SLU7_DROME
ID SLU7_DROME Reviewed; 574 AA.
AC Q9VAQ7; Q95RD1;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Pre-mRNA-splicing factor Slu7;
GN Name=Slu7; ORFNames=CG1420;
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 [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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
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 [4]
RP IDENTIFICATION.
RX PubMed=10908584; DOI=10.1083/jcb.150.2.f37;
RA Mount S.M., Salz H.K.;
RT "Pre-messenger RNA processing factors in the Drosophila genome.";
RL J. Cell Biol. 150:F37-F44(2000).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207 AND TYR-216, AND
RP 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).
CC -!- FUNCTION: Required for pre-mRNA splicing as component of the
CC spliceosome. Participates in the second catalytic step of pre-mRNA
CC splicing, when the free hydroxyl group of exon I attacks the 3'-splice
CC site to generate spliced mRNA and the excised lariat intron. Required
CC for holding exon 1 properly in the spliceosome and for correct AG
CC identification when more than one possible AG exists in 3'-splicing
CC site region. May be involved in the activation of proximal AG. Probably
CC also involved in alternative splicing regulation.
CC {ECO:0000250|UniProtKB:O95391}.
CC -!- SUBUNIT: Component of pre-catalytic, catalytic and post-catalytic
CC spliceosomes. Associates with the spliceosome prior to recognition of
CC the 3'-splice site for step II, probably during catalysis of step I.
CC {ECO:0000250|UniProtKB:O95391}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O95391}. Nucleus
CC speckle {ECO:0000250|UniProtKB:O95391}. Cytoplasm
CC {ECO:0000250|UniProtKB:O95391}. Note=Predominantly nuclear.
CC {ECO:0000250|UniProtKB:O95391}.
CC -!- SIMILARITY: Belongs to the SLU7 family. {ECO:0000305}.
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DR EMBL; AE014297; AAF56845.2; -; Genomic_DNA.
DR EMBL; AY061470; AAL29018.1; -; mRNA.
DR RefSeq; NP_651659.2; NM_143402.4.
DR AlphaFoldDB; Q9VAQ7; -.
DR SMR; Q9VAQ7; -.
DR BioGRID; 68298; 5.
DR IntAct; Q9VAQ7; 2.
DR STRING; 7227.FBpp0084787; -.
DR iPTMnet; Q9VAQ7; -.
DR PaxDb; Q9VAQ7; -.
DR DNASU; 43427; -.
DR EnsemblMetazoa; FBtr0085418; FBpp0084787; FBgn0039626.
DR GeneID; 43427; -.
DR KEGG; dme:Dmel_CG1420; -.
DR UCSC; CG1420-RA; d. melanogaster.
DR CTD; 10569; -.
DR FlyBase; FBgn0039626; Slu7.
DR VEuPathDB; VectorBase:FBgn0039626; -.
DR eggNOG; KOG2560; Eukaryota.
DR GeneTree; ENSGT00390000002292; -.
DR HOGENOM; CLU_019317_2_0_1; -.
DR InParanoid; Q9VAQ7; -.
DR OMA; KKPFYVD; -.
DR OrthoDB; 816947at2759; -.
DR PhylomeDB; Q9VAQ7; -.
DR Reactome; R-DME-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-DME-72187; mRNA 3'-end processing.
DR Reactome; R-DME-73856; RNA Polymerase II Transcription Termination.
DR SignaLink; Q9VAQ7; -.
DR BioGRID-ORCS; 43427; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 43427; -.
DR PRO; PR:Q9VAQ7; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0039626; Expressed in eye disc (Drosophila) and 27 other tissues.
DR ExpressionAtlas; Q9VAQ7; baseline and differential.
DR Genevisible; Q9VAQ7; DM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; ISS:FlyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030628; F:pre-mRNA 3'-splice site binding; ISS:UniProtKB.
DR GO; GO:0000389; P:mRNA 3'-splice site recognition; ISS:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:FlyBase.
DR GO; GO:0008380; P:RNA splicing; IBA:GO_Central.
DR InterPro; IPR021715; Slu7_dom.
DR InterPro; IPR039974; Splicing_factor_SLU7.
DR PANTHER; PTHR12942; PTHR12942; 1.
DR Pfam; PF11708; Slu7; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Metal-binding; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; Spliceosome; Zinc; Zinc-finger.
FT CHAIN 1..574
FT /note="Pre-mRNA-splicing factor Slu7"
FT /id="PRO_0000289202"
FT ZN_FING 116..133
FT /note="CCHC-type"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 78..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 252..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 433..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..61
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..98
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..512
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..568
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 207
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 216
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 387
FT /note="R -> C (in Ref. 3; AAL29018)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 574 AA; 65978 MW; D0FB40E533B32809 CRC64;
MSSGPMRTPV SQIILSKHDQ DAEEEPKKKS REDWRKAKEL EEARKAGTAP AAVDEEGRDI
NPHIPQYISN APWYYGSAGP TLKHQRPQHE DEQGQLDKRA PKGLNTARII TKFRKGACEN
CGAVTHKRKD CLERPRKVQA KYAESIVVHD EHLVNEAAVN YDEKRDRWSS YDPANHREII
EEYEKVEEAK RQLKAEKLKN DPDAEISDEE GNEDKYVDEV DMPGTKVDSK QRITVRNLRI
REDTAKYLRN LDPNSAYYDP KTRSMRDNPN PAVPEEEAEF AGENFVRFSG DTTAQATAQL
FAWEAHGKGV DVHLLAEPTK LELLQKEYEQ KKEQFKSSTK THIVEKYGGE EHLQVPPKSL
LLAQTEEYIE YSRSGKVIKG VEKPKARSIY EEDVYINNHT TVWGSFWNAG RWGYKCCKSF
IKNSYCVGMQ EPEGYSEHHS TSSTAAATTE PAAQSQFKVP EVPPERPTSE VDSASSSEPS
SSEEEEVKPE KKKTKKKSKK REKKKKAKEQ RKQKGKNKET KDKDKTKEKD IPEELDDRKR
AYNSMYDVKA PTEDEIEEWK KKRPRAEDPM LQFM
