SHDAG_HDVV1
ID SHDAG_HDVV1 Reviewed; 194 AA.
AC Q91DH7;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 3.
DT 29-SEP-2021, entry version 67.
DE RecName: Full=Small delta antigen;
DE Short=S-HDAg;
DE AltName: Full=p24;
OS Hepatitis delta virus genotype III (isolate VnzD8624) (HDV).
OC Viruses; Ribozyviria; Kolmioviridae; Deltavirus.
OX NCBI_TaxID=261993;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND RNA EDITING.
RX PubMed=11514728; DOI=10.1099/0022-1317-82-9-2183;
RA Nakano T., Shapiro C.N., Hadler S.C., Casey J.L., Mizokami M., Orito E.,
RA Robertson B.H.;
RT "Characterization of hepatitis D virus genotype III among Yucpa Indians in
RT Venezuela.";
RL J. Gen. Virol. 82:2183-2189(2001).
RN [2]
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 [3]
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: Promotes both transcription and replication of genomic RNA.
CC Following virus entry into host cell, provides nuclear import of HDV
CC RNPs thanks to its nuclear localization signal. May interact with host
CC RNA polymerase II thereby changing its template requirement from DNA to
CC RNA. RNA pol II complex would then acts as an RNA-directed RNA
CC polymerase, and transcribe and replicate HDV genome (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Homooctamer. Interacts with host RNA polymerase II
CC complex, and with host NPM1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Virion. Host nucleus {ECO:0000250}.
CC -!- PTM: Phosphorylated at serines and threonines by host MAPK1/3, PKR, and
CC CK2. {ECO:0000250}.
CC -!- PTM: Acetylation modulates nuclear localization. Neo-synthesized
CC genomic RNA migrates from the nucleus to the cytoplasm, where they
CC interact with S-HDAg, which once acetylated redirect both partners to
CC the nucleus (By similarity). {ECO:0000250}.
CC -!- PTM: Methylation plays a role in viral genome replication.
CC {ECO:0000250}.
CC -!- RNA EDITING: Modified_positions=196 {ECO:0000269|PubMed:11514728};
CC Note=Partially edited. RNA editing at this position occurs on the
CC antigenomic strand and consists of a conversion of A to G catalyzed by
CC the cellular enzyme ADAR1. The unedited RNA version gives rise to the
CC small delta antigen, which ends with a nonsense codon at position 194.
CC In the edited version, this amber codon is modified to a tryptophan
CC codon and gives rise to the large delta antigen protein (AC P0C6M8). S-
CC HDAg suppresses editing of non-replicating antigenomic RNA, thereby
CC regulating the extent of editing (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; AB037949; BAB68381.1; -; Genomic_RNA.
DR Proteomes; UP000008114; Genome.
DR GO; GO:0042025; C:host cell nucleus; 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; Host-virus interaction; Methylation;
KW Phosphoprotein; RNA editing; RNA-binding;
KW Viral penetration into host nucleus; Virion; Virus entry into host cell.
FT CHAIN 1..194
FT /note="Small delta antigen"
FT /id="PRO_0000038157"
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 57..194
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:P0C6L3"
FT COMPBIAS 57..103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..145
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="Phosphoserine; by host CK2"
FT /evidence="ECO:0000250|UniProtKB:P0C6L3"
FT MOD_RES 13
FT /note="Omega-N-methylated arginine; by host PRMT1"
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:P0C6L3"
FT MOD_RES 176
FT /note="Phosphoserine; by host MAPK1 and MAPK3"
FT /evidence="ECO:0000250|UniProtKB:P0C6L3"
FT MOD_RES 181
FT /note="Phosphothreonine; by host"
FT /evidence="ECO:0000250|UniProtKB:P0C6L3"
SQ SEQUENCE 194 AA; 22082 MW; 6F53D5D7AF7FA535 CRC64;
MSQPGARPGS KXREEALEQW VEERKKKRIA EKELRRINKK IKKLEDENPW LGNIVGLLRR
KKDEEGGPPA KRPRREDMEI DSTPGRKSKT RGFTDQERRD HRRRKALENK KKQLAGGGKN
LSREEEEELR RLARDDDERE RRVAGPRPGG VNPMDGPPRG APGGGFVPSL QGVPESPFSR
TGEGIDIRGT QQFP
