RBP1_DROME
ID RBP1_DROME Reviewed; 144 AA.
AC Q02427; A4V2P0; Q26271; Q26280; Q8T9K6; Q9VGW8;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 09-NOV-2004, sequence version 3.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=RNA-binding protein 1;
GN Name=Rbp1; Synonyms=Rbp11; ORFNames=CG17136;
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 [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=1340470; DOI=10.1101/gad.6.12b.2569;
RA Kim Y.-J., Zuo P., Manley J.L., Baker B.S.;
RT "The Drosophila RNA-binding protein RBP1 is localized to transcriptionally
RT active sites of chromosomes and shows a functional similarity to human
RT splicing factor ASF/SF2.";
RL Genes Dev. 6:2569-2579(1992).
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] (ISOFORM D).
RC STRAIN=Berkeley; TISSUE=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 NUCLEOTIDE SEQUENCE [MRNA] OF 14-52 (ISOFORMS A/D).
RX PubMed=8417324; DOI=10.1128/mcb.13.1.174-183.1993;
RA Kim Y.-J., Baker B.S.;
RT "Isolation of RRM-type RNA-binding protein genes and the analysis of their
RT relatedness by using a numerical approach.";
RL Mol. Cell. Biol. 13:174-183(1993).
RN [6]
RP FUNCTION.
RX PubMed=7664738; DOI=10.1002/j.1460-2075.1995.tb00070.x;
RA Heinrichs V., Baker B.S.;
RT "The Drosophila SR protein RBP1 contributes to the regulation of doublesex
RT alternative splicing by recognizing RBP1 RNA target sequences.";
RL EMBO J. 14:3987-4000(1995).
CC -!- FUNCTION: Contributes to the activation of female-specific DSX splicing
CC in vivo by recognizing the RBP1 target sequences within the purine-rich
CC polypyrimidine tract of the female-specific 3' splice site.
CC {ECO:0000269|PubMed:1340470, ECO:0000269|PubMed:7664738}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:1340470}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=D;
CC IsoId=Q02427-3; Sequence=Displayed;
CC Name=A; Synonyms=RBP1-A, C;
CC IsoId=Q02427-1; Sequence=VSP_011815;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:1340470}.
CC -!- DEVELOPMENTAL STAGE: Found at all developmental stages.
CC {ECO:0000269|PubMed:1340470}.
CC -!- PTM: Extensively phosphorylated on serine residues in the RS domain.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the splicing factor SR 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; L04929; AAA28850.1; -; Genomic_DNA.
DR EMBL; AE014297; AAF54555.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN13487.1; -; Genomic_DNA.
DR EMBL; AY069252; AAL39397.1; -; mRNA.
DR EMBL; S51691; AAB24622.1; -; mRNA.
DR EMBL; S51740; AAB24631.1; -; mRNA.
DR PIR; A46398; A46398.
DR PIR; A47752; A47752.
DR PIR; A48110; A48110.
DR RefSeq; NP_524307.1; NM_079583.3. [Q02427-1]
DR RefSeq; NP_731510.1; NM_169364.3. [Q02427-3]
DR AlphaFoldDB; Q02427; -.
DR SMR; Q02427; -.
DR BioGRID; 66438; 15.
DR IntAct; Q02427; 6.
DR STRING; 7227.FBpp0081754; -.
DR PaxDb; Q02427; -.
DR DNASU; 41294; -.
DR EnsemblMetazoa; FBtr0082275; FBpp0081752; FBgn0260944. [Q02427-1]
DR EnsemblMetazoa; FBtr0082277; FBpp0081754; FBgn0260944. [Q02427-3]
DR GeneID; 41294; -.
DR KEGG; dme:Dmel_CG17136; -.
DR CTD; 5947; -.
DR FlyBase; FBgn0260944; Rbp1.
DR VEuPathDB; VectorBase:FBgn0260944; -.
DR eggNOG; KOG0107; Eukaryota.
DR GeneTree; ENSGT00910000144115; -.
DR InParanoid; Q02427; -.
DR OMA; XSPRRRS; -.
DR PhylomeDB; Q02427; -.
DR Reactome; R-DME-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-DME-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-DME-72165; mRNA Splicing - Minor Pathway.
DR Reactome; R-DME-72187; mRNA 3'-end processing.
DR Reactome; R-DME-73856; RNA Polymerase II Transcription Termination.
DR BioGRID-ORCS; 41294; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 41294; -.
DR PRO; PR:Q02427; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0260944; Expressed in adult abdomen and 42 other tissues.
DR ExpressionAtlas; Q02427; baseline and differential.
DR Genevisible; Q02427; DM.
DR GO; GO:0000791; C:euchromatin; IDA:FlyBase.
DR GO; GO:0016607; C:nuclear speck; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0003729; F:mRNA binding; IDA:FlyBase.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IDA:FlyBase.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IMP:FlyBase.
DR GO; GO:0010468; P:regulation of gene expression; IMP:FlyBase.
DR GO; GO:0031440; P:regulation of mRNA 3'-end processing; IMP:FlyBase.
DR GO; GO:0001178; P:regulation of transcriptional start site selection at RNA polymerase II promoter; IMP:FlyBase.
DR GO; GO:0008380; P:RNA splicing; IMP:FlyBase.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; RNA-binding.
FT CHAIN 1..144
FT /note="RNA-binding protein 1"
FT /id="PRO_0000081797"
FT DOMAIN 11..84
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 78..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..95
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 107..144
FT /note="ITPSARTTSTATSSFYNINNLQQQPSSQPQPATFNLQL -> SRSPRRSRSP
FT RSRSFSRDRRSRSDSRDRH (in isoform A)"
FT /evidence="ECO:0000305"
FT /id="VSP_011815"
FT CONFLICT 14
FT /note="Y -> F (in Ref. 5; AAB24622/AAB24631)"
FT /evidence="ECO:0000305"
FT CONFLICT 19..29
FT /note="GSSASKHEIEG -> APRRSKPRDRS (in Ref. 5; AAB24631)"
FT /evidence="ECO:0000305"
FT CONFLICT 65
FT /note="R -> A (in Ref. 1; AAA28850)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 144 AA; 16013 MW; AB5B6D782CED5A46 CRC64;
MPRYREWDLA CKVYVGNLGS SASKHEIEGA FAKYGPLRNV WVARNPPGFA FVEFEDRRDA
EDATRALDGT RCCGTRIRVE MSSGRSRDRR RGEGGSSGRS GSGRYRITPS ARTTSTATSS
FYNINNLQQQ PSSQPQPATF NLQL
