N6-acetyllysine; by host"
FT /evidence="ECO:0000250|UniProtKB:P0C6L3"
FT MOD_RES 122
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000250|UniProtKB:P29996"
FT MOD_RES 176
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:0000305"
FT LIPID 211
FT /note="S-farnesyl cysteine; by host"
FT /evidence="ECO:0000305|PubMed:12239323"
SQ SEQUENCE 214 AA; 24452 MW; BFD86C1F6C356CD5 CRC64;
MSQTVARLTS KEREEILEQW VEERKNRRKL EKDLRRANKK IKKLEDENPW LGNVVGLLRR
KKDEDGAPPA KRPRQETMEV DSGPGRKPKA RGFTDQERRD HRRRKALENK KKQLAGGGKH
LSQEEEEELR RLARDDDERE RRTAGPRPGG VNPMDGPPRG APGGGFVPSL QGVPESPFSR
TGEGIDIRGT QQFPWYGFTP PPPGYYWVPG CTQQ
