SPT4H_DROME
ID SPT4H_DROME Reviewed; 116 AA.
AC Q9TVQ5; Q9V6E5;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Transcription elongation factor SPT4;
DE AltName: Full=DRB sensitivity-inducing factor small subunit;
DE Short=DSIF small subunit;
DE AltName: Full=dSpt4;
GN Name=spt4; ORFNames=CG12372;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RA Chiang P.-W.;
RT "Characterization of Drosophila homolog of SPT4.";
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP INTERACTION WITH SPT5 AND RNA POLYMERASE II.
RX PubMed=15056674; DOI=10.1074/jbc.m402956200;
RA Zhang Z., Wu C.-H., Gilmour D.S.;
RT "Analysis of polymerase II elongation complexes by native gel
RT electrophoresis. Evidence for a novel carboxyl-terminal domain-mediated
RT termination mechanism.";
RL J. Biol. Chem. 279:23223-23228(2004).
CC -!- FUNCTION: Component of the DRB sensitivity-inducing factor complex
CC (DSIF complex), which regulates transcription elongation by RNA
CC polymerase II. DSIF enhances transcriptional pausing at sites proximal
CC to the promoter, which may facilitate the assembly of an elongation
CC competent RNA polymerase II complex. DSIF may also promote
CC transcriptional elongation within coding regions. DSIF is required for
CC the transcriptional induction of heat shock response genes and
CC regulation of genes which control anterior-posterior patterning during
CC embryonic development (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with Spt5 to form DSIF. DSIF interacts with TRX, RNA
CC polymerase II and with the FACT complex, which is composed of
CC DRE4/SPT16 and SSRP/SSRP1. DSIF can also interact with the exosome, a
CC complex with 3'-5' exoribonuclease activity which is composed of at
CC least Csl4, Dis3, Mtr3, Rrp4, Rrp6, Rrp40, Rrp42, Rrp46 and Ski6. DSIF
CC may also interact with the positive transcription elongation factor b
CC complex (P-TEFb complex), which is composed of Cdk9 and cyclin-T
CC (CycT). {ECO:0000269|PubMed:15056674}.
CC -!- INTERACTION:
CC Q9TVQ5; Q9V460: Spt5; NbExp=2; IntAct=EBI-165626, EBI-134850;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SPT4 family. {ECO:0000305}.
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DR EMBL; AF108353; AAF14223.1; -; mRNA.
DR EMBL; AF109133; AAF14224.1; -; Genomic_DNA.
DR EMBL; AE013599; AAF58482.2; -; Genomic_DNA.
DR EMBL; AY075424; AAL68240.1; -; mRNA.
DR RefSeq; NP_610802.1; NM_136958.5.
DR AlphaFoldDB; Q9TVQ5; -.
DR SMR; Q9TVQ5; -.
DR BioGRID; 62161; 4.
DR IntAct; Q9TVQ5; 1.
DR STRING; 7227.FBpp0086953; -.
DR PaxDb; Q9TVQ5; -.
DR PRIDE; Q9TVQ5; -.
DR DNASU; 36387; -.
DR EnsemblMetazoa; FBtr0087840; FBpp0086953; FBgn0028683.
DR GeneID; 36387; -.
DR KEGG; dme:Dmel_CG12372; -.
DR UCSC; CG12372-RA; d. melanogaster.
DR CTD; 36387; -.
DR FlyBase; FBgn0028683; spt4.
DR VEuPathDB; VectorBase:FBgn0028683; -.
DR eggNOG; KOG3490; Eukaryota.
DR GeneTree; ENSGT00390000018559; -.
DR HOGENOM; CLU_138052_3_0_1; -.
DR InParanoid; Q9TVQ5; -.
DR OMA; FDGMIAV; -.
DR OrthoDB; 1617752at2759; -.
DR PhylomeDB; Q9TVQ5; -.
DR Reactome; R-DME-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-DME-113418; Formation of the Early Elongation Complex.
DR Reactome; R-DME-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-DME-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-DME-75955; RNA Polymerase II Transcription Elongation.
DR BioGRID-ORCS; 36387; 1 hit in 1 CRISPR screen.
DR GenomeRNAi; 36387; -.
DR PRO; PR:Q9TVQ5; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0028683; Expressed in ovary and 11 other tissues.
DR ExpressionAtlas; Q9TVQ5; baseline and differential.
DR Genevisible; Q9TVQ5; DM.
DR GO; GO:0032044; C:DSIF complex; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0005705; C:polytene chromosome interband; IDA:UniProtKB.
DR GO; GO:0005703; C:polytene chromosome puff; IDA:UniProtKB.
DR GO; GO:0008023; C:transcription elongation factor complex; IDA:FlyBase.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006325; P:chromatin organization; IBA:GO_Central.
DR GO; GO:0006397; P:mRNA processing; IBA:GO_Central.
DR GO; GO:0032785; P:negative regulation of DNA-templated transcription, elongation; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0032786; P:positive regulation of DNA-templated transcription, elongation; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0034243; P:regulation of transcription elongation from RNA polymerase II promoter; IBA:GO_Central.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IDA:UniProtKB.
DR CDD; cd07973; Spt4; 1.
DR Gene3D; 3.30.40.210; -; 1.
DR InterPro; IPR029040; RPABC4/Spt4.
DR InterPro; IPR009287; Spt4.
DR InterPro; IPR022800; Spt4/RpoE2_Znf.
DR InterPro; IPR038510; Spt4_sf.
DR PANTHER; PTHR12882; PTHR12882; 1.
DR Pfam; PF06093; Spt4; 1.
DR PIRSF; PIRSF025023; Spt4; 1.
DR SMART; SM01389; Spt4; 1.
DR SUPFAM; SSF63393; SSF63393; 1.
PE 1: Evidence at protein level;
KW Activator; Metal-binding; Nucleus; Reference proteome; Repressor;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..116
FT /note="Transcription elongation factor SPT4"
FT /id="PRO_0000210332"
FT ZN_FING 16..36
FT /note="C4-type"
FT /evidence="ECO:0000255"
FT REGION 1..40
FT /note="Interaction with Spt5"
FT /evidence="ECO:0000250"
SQ SEQUENCE 116 AA; 13332 MW; A4EF4580DCAA8A57 CRC64;
MAFDAIPKDL RGLRACLVCS LVKSFDQFET DGCENCEEFL RMKNNKDNVY DHTSNNFDGI
IALTTPTDSW VAKWQRLSRF TRGIYAISVS GTLPQSTLRD MKNRGIVYKS RDRSQR
