SF33K_ADE05
ID SF33K_ADE05 Reviewed; 229 AA.
AC P24940;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 29-SEP-2021, entry version 71.
DE RecName: Full=Protein 33K {ECO:0000250|UniProtKB:P24939};
DE Short=L4-33K;
DE AltName: Full=Splicing factor 33K {ECO:0000305};
DE AltName: Full=Terminase, small subunit {ECO:0000303|PubMed:25954255};
GN ORFNames=L4;
OS Human adenovirus C serotype 5 (HAdV-5) (Human adenovirus 5).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Mastadenovirus.
OX NCBI_TaxID=28285;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1727603; DOI=10.1016/0042-6822(92)90082-z;
RA Chroboczek J., Bieber F., Jacrot B.;
RT "The sequence of the genome of adenovirus type 5 and its comparison with
RT the genome of adenovirus type 2.";
RL Virology 186:280-285(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=23142869; DOI=10.1038/nmeth.2227;
RA Evans V.C., Barker G., Heesom K.J., Fan J., Bessant C., Matthews D.A.;
RT "De novo derivation of proteomes from transcriptomes for transcript and
RT protein identification.";
RL Nat. Methods 9:1207-1211(2012).
RN [3]
RP FUNCTION, AND MUTAGENESIS OF SER-178; SER-191; SER-194 AND SER-198.
RX PubMed=17028184; DOI=10.1074/jbc.m607601200;
RA Tormanen H., Backstrom E., Carlsson A., Akusjarvi G.;
RT "L4-33K, an adenovirus-encoded alternative RNA splicing factor.";
RL J. Biol. Chem. 281:36510-36517(2006).
RN [4]
RP FUNCTION.
RX PubMed=19176628; DOI=10.1128/jvi.02455-08;
RA Morris S.J., Leppard K.N.;
RT "Adenovirus serotype 5 L4-22K and L4-33K proteins have distinct functions
RT in regulating late gene expression.";
RL J. Virol. 83:3049-3058(2009).
RN [5]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-178; SER-191; SER-194 AND
RP SER-198.
RX PubMed=22944109; DOI=10.1016/j.virol.2012.08.021;
RA Ostberg S., Tormanen Persson H., Akusjarvi G.;
RT "Serine 192 in the tiny RS repeat of the adenoviral L4-33K splicing
RT enhancer protein is essential for function and reorganization of the
RT protein to the periphery of viral replication centers.";
RL Virology 433:273-281(2012).
RN [6]
RP FUNCTION.
RX PubMed=23552425; DOI=10.1128/jvi.00652-13;
RA Wu K., Guimet D., Hearing P.;
RT "The adenovirus L4-33K protein regulates both late gene expression patterns
RT and viral DNA packaging.";
RL J. Virol. 87:6739-6747(2013).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH DBP, AND INTERACTION WITH
RP IVA2.
RX PubMed=23388198; DOI=10.1099/vir.0.049346-0;
RA Ahi Y.S., Vemula S.V., Mittal S.K.;
RT "Adenoviral E2 IVa2 protein interacts with L4 33K protein and E2 DNA-
RT binding protein.";
RL J. Gen. Virol. 94:1325-1334(2013).
RN [8]
RP FUNCTION.
RX PubMed=25954255; DOI=10.3389/fmicb.2015.00318;
RA Ahi Y.S., Vemula S.V., Hassan A.O., Costakes G., Stauffacher C.,
RA Mittal S.K.;
RT "Adenoviral L4 33K forms ring-like oligomers and stimulates ATPase activity
RT of IVa2: implications in viral genome packaging.";
RL Front. Microbiol. 6:318-318(2015).
CC -!- FUNCTION: Promotes alternative splicing of late transcripts by
CC promoting splicing at weak 3' splice sites. Required for the temporal
CC activation of major late pre-mRNA splicing at late times of infection.
CC Induces the splicing and expression of the late capsid vertex protein.
CC {ECO:0000269|PubMed:17028184, ECO:0000269|PubMed:19176628}.
CC -!- FUNCTION: Probably functions as the small terminase that is part of the
CC molecular motor that translocates genomic DNA in empty capsid during
CC DNA packaging. This motor is located at a unique vertex and comprises
CC at least the IVa2 ATPase, the small terminase 33K and probably a
CC portal. Forms a ring-like structure of about 17 nm in which genomic DNA
CC is translocated into the capsid. Stimulates IVa2 ATPase activity in the
CC presence of the viral genome. Once the DNA is packaged, the terminase
CC detaches: the 33K protein is present in the empty particles, but not in
CC the mature virions. Also involved in virion assembly.
CC {ECO:0000269|PubMed:23388198, ECO:0000269|PubMed:23552425,
CC ECO:0000269|PubMed:25954255}.
