SPT5H_CHICK
ID SPT5H_CHICK Reviewed; 1079 AA.
AC Q5ZI08;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Transcription elongation factor SPT5;
DE AltName: Full=DRB sensitivity-inducing factor large subunit;
DE Short=DSIF large subunit;
GN Name=SUPT5H; ORFNames=RCJMB04_31j17;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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 acts cooperatively with the
CC negative elongation factor complex (NELF complex) to enhance
CC transcriptional pausing at sites proximal to the promoter.
CC Transcriptional pausing may facilitate the assembly of an elongation
CC competent RNA polymerase II complex (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with SUPT4H1 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
CC WHSC2/NELFA, COBRA1/NELFB, TH1L/NELFD and RDBP/NELFE, and this
CC interaction occurs following prior binding of DSIF to RNA polymerase
CC II. Also interacts with SUPT6H (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- PTM: Phosphorylated. Phosphorylation by P-TEFb alleviates
CC transcriptional pausing. Phosphorylation may also stimulate interaction
CC with PIN1. Bulk phosphorylation occurs predominantly in mitosis (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SPT5 family. {ECO:0000305}.
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DR EMBL; AJ720976; CAG32635.1; -; mRNA.
DR RefSeq; NP_001026555.1; NM_001031384.1.
DR AlphaFoldDB; Q5ZI08; -.
DR SMR; Q5ZI08; -.
DR STRING; 9031.ENSGALP00000023081; -.
DR PaxDb; Q5ZI08; -.
DR GeneID; 426493; -.
DR KEGG; gga:426493; -.
DR CTD; 6829; -.
DR VEuPathDB; HostDB:geneid_426493; -.
DR eggNOG; KOG1999; Eukaryota.
DR InParanoid; Q5ZI08; -.
DR OrthoDB; 828863at2759; -.
DR PhylomeDB; Q5ZI08; -.
DR PRO; PR:Q5ZI08; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0032044; C:DSIF complex; ISS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0032784; P:regulation of DNA-templated transcription, elongation; IEA:InterPro.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IBA:GO_Central.
DR CDD; cd06081; KOW_Spt5_1; 1.
DR CDD; cd06082; KOW_Spt5_2; 1.
DR CDD; cd06083; KOW_Spt5_3; 1.
DR CDD; cd06084; KOW_Spt5_4; 1.
DR CDD; cd06085; KOW_Spt5_5; 1.
DR CDD; cd06086; KOW_Spt5_6; 1.
DR CDD; cd09888; NGN_Euk; 1.
DR Gene3D; 2.30.30.30; -; 3.
DR Gene3D; 3.30.70.940; -; 1.
DR InterPro; IPR005824; KOW.
DR InterPro; IPR041973; KOW_Spt5_1.
DR InterPro; IPR041975; KOW_Spt5_2.
DR InterPro; IPR041976; KOW_Spt5_3.
DR InterPro; IPR041977; KOW_Spt5_4.
DR InterPro; IPR041978; KOW_Spt5_5.
DR InterPro; IPR041980; KOW_Spt5_6.
DR InterPro; IPR005100; NGN-domain.
DR InterPro; IPR006645; NGN_dom.
DR InterPro; IPR036735; NGN_dom_sf.
DR InterPro; IPR039385; NGN_Euk.
DR InterPro; IPR014722; Rib_L2_dom2.
DR InterPro; IPR039659; SPT5.
DR InterPro; IPR024945; Spt5_C_dom.
DR InterPro; IPR022581; Spt5_N.
DR InterPro; IPR017071; TF_Spt5_eukaryote.
DR InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR PANTHER; PTHR11125; PTHR11125; 1.
DR Pfam; PF00467; KOW; 1.
DR Pfam; PF03439; Spt5-NGN; 1.
DR Pfam; PF11942; Spt5_N; 1.
DR PIRSF; PIRSF036945; Spt5; 1.
DR SMART; SM01104; CTD; 1.
DR SMART; SM00739; KOW; 6.
DR SMART; SM00738; NGN; 1.
DR SUPFAM; SSF50104; SSF50104; 1.
