SHDAG_HDV27
ID SHDAG_HDV27 Reviewed; 195 AA.
AC P0DTC0;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 22-APR-2020, sequence version 1.
DT 29-SEP-2021, entry version 5.
DE RecName: Full=Small delta antigen;
DE Short=S-HDAg;
DE AltName: Full=p24;
OS Hepatitis delta virus genotype I (isolate HDV/Human/Central African
OS Republic/FH27/1985) (HDV).
OC Viruses; Ribozyviria; Kolmioviridae; Deltavirus.
OX NCBI_TaxID=2691025;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=29698488; DOI=10.1371/journal.pntd.0006377;
RA Komas N.P., Ghosh S., Abdou-Chekaraou M., Pradat P., Al Hawajri N.,
RA Manirakiza A., Laghoe G.L., Bekondi C., Brichler S., Ouavene J.O.,
RA Sepou A., Yambiyo B.M., Gody J.C., Fikouma V., Gerber A.,
RA Abeywickrama Samarakoon N., Alfaiate D., Scholtes C., Martel N., Le Gal F.,
RA Lo Pinto H., Amri I., Hantz O., Durantel D., Lesbordes J.L., Gordien E.,
RA Merle P., Drugan T., Trepo C., Zoulim F., Cortay J.C., Kay A.C., Deny P.;
RT "Hepatitis B and hepatitis D virus infections in the Central African
RT Republic, twenty-five years after a fulminant hepatitis outbreak, indicate
RT continuing spread in asymptomatic young adults.";
RL PLoS Negl. Trop. Dis. 12:E0006377-E0006377(2018).
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.
CC {ECO:0000250|UniProtKB:P0C6L3}.
CC -!- SUBUNIT: Homodimer. Homooctamer. Interacts with host RNA polymerase II
CC complex, and with host NPM1. {ECO:0000250|UniProtKB:P0C6L3}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:P0C6L3}. Host
CC nucleus {ECO:0000250|UniProtKB:P0C6L3}.
CC -!- PTM: Phosphorylated at serines and threonines by host MAPK1/3, PKR, and
CC CK2. {ECO:0000250|UniProtKB:P0C6L3}.
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. {ECO:0000250|UniProtKB:P0C6L3}.
CC -!- PTM: Methylation plays a role in viral genome replication.
CC {ECO:0000250|UniProtKB:P0C6L3}.
CC -!- RNA EDITING: Modified_positions=196 {ECO:0000250|UniProtKB:P0C6L3};
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 196.
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 P29996). S-
CC HDAg suppresses editing of non-replicating antigenomic RNA, thereby
CC regulating the extent of editing. {ECO:0000250|UniProtKB:P0C6L3};
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 {ECO:0000250|UniProtKB:P0C6L3}.
CC -!- SIMILARITY: Belongs to the hepatitis delta antigen family.
CC {ECO:0000305}.
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DR SMR; P0DTC0; -.
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.
PE 3: Inferred from homology;
KW Acetylation; Host nucleus; Host-virus interaction; Methylation;
KW Phosphoprotein; RNA-binding; Viral penetration into host nucleus; Virion;
KW Virus entry into host cell.
FT CHAIN 1..195
FT /note="Small delta antigen"
FT /evidence="ECO:0000250|UniProtKB:P0C6L3"
FT /id="PRO_0000449503"
FT DOMAIN 20..195
FT /note="HDAg"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01183"
FT REGION 1..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 12..60
FT /note="Dimerization"
FT /evidence="ECO:0000255"
FT REGION 130..195
FT /note="RNAPII-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01183"
FT MOTIF 66..75
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:P0C6L3"
FT COMPBIAS 1..46
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..105
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..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:P0C6L3"
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:P0C6L3"
FT MOD_RES 177
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000250|UniProtKB:P0C6L3"
SQ SEQUENCE 195 AA; 22071 MW; 43BC3FBB76577065 CRC64;
MSRSESKESR KGREESLEKW VNSRKKVEEL ERELRKEKKK IKRLEDQNPW LGNIKGILGK
KDKDGEGAPP AKRARTDQME VDSGPRKRPL RGGFTDKERQ DHRRRKALEN KKKQLAGGGK
NLSREEEEEL KRLTEEDERR ERRVAGPPTG GVNPLEGGQR GAPGGGFVPS MQGVPESPFS
RHGEGLDTRG DRGFP
