ID   SPT4H_BOVIN             Reviewed;         117 AA.
AC   Q3SYX6;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Transcription elongation factor SPT4;
DE   AltName: Full=DRB sensitivity-inducing factor small subunit;
DE            Short=DSIF small subunit;
GN   Name=SUPT4H1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the DRB sensitivity-inducing factor complex
CC       (DSIF complex), which regulates mRNA processing and transcription
CC       elongation by RNA polymerase II. DSIF positively regulates mRNA capping
CC       by stimulating the mRNA guanylyltransferase activity of RNGTT/CAP1A.
CC       DSIF also acts cooperatively with the negative elongation factor
CC       complex (NELF complex) to enhance transcriptional pausing at sites
CC       proximal to the promoter. Transcriptional pausing may facilitate the
CC       assembly of an elongation competent RNA polymerase II complex. DSIF and
CC       NELF promote pausing by inhibition of the transcription elongation
CC       factor TFIIS/S-II. TFIIS/S-II binds to RNA polymerase II at
CC       transcription pause sites and stimulates the weak intrinsic nuclease
CC       activity of the enzyme. Cleavage of blocked transcripts by RNA
CC       polymerase II promotes the resumption of transcription from the new 3'
CC       terminus and may allow repeated attempts at transcription through
CC       natural pause sites (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with SUPT5H to form DSIF. DSIF interacts with the
CC       positive transcription elongation factor b complex (P-TEFb complex),
CC       which is composed of CDK9 and cyclin-T (CCNT1 or CCNT2). DSIF interacts
CC       with RNA polymerase II, and this interaction is reduced by
CC       phosphorylation of the C-terminal domain (CTD) of POLR2A by P-TEFb.
CC       DSIF also interacts with the NELF complex, which is composed of NELFA,
CC       NELFB, NELFD and NELFE, and this interaction occurs following prior
CC       binding of DSIF to RNA polymerase II. DSIF also interacts with
CC       PRMT1/HRMT1L2, HTATSF1/TATSF1, RNGTT/CAP1A, PRMT5/SKB1, SUPT6H, and can
CC       interact with PIN1 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SPT4 family. {ECO:0000305}.
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DR   EMBL; BT025461; ABF57417.1; -; mRNA.
DR   EMBL; BC103340; AAI03341.1; -; mRNA.
DR   RefSeq; NP_001029964.1; NM_001034792.2.
DR   AlphaFoldDB; Q3SYX6; -.
DR   SMR; Q3SYX6; -.
DR   STRING; 9913.ENSBTAP00000004389; -.
DR   PaxDb; Q3SYX6; -.
DR   GeneID; 616425; -.
DR   KEGG; bta:616425; -.
DR   CTD; 6827; -.
DR   eggNOG; KOG3490; Eukaryota.
DR   HOGENOM; CLU_138052_3_0_1; -.
DR   InParanoid; Q3SYX6; -.
DR   OrthoDB; 1617752at2759; -.
DR   TreeFam; TF300105; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0032044; C:DSIF complex; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0032786; P:positive regulation of DNA-templated transcription, elongation; IEA:InterPro.
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   3: Inferred from homology;
KW   Acetylation; Activator; Metal-binding; Nucleus; Reference proteome;
KW   Repressor; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P63272"
FT   CHAIN           2..117
FT                   /note="Transcription elongation factor SPT4"
FT                   /id="PRO_0000246082"
FT   ZN_FING         16..36
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255"
FT   REGION          2..40
FT                   /note="Interaction with SUPT5H"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P63272"
SQ   SEQUENCE   117 AA;  13193 MW;  09EDF007501D0F03 CRC64;
     MALETVPKDL RHLRACLLCS LVKTIDQFEY DGCDNCDAYL QMKGNREMVY DCTSSSFDGI
     IAMMSPEDSW VSKWQRVSNF KPGVYAVSVT GRLPQGIVRE LKSRGVAYKS RDTAIKT