SPT16_DROME
ID SPT16_DROME Reviewed; 1083 AA.
AC Q8IRG6; O17045; O17046; Q7YTY1; Q86SB9; Q9W071;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=FACT complex subunit spt16;
DE AltName: Full=Facilitates chromatin transcription complex subunit SPT16;
DE AltName: Full=dSPT16;
GN Name=dre4; Synonyms=spt16; ORFNames=CG1828;
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 [MRNA] (ISOFORM A).
RA Washington A.V., Robinson P., Sliter T.J.;
RL Submitted (SEP-1997) 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, AND ALTERNATIVE SPLICING.
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] (ISOFORM B).
RC STRAIN=Berkeley; TISSUE=Testis;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 40-1083 (ISOFORM B), PROTEIN SEQUENCE OF
RP 134-410; 613-627; 670-678; 703-710 AND 760-771, FUNCTION, AND INTERACTION
RP WITH SSRP AND TRL.
RX PubMed=12815073; DOI=10.1101/gad.1086803;
RA Shimojima T., Okada M., Nakayama T., Ueda H., Okawa K., Iwamatsu A.,
RA Handa H., Hirose S.;
RT "Drosophila FACT contributes to Hox gene expression through physical and
RT functional interactions with GAGA factor.";
RL Genes Dev. 17:1605-1616(2003).
RN [6]
RP PRELIMINARY FUNCTION.
RX PubMed=1551577; DOI=10.1093/genetics/130.3.555;
RA Sliter T.J., Gilbert L.I.;
RT "Developmental arrest and ecdysteroid deficiency resulting from mutations
RT at the dre4 locus of Drosophila.";
RL Genetics 130:555-568(1992).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=12934007; DOI=10.1126/science.1085712;
RA Saunders A., Werner J., Andrulis E.D., Nakayama T., Hirose S., Reinberg D.,
RA Lis J.T.;
RT "Tracking FACT and the RNA polymerase II elongation complex through
RT chromatin in vivo.";
RL Science 301:1094-1096(2003).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Component of the FACT complex, a general chromatin factor
CC that acts to reorganize nucleosomes. The FACT complex is involved in
CC multiple processes that require DNA as a template such as mRNA
CC elongation, DNA replication and DNA repair. During transcription
CC elongation the FACT complex acts as a histone chaperone that both
CC destabilizes and restores nucleosomal structure. It facilitates the
CC passage of RNA polymerase II and transcription by promoting the
CC dissociation of one histone H2A-H2B dimer from the nucleosome, then
CC subsequently promotes the reestablishment of the nucleosome following
CC the passage of RNA polymerase II. The FACT complex is required for
CC expression of Hox genes. {ECO:0000269|PubMed:12815073}.
CC -!- SUBUNIT: Component of the FACT complex, a stable heterodimer of
CC dre4/spt16 and Ssrp. Interacts with TRL/GAGA.
CC {ECO:0000269|PubMed:12815073}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12934007}. Chromosome
CC {ECO:0000269|PubMed:12934007}. Note=Colocalizes with RNA polymerase II
CC on chromatin. Recruited to actively transcribed loci.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=B;
CC IsoId=Q8IRG6-1; Sequence=Displayed;
CC Name=A;
CC IsoId=Q8IRG6-2; Sequence=VSP_019625;
CC -!- SIMILARITY: Belongs to the peptidase M24 family. SPT16 subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: Although related to the peptidase M24 family, this protein
CC lacks conserved active site residues suggesting that it may lack
CC peptidase activity. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB80935.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAB80936.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF023269; AAB80935.1; ALT_FRAME; mRNA.
DR EMBL; AF023270; AAB80936.1; ALT_FRAME; mRNA.
DR EMBL; AE014296; AAF47587.2; -; Genomic_DNA.
DR EMBL; AE014296; AAN11502.2; -; Genomic_DNA.
DR EMBL; BT010116; AAQ22585.1; -; mRNA.
DR EMBL; AB083008; BAC54898.1; -; mRNA.
DR PIR; T13928; T13928.
DR PIR; T13929; T13929.
DR RefSeq; NP_476610.2; NM_057262.4. [Q8IRG6-2]
DR RefSeq; NP_728686.2; NM_167922.3. [Q8IRG6-1]
DR AlphaFoldDB; Q8IRG6; -.
DR SMR; Q8IRG6; -.
DR BioGRID; 63776; 8.
DR IntAct; Q8IRG6; 9.
DR STRING; 7227.FBpp0072743; -.
DR MEROPS; M24.974; -.
DR iPTMnet; Q8IRG6; -.
DR PaxDb; Q8IRG6; -.
DR PRIDE; Q8IRG6; -.
DR DNASU; 38248; -.
DR EnsemblMetazoa; FBtr0072864; FBpp0072743; FBgn0002183. [Q8IRG6-2]
DR EnsemblMetazoa; FBtr0072865; FBpp0072744; FBgn0002183. [Q8IRG6-1]
DR GeneID; 38248; -.
DR KEGG; dme:Dmel_CG1828; -.
DR CTD; 38248; -.
DR FlyBase; FBgn0002183; dre4.
DR VEuPathDB; VectorBase:FBgn0002183; -.
DR eggNOG; KOG1189; Eukaryota.
DR GeneTree; ENSGT00390000014495; -.
DR HOGENOM; CLU_004627_0_0_1; -.
DR InParanoid; Q8IRG6; -.
DR OMA; HQFFLDG; -.
DR PhylomeDB; Q8IRG6; -.
DR Reactome; R-DME-112382; Formation of RNA Pol II 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-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-DME-75955; RNA Polymerase II Transcription Elongation.
DR SignaLink; Q8IRG6; -.
