RB87F_DROME
ID RB87F_DROME Reviewed; 385 AA.
AC P48810; Q24486; Q8INH0; Q9VFT2;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 2.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Heterogeneous nuclear ribonucleoprotein 87F;
DE AltName: Full=HRP36.1 protein;
DE AltName: Full=Protein P11;
GN Name=Hrb87F; Synonyms=hrp36; ORFNames=CG12749;
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), AND DEVELOPMENTAL STAGE.
RC STRAIN=Canton-S, and Oregon-R; TISSUE=Embryo, and Ovary;
RX PubMed=1849257; DOI=10.1093/nar/19.1.25;
RA Haynes S.R., Johnson D., Raychaudhuri G., Beyer A.L.;
RT "The Drosophila Hrb87F gene encodes a new member of the A and B hnRNP
RT protein group.";
RL Nucleic Acids Res. 19:25-31(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=Canton-S; TISSUE=Embryo;
RX PubMed=1717937; DOI=10.1093/nar/19.18.4909;
RA Hovemann B.T., Dessen E., Mechler H., Mack E.;
RT "Drosophila snRNP associated protein P11 which specifically binds to heat
RT shock puff 93D reveals strong homology with hnRNP core protein A1.";
RL Nucleic Acids Res. 19:4909-4914(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), AND FUNCTION.
RC STRAIN=Canton-S; TISSUE=Embryo;
RX PubMed=1730754; DOI=10.1083/jcb.116.2.257;
RA Matunis E.L., Matunis M.J., Dreyfuss G.;
RT "Characterization of the major hnRNP proteins from Drosophila
RT melanogaster.";
RL J. Cell Biol. 116:257-269(1992).
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: This protein is a component of ribonucleosomes. Could be
CC needed to organize a concentration gradient of a dorsalizing morphogen
CC (Dm) originating in the germinal vesicle. {ECO:0000269|PubMed:1730754}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:1717937}. Cytoplasm
CC {ECO:0000269|PubMed:1717937}. Note=Nuclear and/or cytoplasmic.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A;
CC IsoId=P48810-1; Sequence=Displayed;
CC Name=B;
CC IsoId=P48810-2; Sequence=VSP_005807;
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC {ECO:0000269|PubMed:1849257}.
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DR EMBL; X54803; CAA38574.1; -; mRNA.
DR EMBL; X58183; CAA41170.1; -; Genomic_DNA.
DR EMBL; X58184; CAA41170.1; JOINED; Genomic_DNA.
DR EMBL; X59691; CAA42212.1; -; Genomic_DNA.
DR EMBL; X62636; CAA44502.1; -; mRNA.
DR EMBL; AE014297; AAF54967.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN13574.1; -; Genomic_DNA.
DR EMBL; BT012315; AAS77440.1; -; mRNA.
DR PIR; A41732; A41732.
DR PIR; S22315; S22315.
DR RefSeq; NP_001163602.1; NM_001170131.2. [P48810-1]
DR RefSeq; NP_001262538.1; NM_001275609.1. [P48810-1]
DR RefSeq; NP_476806.2; NM_057458.5. [P48810-1]
DR RefSeq; NP_476807.1; NM_057459.5. [P48810-1]
DR AlphaFoldDB; P48810; -.
DR SMR; P48810; -.
DR BioGRID; 71477; 24.
DR IntAct; P48810; 8.
DR STRING; 7227.FBpp0302741; -.
DR PaxDb; P48810; -.
DR PRIDE; P48810; -.
DR DNASU; 48535; -.
DR EnsemblMetazoa; FBtr0082851; FBpp0082316; FBgn0004237. [P48810-1]
DR EnsemblMetazoa; FBtr0300590; FBpp0289817; FBgn0004237. [P48810-1]
DR EnsemblMetazoa; FBtr0310621; FBpp0302741; FBgn0004237. [P48810-1]
DR EnsemblMetazoa; FBtr0334495; FBpp0306562; FBgn0004237. [P48810-1]
DR GeneID; 48535; -.
DR KEGG; dme:Dmel_CG12749; -.
DR CTD; 48535; -.
DR FlyBase; FBgn0004237; Hrb87F.
DR VEuPathDB; VectorBase:FBgn0004237; -.
DR eggNOG; KOG0118; Eukaryota.
DR GeneTree; ENSGT00940000167175; -.
DR HOGENOM; CLU_012062_1_3_1; -.
DR InParanoid; P48810; -.
DR OMA; WGNNRQN; -.
DR PhylomeDB; P48810; -.
DR SignaLink; P48810; -.
DR BioGRID-ORCS; 48535; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Hrb87F; fly.
DR GenomeRNAi; 48535; -.
DR PRO; PR:P48810; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0004237; Expressed in wing disc and 26 other tissues.
DR ExpressionAtlas; P48810; baseline and differential.
DR Genevisible; P48810; DM.
DR GO; GO:0000785; C:chromatin; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0000792; C:heterochromatin; IDA:FlyBase.
DR GO; GO:0005654; C:nucleoplasm; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0035062; C:omega speckle; IDA:FlyBase.
DR GO; GO:0005703; C:polytene chromosome puff; IDA:FlyBase.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:FlyBase.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; ISS:FlyBase.
DR GO; GO:0034046; F:poly(G) binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:FlyBase.
DR GO; GO:0001745; P:compound eye morphogenesis; IGI:FlyBase.
DR GO; GO:0008585; P:female gonad development; IMP:FlyBase.
DR GO; GO:0000278; P:mitotic cell cycle; HMP:FlyBase.
DR GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IMP:FlyBase.
DR GO; GO:0009408; P:response to heat; IMP:FlyBase.
DR GO; GO:0042594; P:response to starvation; IMP:FlyBase.
DR Gene3D; 3.30.70.330; -; 2.
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; 2.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50102; RRM; 2.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cytoplasm; Nucleus; Reference proteome; Repeat;
KW Ribonucleoprotein; RNA-binding.
FT CHAIN 1..385
FT /note="Heterogeneous nuclear ribonucleoprotein 87F"
FT /id="PRO_0000081750"
FT DOMAIN 24..101
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 115..192
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 192..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..340
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..375
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 310..369
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:1730754"
FT /id="VSP_005807"
FT CONFLICT 241
FT /note="A -> R (in Ref. 2; CAA41170)"
FT /evidence="ECO:0000305"
FT CONFLICT 271
FT /note="S -> T (in Ref. 2; CAA41170/CAA42212)"
FT /evidence="ECO:0000305"
FT CONFLICT 293
FT /note="G -> GG (in Ref. 1, 2 and 3)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 385 AA; 39499 MW; 2E2635EDDCA9EFBA CRC64;
MAEQNDSNGN YDDGEEITEP EQLRKLFIGG LDYRTTDDGL KAHFEKWGNI VDVVVMKDPK
TKRSRGFGFI TYSQSYMIDN AQNARPHKID GRTVEPKRAV PRQEIDSPNA GATVKKLFVG
GLRDDHDEEC LREYFKDFGQ IVSVNIVSDK DTGKKRGFAF IEFDDYDPVD KIILQKTHSI
KNKTLDVKKA IAKQDMDRQG GGGGRGGPRA GGRGGQGDRG QGGGGWGGQN RQNGGGNWGG
AGGGGGFGNS GGNFGGGQGG GSGGWNQQGG SGGGPWNNQG GGNGGWNGGG GGGYGGGNSN
GSWGGNGGGG GGGGGFGNEY QQSYGGGPQR NSNFGNNRPA PYSQGGGGGG FNKGNQGGGQ
GFAGNNYNTG GGGQGGNMGG GNRRY
