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SF33K_ADE02
ID   SF33K_ADE02             Reviewed;         228 AA.
AC   P24939;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   02-JUN-2021, entry version 60.
DE   RecName: Full=Protein 33K {ECO:0000303|PubMed:6296434};
DE            Short=L4-33K {ECO:0000305};
DE   AltName: Full=Splicing factor 33K;
DE   AltName: Full=Terminase, small subunit {ECO:0000250|UniProtKB:P24940};
GN   ORFNames=L4;
OS   Human adenovirus C serotype 2 (HAdV-2) (Human adenovirus 2).
OC   Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC   Rowavirales; Adenoviridae; Mastadenovirus.
OX   NCBI_TaxID=10515;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=478297; DOI=10.1016/0378-1119(79)90081-7;
RA   Galibert F., Herisse J., Courtois G.;
RT   "Nucleotide sequence of the EcoRI-F fragment of adenovirus 2 genome.";
RL   Gene 6:1-22(1979).
RN   [2]
RP   IDENTIFICATION.
RX   PubMed=6296434; DOI=10.1128/jvi.45.1.251-263.1983;
RA   Oosterom-Dragon E.A., Anderson C.W.;
RT   "Polypeptide structure and encoding location of the adenovirus serotype 2
RT   late, nonstructural 33K protein.";
RL   J. Virol. 45:251-263(1983).
RN   [3]
RP   IDENTIFICATION.
RC   STRAIN=Human adenovirus C serotype 5;
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   [4]
RP   FUNCTION, AND MUTAGENESIS OF SER-177; SER-190; SER-193 AND SER-197.
RC   STRAIN=Human adenovirus C serotype 5;
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   [5]
RP   REVIEW, AND ALTERNATIVE SPLICING.
RX   PubMed=18508565; DOI=10.2741/3059;
RA   Akusjarvi G.;
RT   "Temporal regulation of adenovirus major late alternative RNA splicing.";
RL   Front. Biosci. 13:5006-5015(2008).
RN   [6]
RP   FUNCTION.
RC   STRAIN=Human adenovirus C serotype 5;
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   [7]
RP   PHOSPHORYLATION, AND INTERACTION WITH HOST PKA AND PRKDC.
RX   PubMed=22363758; DOI=10.1371/journal.pone.0031871;
RA   Tormanen Persson H., Aksaas A.K., Kvissel A.K., Punga T., Engstrom A.,
RA   Skalhegg B.S., Akusjarvi G.;
RT   "Two cellular protein kinases, DNA-PK and PKA, phosphorylate the adenoviral
RT   L4-33K protein and have opposite effects on L1 alternative RNA splicing.";
RL   PLoS ONE 7:E31871-E31871(2012).
RN   [8]
RP   SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-177; SER-190; SER-193 AND
RP   SER-197.
RC   STRAIN=Human adenovirus C serotype 5;
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).
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:0000250|UniProtKB:P24940}.
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:0000250|UniProtKB:P24940}.
CC   -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000269|PubMed:22944109}.
CC       Note=At late time of infection, reorganized from the nuclear margin to
CC       ring-like structures at viral replication centers.
CC       {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=P24939-1; Sequence=Displayed;
CC       Name=Packaging protein 2; Synonyms=Packaging protein 22K, L4-22K;
CC         IsoId=P0DJX1-1; 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.
CC       {ECO:0000269|PubMed:22363758}.
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; J01917; AAA92219.1; -; Genomic_DNA.
DR   RefSeq; AP_000179.1; AC_000007.1. [P24939-1]
DR   RefSeq; NP_040529.1; NC_001405.1.
DR   GeneID; 2653005; -.
DR   Proteomes; UP000008167; Genome.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   GO; GO:0019073; P:viral DNA genome packaging; IEA:InterPro.
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; mRNA splicing; Phosphoprotein; Reference proteome;
KW   Viral capsid assembly; Viral genome packaging;
KW   Viral release from host cell.
FT   CHAIN           1..228
FT                   /note="Protein 33K"
FT                   /id="PRO_0000221911"
FT   REGION          1..156
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          171..198
FT                   /note="Necessary for nuclear subcellular location"
FT   REGION          177..197
FT                   /note="RS-repeat; required for splicing enhancer activity"
FT   COMPBIAS        1..17
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..51
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         177
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         190
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         193
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         197
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"
SQ   SEQUENCE   228 AA;  25023 MW;  4AF06B5F24F880D4 CRC64;
     MAPKKKLQLP PPPPTDEEEY WDSQAEEVLD EEEEMMEDWD SLDEASEAEE VSDETPSPSV
     AFPSPAPQKL ATVPSIATTS APQAPPALPV RRPNRRWDTT GTRAAPTAPA AAAAAATAAV
     TQKQRRPDSK TLTKPKKSTA AAAAGGGALR LAPNEPVSTR ELRNRIFPTL YAIFQQSRGQ
     EQELKIKNRS LRSLTRSCLY HKSEDQLRRT LEDAEALFSK YCALTLKD
 
 
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