SSRP1_DROME
ID SSRP1_DROME Reviewed; 723 AA.
AC Q05344; Q86NM5; Q9W1J4;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=FACT complex subunit Ssrp1;
DE AltName: Full=Chorion-factor 5;
DE AltName: Full=Facilitates chromatin transcription complex subunit Ssrp1;
DE AltName: Full=Recombination signal sequence recognition protein;
DE AltName: Full=Single-strand recognition protein;
DE AltName: Full=dSSRP1;
GN Name=Ssrp; Synonyms=CF5, SSRP1; ORFNames=CG4817;
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].
RC TISSUE=Ovary;
RX PubMed=7688122; DOI=10.1073/pnas.90.14.6488;
RA Hsu T., King D.L., Labonne C., Kafatos F.C.;
RT "A Drosophila single-strand DNA/RNA-binding factor contains a high-
RT mobility-group box and is enriched in the nucleolus.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:6488-6492(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8479916; DOI=10.1093/nar/21.7.1643;
RA Bruhn S.L., Housman D.E., Lippard S.J.;
RT "Isolation and characterization of cDNA clones encoding the Drosophila
RT homolog of the HMG-box SSRP family that recognizes specific DNA
RT structures.";
RL Nucleic Acids Res. 21:1643-1646(1993).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
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 (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PROTEIN SEQUENCE OF 68-74; 305-309; 326-334 AND 414-420, FUNCTION, AND
RP INTERACTION WITH DRE4 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 [7]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH CHD1.
RX PubMed=10199952; DOI=10.1007/s004120050347;
RA Kelley D.E., Stokes D.G., Perry R.P.;
RT "CHD1 interacts with SSRP1 and depends on both its chromodomain and its
RT ATPase/helicase-like domain for proper association with chromatin.";
RL Chromosoma 108:10-25(1999).
RN [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-443 AND SER-628, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-443; SER-664; SER-668;
RP THR-669; SER-670 AND SER-671, AND IDENTIFICATION BY 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).
RN [11]
RP STRUCTURE BY NMR OF 555-624.
RX PubMed=16041486; DOI=10.1007/s10858-005-3662-3;
RA Kasai N., Tsunaka Y., Ohki I., Hirose S., Morikawa K., Tate S.;
RT "Solution structure of the HMG-box domain in the SSRP1 subunit of FACT.";
RL J. Biomol. NMR 32:83-88(2005).
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. Binds specifically to single-stranded
CC DNA and RNA with highest affinity for nucleotides G and U. The FACT
CC complex is required for expression of Hox genes.
CC {ECO:0000269|PubMed:12815073}.
CC -!- SUBUNIT: Component of the FACT complex, a stable heterodimer of
CC dre4/spt16 and Ssrp. Interacts with CHD1 and TRL/GAGA.
CC {ECO:0000269|PubMed:10199952, ECO:0000269|PubMed:12815073}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12934007,
CC ECO:0000303|PubMed:10199952}. Chromosome {ECO:0000269|PubMed:12934007,
CC ECO:0000303|PubMed:10199952}. Nucleus, nucleolus
CC {ECO:0000269|PubMed:12934007}. Note=Colocalizes with RNA polymerase II
CC on chromatin. Recruited to actively transcribed loci.
CC {ECO:0000269|PubMed:12934007}.
CC -!- TISSUE SPECIFICITY: Expressed at highest levels in nurse cells of the
CC ovary.
CC -!- DEVELOPMENTAL STAGE: Abundant throughout oogenesis and embryogenesis,
CC decreases during larval stages and increases again in pupae.
CC -!- SIMILARITY: Belongs to the SSRP1 family. {ECO:0000305}.
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DR EMBL; L08825; AAA28914.1; -; mRNA.
DR EMBL; X68408; CAA48471.1; -; mRNA.
DR EMBL; AE013599; AAF47064.1; -; Genomic_DNA.
DR EMBL; BT004831; AAO45187.1; -; mRNA.
DR PIR; A48217; A48217.
DR PIR; S33688; S33688.
DR RefSeq; NP_523830.2; NM_079106.3.
DR PDB; 1WXL; NMR; -; A=555-624.
DR PDBsum; 1WXL; -.
DR AlphaFoldDB; Q05344; -.
DR BMRB; Q05344; -.
DR SMR; Q05344; -.
DR BioGRID; 63363; 11.
DR IntAct; Q05344; 3.
DR STRING; 7227.FBpp0072151; -.
DR iPTMnet; Q05344; -.
DR PaxDb; Q05344; -.
DR PRIDE; Q05344; -.
DR DNASU; 37767; -.
DR EnsemblMetazoa; FBtr0072242; FBpp0072151; FBgn0010278.
DR GeneID; 37767; -.
DR KEGG; dme:Dmel_CG4817; -.
DR CTD; 37767; -.
DR FlyBase; FBgn0010278; Ssrp.
DR VEuPathDB; VectorBase:FBgn0010278; -.
DR eggNOG; KOG0526; Eukaryota.
DR GeneTree; ENSGT00940000167382; -.
DR HOGENOM; CLU_017374_2_0_1; -.
DR InParanoid; Q05344; -.
DR OMA; SKQPGKC; -.
DR OrthoDB; 915055at2759; -.
DR PhylomeDB; Q05344; -.
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; Q05344; -.
DR BioGRID-ORCS; 37767; 1 hit in 1 CRISPR screen.
DR EvolutionaryTrace; Q05344; -.
DR GenomeRNAi; 37767; -.
DR PRO; PR:Q05344; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0010278; Expressed in secondary oocyte and 28 other tissues.
