SLBP_DROME
ID SLBP_DROME Reviewed; 276 AA.
AC Q9VAN6; Q9GU71;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Histone RNA hairpin-binding protein;
DE AltName: Full=Histone stem-loop-binding protein;
GN Name=Slbp; ORFNames=CG11886;
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, FUNCTION, AND DEVELOPMENTAL STAGE.
RC STRAIN=Oregon-R; TISSUE=Embryo;
RX PubMed=11157774; DOI=10.1101/gad.862801;
RA Sullivan E.O., Santiago C., Parker E.D., Dominski Z., Yang X.,
RA Lanzotti D.J., Ingledue T.C., Marzluff W.F., Duronio R.J.;
RT "Drosophila stem loop binding protein coordinates accumulation of mature
RT histone mRNA with cell cycle progression.";
RL Genes Dev. 15:173-187(2001).
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.
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].
RC STRAIN=Berkeley; TISSUE=Head, and Ovary;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24; SER-29; SER-118; THR-120;
RP SER-123; SER-127; SER-131; TYR-177 AND SER-182, AND IDENTIFICATION BY MASS
RP 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 [6]
RP FUNCTION, AND INTERACTION WITH SYM AND CPSF73.
RX PubMed=19450530; DOI=10.1016/j.molcel.2009.04.024;
RA Sullivan K.D., Steiniger M., Marzluff W.F.;
RT "A core complex of CPSF73, CPSF100, and Symplekin may form two different
RT cleavage factors for processing of poly(A) and histone mRNAs.";
RL Mol. Cell 34:322-332(2009).
CC -!- FUNCTION: Involved in histone pre-mRNA 3' processing and couples
CC histone mRNA production with the cell cycle. Both maternal and zygotic
CC proteins play an essential and vital function for development.
CC {ECO:0000269|PubMed:11157774, ECO:0000269|PubMed:19450530}.
CC -!- SUBUNIT: Interacts with Sym and Cpsf73. {ECO:0000269|PubMed:19450530}.
CC -!- TISSUE SPECIFICITY: In late embryos, expression is restricted to
CC proliferating (CNS and PNS) and endoreplicating (midgut) cell
CC populations.
CC -!- DEVELOPMENTAL STAGE: Expressed both zygotically and maternally.
CC Expression is highest in early embryos and adult females.
CC {ECO:0000269|PubMed:11157774}.
CC -!- SIMILARITY: Belongs to the SLBP family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF186594; AAG16723.1; -; Genomic_DNA.
DR EMBL; AF258617; AAF71752.1; -; mRNA.
DR EMBL; AE014297; AAF56867.1; -; Genomic_DNA.
DR EMBL; AY089675; AAL90413.1; -; mRNA.
DR EMBL; AY118836; AAM50696.1; -; mRNA.
DR RefSeq; NP_477480.1; NM_058132.3.
DR PDB; 4TUW; X-ray; 2.90 A; A/B=184-276.
DR PDB; 4TUX; X-ray; 3.08 A; A/B=184-276.
DR PDB; 4TV0; X-ray; 2.60 A; A=184-267.
DR PDBsum; 4TUW; -.
DR PDBsum; 4TUX; -.
DR PDBsum; 4TV0; -.
DR AlphaFoldDB; Q9VAN6; -.
DR BMRB; Q9VAN6; -.
DR SMR; Q9VAN6; -.
DR BioGRID; 68319; 7.
DR STRING; 7227.FBpp0084778; -.
DR iPTMnet; Q9VAN6; -.
DR PaxDb; Q9VAN6; -.
DR DNASU; 43448; -.
DR EnsemblMetazoa; FBtr0085409; FBpp0084778; FBgn0041186.
DR GeneID; 43448; -.
DR KEGG; dme:Dmel_CG11886; -.
DR CTD; 7884; -.
DR FlyBase; FBgn0041186; Slbp.
DR VEuPathDB; VectorBase:FBgn0041186; -.
DR eggNOG; KOG3934; Eukaryota.
DR GeneTree; ENSGT00940000170890; -.
DR HOGENOM; CLU_079454_0_0_1; -.
DR InParanoid; Q9VAN6; -.
DR OMA; TPYKRRH; -.
DR OrthoDB; 1368804at2759; -.
DR PhylomeDB; Q9VAN6; -.
DR Reactome; R-DME-159230; Transport of the SLBP Dependant Mature mRNA.
DR Reactome; R-DME-73856; RNA Polymerase II Transcription Termination.
DR Reactome; R-DME-77588; SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs.
DR BioGRID-ORCS; 43448; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 43448; -.
DR PRO; PR:Q9VAN6; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0041186; Expressed in secondary oocyte and 62 other tissues.
DR ExpressionAtlas; Q9VAN6; baseline and differential.
DR Genevisible; Q9VAN6; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0071204; C:histone pre-mRNA 3'end processing complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0071207; F:histone pre-mRNA stem-loop binding; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0035613; F:RNA stem-loop binding; IDA:FlyBase.
DR GO; GO:1990825; F:sequence-specific mRNA binding; IMP:CAFA.
DR GO; GO:0007076; P:mitotic chromosome condensation; IMP:FlyBase.
DR GO; GO:0006398; P:mRNA 3'-end processing by stem-loop binding and cleavage; IDA:FlyBase.
DR GO; GO:0051028; P:mRNA transport; IBA:GO_Central.
DR DisProt; DP00144; -.
DR Gene3D; 1.10.8.1120; -; 1.
DR InterPro; IPR026502; SLBP1/SLBP2.
DR InterPro; IPR029344; SLBP_RNA_bind.
DR InterPro; IPR038294; SLBP_RNA_bind_sf.
DR PANTHER; PTHR17408; PTHR17408; 1.
DR Pfam; PF15247; SLBP_RNA_bind; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Developmental protein; mRNA processing; Phosphoprotein;
KW Reference proteome; RNA-binding.
FT CHAIN 1..276
FT /note="Histone RNA hairpin-binding protein"
FT /id="PRO_0000100361"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 50..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 104..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 191..260
FT /note="RNA-binding"
FT /evidence="ECO:0000250"
FT REGION 254..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..175
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..192
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..233
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 120
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 123
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 131
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 177
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 3
FT /note="C -> G (in Ref. 1; AAG16723)"
FT /evidence="ECO:0000305"
FT CONFLICT 82
FT /note="G -> C (in Ref. 1; AAG16723)"
FT /evidence="ECO:0000305"
FT HELIX 192..205
FT /evidence="ECO:0007829|PDB:4TV0"
FT HELIX 209..212
FT /evidence="ECO:0007829|PDB:4TUW"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:4TUW"
FT HELIX 239..250
FT /evidence="ECO:0007829|PDB:4TV0"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:4TUW"
SQ SEQUENCE 276 AA; 30624 MW; 915C9F308F09C607 CRC64;
MLCEDQHMSV ENTPQKGSGS LNSSASSISI DVKPTMQSWA QEVRAEFGHS DEASSSLNSS
AASCGSLAKK ETADGNLESK DGEGREMAFE FLDGVNEVKF ERLVKEEKLK TPYKRRHSFT
PPSNENSRSN SPNSSNSSAN GDAAAPKGGN NPHSRNSKKS GNFRAHKEEK RVRHNSYTSS
TSSSSSYTEA DPAILSRRQK QIDYGKNTAA YERYVEMVPK DERTRDHPRT PNKYGKYSRR
AFDGLVKIWR KSLHIYDPPT QARDTAKDSN SDSDSD
