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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
 
 
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