DR ExpressionAtlas; Q05344; baseline and differential.
DR Genevisible; Q05344; 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:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:CAFA.
DR GO; GO:0070087; F:chromo shadow domain binding; IMP:CAFA.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0031492; F:nucleosomal DNA 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:0043621; F:protein self-association; IDA:FlyBase.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:UniProtKB.
DR GO; GO:0030707; P:ovarian follicle cell development; IMP:FlyBase.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IMP:UniProtKB.
DR GO; GO:1902275; P:regulation of chromatin organization; IMP:FlyBase.
DR GO; GO:0051101; P:regulation of DNA binding; IMP:FlyBase.
DR DisProt; DP00720; -.
DR Gene3D; 1.10.30.10; -; 1.
DR Gene3D; 2.30.29.220; -; 1.
DR Gene3D; 2.30.29.30; -; 2.
DR IDEAL; IID50086; -.
DR InterPro; IPR013719; DUF1747.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR035417; POB3_N.
DR InterPro; IPR000969; SSrcognition.
DR InterPro; IPR024954; SSRP1_dom.
DR InterPro; IPR038167; SSRP1_sf.
DR Pfam; PF00505; HMG_box; 1.
DR Pfam; PF17292; POB3_N; 1.
DR Pfam; PF08512; Rtt106; 1.
DR Pfam; PF03531; SSrecog; 1.
DR PRINTS; PR00887; SSRCOGNITION.
DR SMART; SM00398; HMG; 1.
DR SMART; SM01287; Rtt106; 1.
DR SUPFAM; SSF47095; SSF47095; 1.
DR PROSITE; PS50118; HMG_BOX_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromosome; Direct protein sequencing; DNA damage;
KW DNA repair; DNA replication; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding; Transcription; Transcription regulation.
FT CHAIN 1..723
FT /note="FACT complex subunit Ssrp1"
FT /id="PRO_0000048604"
FT DNA_BIND 555..621
FT /note="HMG box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 459..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 586..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..482
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..510
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..554
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..646
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 674..703
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 704..723
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 443
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656,
FT ECO:0000269|PubMed:18327897"
FT MOD_RES 628
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT MOD_RES 664
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 668
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 669
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 670
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 671
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 13
FT /note="E -> Q (in Ref. 1; AAA28914)"
FT /evidence="ECO:0000305"
FT CONFLICT 33
FT /note="K -> E (in Ref. 1; AAA28914)"
FT /evidence="ECO:0000305"
FT CONFLICT 212
FT /note="G -> R (in Ref. 1; AAA28914)"
FT /evidence="ECO:0000305"
FT CONFLICT 428
FT /note="M -> T (in Ref. 1; AAA28914)"
FT /evidence="ECO:0000305"
FT CONFLICT 498
FT /note="V -> E (in Ref. 1; AAA28914)"
FT /evidence="ECO:0000305"
FT CONFLICT 504
FT /note="D -> E (in Ref. 1; AAA28914)"
FT /evidence="ECO:0000305"
FT CONFLICT 573
FT /note="I -> Y (in Ref. 1; AAA28914)"
FT /evidence="ECO:0000305"
FT CONFLICT 681
FT /note="K -> T (in Ref. 5; AAO45187)"
FT /evidence="ECO:0000305"
FT HELIX 561..576
FT /evidence="ECO:0007829|PDB:1WXL"
FT HELIX 582..594
FT /evidence="ECO:0007829|PDB:1WXL"
FT HELIX 599..614
FT /evidence="ECO:0007829|PDB:1WXL"
FT TURN 615..617
FT /evidence="ECO:0007829|PDB:1WXL"
FT HELIX 618..620
FT /evidence="ECO:0007829|PDB:1WXL"
SQ SEQUENCE 723 AA; 81533 MW; DE8017F75C6CA207 CRC64;
MTDSLEYNDI NAEVRGVLCS GRLKMTEQNI IFKNTKTGKV EQISAEDIDL INSQKFVGTW
GLRVFTKGGV LHRFTGFRDS EHEKLGKFIK AAYSQEMVEK EMCVKGWNWG TARFMGSVLS
FDKESKTIFE VPLSHVSQCV TGKNEVTLEF HQNDDAPVGL LEMRFHIPAV ESAEEDPVDK
FHQNVMSKAS VISASGESIA IFREIQILTP RGRYDIKIFS TFFQLHGKTF DYKIPMDSVL
RLFMLPHKDS RQMFFVLSLD PPIKQGQTRY HYLVLLFAPD EETTIELPFS EAELRDKYEG
KLEKEISGPV YEVMGKVMKV LIGRKITGPG NFIGHSGTAA VGCSFKAAAG YLYPLERGFI
YIHKPPLHIR FEEISSVNFA RSGGSTRSFD FEVTLKNGTV HIFSSIEKEE YAKLFDYITQ
KKLHVSNMGK DKSGYKDVDF GDSDNENEPD AYLARLKAEA REKEEDDDDG DSDEESTDED
FKPNENESDV AEEYDSNVES DSDDDSDASG GGGDSDGAKK KKEKKSEKKE KKEKKHKEKE
RTKKPSKKKK DSGKPKRATT AFMLWLNDTR ESIKRENPGI KVTEIAKKGG EMWKELKDKS
KWEDAAAKDK QRYHDEMRNY KPEAGGDSDN EKGGKSSKKR KTEPSPSKKA NTSGSGFKSK
EYISDDDSTS SDDEKDNEPA KKKSKPPSDG DAKKKKAKSE SEPEESEEDS NASDEDEEDE
ASD