DR BioGRID-ORCS; 38248; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 38248; -.
DR PRO; PR:Q8IRG6; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0002183; Expressed in oocyte and 25 other tissues.
DR ExpressionAtlas; Q8IRG6; baseline and differential.
DR Genevisible; Q8IRG6; DM.
DR GO; GO:0005829; C:cytosol; IDA:CAFA.
DR GO; GO:0035101; C:FACT complex; IDA:FlyBase.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0005703; C:polytene chromosome puff; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:FlyBase.
DR GO; GO:0031491; F:nucleosome binding; IDA:FlyBase.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:CAFA.
DR GO; GO:0047485; F:protein N-terminus binding; IMP:CAFA.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0034724; P:DNA replication-independent chromatin organization; IBA:GO_Central.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IMP:FlyBase.
DR GO; GO:1902275; P:regulation of chromatin organization; IMP:FlyBase.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IBA:GO_Central.
DR CDD; cd01091; CDC68-like; 1.
DR DisProt; DP00721; -.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.40.350.10; -; 1.
DR Gene3D; 3.90.230.10; -; 1.
DR IDEAL; IID50095; -.
DR InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR013719; DUF1747.
DR InterPro; IPR029148; FACT-Spt16_Nlobe.
DR InterPro; IPR013953; FACT_Spt16.
DR InterPro; IPR000994; Pept_M24.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR040258; Spt16.
DR InterPro; IPR033825; Spt16_M24.
DR PANTHER; PTHR13980; PTHR13980; 1.
DR Pfam; PF14826; FACT-Spt16_Nlob; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR Pfam; PF08512; Rtt106; 1.
DR Pfam; PF08644; SPT16; 1.
DR SMART; SM01285; FACT-Spt16_Nlob; 1.
DR SMART; SM01287; Rtt106; 1.
DR SMART; SM01286; SPT16; 1.
DR SUPFAM; SSF55920; SSF55920; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromosome; Coiled coil; Direct protein sequencing;
KW DNA damage; DNA repair; DNA replication; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..1083
FT /note="FACT complex subunit spt16"
FT /id="PRO_0000245174"
FT REGION 923..1083
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 466..504
FT /evidence="ECO:0000255"
FT COMPBIAS 938..988
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 989..1022
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1032..1076
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 437
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 1031
FT /note="H -> HSRRDREEARSSSHSKKHKSNSSSSSSHLKSSSSKHGSSS (in
FT isoform A)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_019625"
FT CONFLICT 345
FT /note="L -> V (in Ref. 1; AAB80935/AAB80936)"
FT /evidence="ECO:0000305"
FT CONFLICT 598
FT /note="A -> R (in Ref. 1; AAB80935/AAB80936)"
FT /evidence="ECO:0000305"
FT CONFLICT 1057
FT /note="S -> I (in Ref. 1; AAB80935/AAB80936)"
FT /evidence="ECO:0000305"
FT CONFLICT 1080..1081
FT /note="KS -> NA (in Ref. 1; AAB80935/AAB80936)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1083 AA; 123583 MW; 6A2AF4012D93D449 CRC64;
MSSFVLDKEA FVRRVKRLYT EWRAPSIGHD DALRNLDCIM SIVGVEEDVM YSKSMALQLW
LLGYELTDTI SVFCSDAVYF LTSKKKIEFL KQTQNITEEG FPEINLLVRD RTDKDQGNFE
KLIKALQNSK KGKRLGVFAK DAYPGEFSEA WKKSLTASKF EHVDISTIIA YLMCPKDESE
INNIRKASLV SMDIFNKYLK DEIMDIIDSD RKVKHNKLSD GCEAAIGEKK YTSGLDPRLL
DMAYPPIIQS GGAYSLKFSA VADKNPLHFG VIVCSLGARY KSYCSNISRT FLVNPTEAMQ
ENYTFLVSVQ EEILKLLVPG TKLCDVYEKT LDFVKKEKPS MVDNLPKSFG FAMGLEFREN
SIVIGPKCQA LLKKNMVFNL HVGISNLTNP EATDKEGKNY ALFIGDTVLV GEQSPASVMT
PSKKKIKNVG IFIKDDSDEE DVDDKKTAKE DQGTEILGRS KRNAVLESKL RNEINTEEKR
KEHQRELAQQ LNERAKDRLA RQGNSKEVEK VRKNTVSYKS ISQMPREPEV KELKLYVDKK
YETVIMPVFG IQVPFHISTI KNISQSVEGE YTYLRINFFH PGATMGRNEG GLYPQPEATF
VKEVTYRSSN VKEHGEVGAP SANLNNAFRL IKEVQKRFKT REAEEREKED LVKQDTLILS
QNKGNPKLKD LYIRPNIVTK RMTGSLEAHS NGFRYISVRG DKVDILYNNI KSAFFQPCDG
EMIILLHFHL KYAIMFGKKK HVDVQFYTEV GEITTDLGKH QHMHDRDDLA AEQAERELRH
KLKTAFKSFC EKVETMTKSV VEFDTPFREL GFPGAPFRST VTLQPTSGSL VNLTEWPPFV
ITLDDVELVH FERVQFHLRN FDMIFVFKEY NKKVAMVNAI PMNMLDHVKE WLNSCDIRYS
EGVQSLNWQK IMKTITDDPE GFFEQGGWTF LDPESGSEGE NETAESEEDE AYNPTDAESD
EESDEDSEYS EASEDSEESD EDLGSDEESG KDWSDLEREA AEEDRNHDYA ADDKPRNGKF
DSKKHGKSSK HSPSKSSKDK YNSRDKHHSS SSSGNKSSSK DKDRKRSRDD SRDNGHKSKK
SRH