CC -!- SUBUNIT: Homooligomer. Interacts with DBP; this interaction occurs at a
CC unique vertex during genome packaging. Interacts with IVa2; this
CC interaction occurs at a unique vertex during genome packaging and seems
CC to potentiate IVa2 and 33K oligomerization.
CC {ECO:0000269|PubMed:23388198}.
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000269|PubMed:22944109,
CC ECO:0000269|PubMed:23388198}. Note=At late time of infection,
CC reorganized from the nuclear margin to ring-like structures at viral
CC replication centers. {ECO:0000269|PubMed:22944109}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Protein 33K; Synonyms=Splicing factor 33K, L4-33K;
CC IsoId=P24940-1; Sequence=Displayed;
CC Name=Packaging protein 2; Synonyms=Packaging protein 22K, L4-22K;
CC IsoId=Q2KS03-1; Sequence=External;
CC -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC -!- DOMAIN: The tiny Arg-Ser repeat region (RS repeat) is necessary for the
CC splicing enhancer function.
CC -!- PTM: Phosphorylated in vitro by human PKA and PRKDC. PRKDC inhibits,
CC whereas PKA activates the splicing factor (By similarity).
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: All late proteins expressed from the major late promoter
CC are produced by alternative splicing and alternative polyadenylation of
CC the same gene giving rise to non-overlapping ORFs. Expression of
CC packaging protein 2 and splicing factor is controlled by a L4 promoter
CC distinct from the major late promoter.
CC -!- MISCELLANEOUS: [Isoform Protein 33K]: Spliced isoform.
CC -!- SIMILARITY: Belongs to the adenoviridae splicing factor family.
CC {ECO:0000305}.
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DR EMBL; M73260; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; F39449; WMAD51.
DR RefSeq; AP_000215.1; AC_000008.1. [P24940-1]
DR Proteomes; UP000004992; Genome.
DR GO; GO:0042025; C:host cell nucleus; IDA:UniProtKB.
DR GO; GO:0098009; C:viral terminase, large subunit; IDA:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0043484; P:regulation of RNA splicing; IDA:UniProtKB.
DR GO; GO:0019073; P:viral DNA genome packaging; IEA:InterPro.
DR GO; GO:0019072; P:viral genome packaging; IDA:UniProtKB.
DR InterPro; IPR021304; Adeno_L4-33K/L4-22K.
DR Pfam; PF11081; DUF2890; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Host nucleus; Host-virus interaction; Late protein;
KW mRNA processing; Phosphoprotein; Viral capsid assembly;
KW Viral genome packaging; Viral release from host cell.
FT CHAIN 1..229
FT /note="Protein 33K"
FT /id="PRO_0000221912"
FT REGION 1..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..199
FT /note="Necessary for nuclear subcellular location"
FT /evidence="ECO:0000250"
FT REGION 178..198
FT /note="RS-repeat; required for splicing enhancer activity"
FT /evidence="ECO:0000250"
FT COMPBIAS 18..52
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 178
FT /note="S->G: No effect on nuclear subcellular location. No
FT effect on splicing enhancer activity."
FT /evidence="ECO:0000269|PubMed:17028184,
FT ECO:0000269|PubMed:22944109"
FT MUTAGEN 191
FT /note="S->G: No effect on nuclear subcellular location. No
FT effect on splicing enhancer activity."
FT /evidence="ECO:0000269|PubMed:17028184,
FT ECO:0000269|PubMed:22944109"
FT MUTAGEN 194
FT /note="S->G: 50% redistribution of subcellular location to
FT the cytoplasm. Complete loss of splicing enhancer activity.
FT Loss of colocalization in viral replication centers."
FT /evidence="ECO:0000269|PubMed:17028184,
FT ECO:0000269|PubMed:22944109"
FT MUTAGEN 198
FT /note="S->G: No effect on nuclear subcellular location. No
FT effect on splicing enhancer activity."
FT /evidence="ECO:0000269|PubMed:17028184,
FT ECO:0000269|PubMed:22944109"
FT CONFLICT 116..117
FT /note="Missing (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 229 AA; 25164 MW; CF9B385F3842B491 CRC64;
MAPKKKLQLP PPPTDEEEYW DSQAEEVLDE EEEDMMEDWE SLDEEASEVE EVSDETPSPS
VAFPSPAPQK SATGSSMATT SAPQAPPALP VRRPNRRWDT TGTRAAHTAP AAAAAAATAA
ATQKQRRPDS KTLTKPKKST AAAAAGGGAL RLAPNEPVST RELRNRIFPT LYAIFQQSRG
QEQELKIKNR SLRSLTRSCL YHKSEDQLRR TLEDAEALFS KYCALTLKD