PE 2: Evidence at transcript level;
KW Activator; Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..1079
FT /note="Transcription elongation factor SPT5"
FT /id="PRO_0000208471"
FT DOMAIN 270..303
FT /note="KOW 1"
FT DOMAIN 417..448
FT /note="KOW 2"
FT DOMAIN 469..500
FT /note="KOW 3"
FT DOMAIN 591..624
FT /note="KOW 4"
FT DOMAIN 696..729
FT /note="KOW 5"
FT REPEAT 746..751
FT /note="CTR1-1; approximate"
FT REPEAT 752..757
FT /note="CTR1-2"
FT REPEAT 758..763
FT /note="CTR1-3"
FT REPEAT 764..770
FT /note="CTR1-4"
FT REPEAT 773..779
FT /note="CTR1-5"
FT REPEAT 780..786
FT /note="CTR1-6"
FT REPEAT 788..794
FT /note="CTR1-7"
FT REPEAT 795..801
FT /note="CTR1-8"
FT REPEAT 803..809
FT /note="CTR1-9"
FT REPEAT 836..843
FT /note="CTR2-1"
FT REPEAT 846..854
FT /note="CTR2-2; approximate"
FT REPEAT 855..861
FT /note="CTR2-3; approximate"
FT REPEAT 873..877
FT /note="CTR2-4; half-length"
FT REPEAT 888..894
FT /note="CTR2-5; approximate"
FT REPEAT 896..903
FT /note="CTR2-6"
FT REPEAT 908..913
FT /note="CTR2-7; approximate"
FT REPEAT 916..922
FT /note="CTR2-8"
FT REPEAT 924..931
FT /note="CTR2-9"
FT REPEAT 935..942
FT /note="CTR2-10"
FT REGION 1..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..267
FT /note="Interaction with SUPT4H1"
FT /evidence="ECO:0000250"
FT REGION 310..417
FT /note="Interaction with RNA polymerase II"
FT /evidence="ECO:0000250"
FT REGION 664..700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 739..970
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 746..809
FT /note="9 X 7 AA approximate tandem repeats of G-S-[QR]-T-P-
FT X-[YQ], motif CTR1"
FT REGION 836..942
FT /note="10 X 8 AA approximate tandem repeats of P-[TS]-P-S-
FT P-[QA]-[SG]-Y, motif CTR2"
FT COMPBIAS 1..29
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..60
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..76
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 739..823
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 842..864
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 865..939
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 940..954
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 767
FT /note="Phosphothreonine; by CDK9"
FT /evidence="ECO:0000250"
FT MOD_RES 776
FT /note="Phosphothreonine; by CDK9"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1079 AA; 119982 MW; 3A865A238804474B CRC64;
MSDSDDSNFS EEESEHSSEA EEAEEAEAEE ERASAAGSEK EEVEEEEEEE YDEEEEEEDD
DRPAKKPRHG GFILDEADVD DEYEDEDQWE DGAEDILEKE EIEASNIDNV VLDEDRSGAR
RLQNLWRDQR EEELGEYYMK KYAKSSVGET VYGGSDELSD DITQQQLLPG VKDPNLWTVK
CKIGEERATA IALMRKFIAY QFTDTPLQIK SVVAPEHVKG YIYVEAYKQT HVKQAIEGVG
NLRMGYWNQQ MVPIKEMTDV LKVVKEVTNL KPKSWVRLKR GIYKDDIAQV DYVEPSQNQI
SLKMIPRIDF DRIKARMSLK DWFAKRKKFK RPPQRLFDAE KIRSLGGDVA SDGDFLIFEG
NRYSRKGFLF KSFAMSAVIT EGVKPTLSEL EKFEDQPEGI DLEVVTESTG KEREHNFQPG
DNVEVCEGEL INLQGKILSV DGNKITIMPK HEDLKDMLEF PAQELRKYFK MGDHVKVIAG
RFEGDTGLIV RVEENFVILF SDLTMHELKV LPRDLQLCSE TASGVDVGGQ HEWGELVQLD
PQTVGVIVRL ERETFQVLNM YGKVVTVRHQ AVTRKKDNRF AVALDSEQNN IHVKDIVKVI
DGPHSGREGE IRHLFRGFAF LHCKKLVENG GMFVCKTRHL VLAGGSKPRD VTNFTVGSFA
PMSPRISSPM HPSGAGQRGG FGGGGMSRGR GRRDNDLIGQ TVRISQGPYK GYIGVVKDAT
ESTARVELHS TCQTISVDRQ RLTTVGSRRP GGMTSTYGRT PMYGSQTPMY GSGSRTPMYG
SQTPLHDGSR TPHYGSQTPL HDGSRTPAQS GAWDPNNPNT PSRADEDFEY GFDDEPTPSP
QGYGGTPNPQ TPGYPDPSSP QVTQPYNPQT PGTPAMYNTD QFSPYAVPSP QGSYQPSPSP
QSYHQVAPSP VGYQNTHSPA SYHPTPSPMA YQASPSPSPV GYSPMTPGAP SPGGYNPHTP
GSGIEQSSSD WVTTDIQVKV RDTYLDSQAV GQTGVIRSVT GGMCSVYLKD SEKVVSISSE
HLEPVTPTKS NKVKVILGED REATGILLSI DGEDGIVRMD LDEQLKILNL RFLGKLLEA
