SPT4H_MACFA
ID SPT4H_MACFA Reviewed; 117 AA.
AC Q4R941;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Transcription elongation factor SPT4;
DE AltName: Full=DRB sensitivity-inducing factor small subunit;
DE Short=DSIF small subunit;
GN Name=SUPT4H1; ORFNames=QtsA-10763;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-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; AB168256; BAE00380.1; -; mRNA.
DR RefSeq; NP_001271726.1; NM_001284797.1.
DR AlphaFoldDB; Q4R941; -.
DR SMR; Q4R941; -.
DR STRING; 9541.XP_005583886.1; -.
DR Ensembl; ENSMFAT00000008997; ENSMFAP00000034767; ENSMFAG00000003856.
DR GeneID; 101925811; -.
DR CTD; 6827; -.
DR VEuPathDB; HostDB:ENSMFAG00000003856; -.
DR eggNOG; KOG3490; Eukaryota.
DR GeneTree; ENSGT00390000018559; -.
DR OMA; FDGMIAV; -.
DR OrthoDB; 1617752at2759; -.
DR Proteomes; UP000233100; Chromosome 16.
DR Bgee; ENSMFAG00000003856; Expressed in bone marrow and 13 other tissues.
DR GO; GO:0032044; C:DSIF complex; ISS:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0034244; P:negative regulation of transcription elongation from RNA polymerase II promoter; IEA:Ensembl.
DR GO; GO:0032786; P:positive regulation of DNA-templated transcription, elongation; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IEA:Ensembl.
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_0000210326"
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
