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Heterogeneous nuclear ribonucleoprotein 87F (HRP36.1 protein) (Protein P11)

 RB87F_DROME             Reviewed;         385 AA.
P48810; Q24486; Q8INH0; Q9VFT2;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
25-OCT-2005, sequence version 2.
30-AUG-2017, entry version 147.
RecName: Full=Heterogeneous nuclear ribonucleoprotein 87F;
AltName: Full=HRP36.1 protein;
AltName: Full=Protein P11;
Name=Hrb87F; Synonyms=hrp36; ORFNames=CG12749;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), AND DEVELOPMENTAL STAGE.
STRAIN=Canton-S, and Oregon-R; TISSUE=Embryo, and Ovary;
PubMed=1849257; DOI=10.1093/nar/19.1.25;
Haynes S.R., Johnson D., Raychaudhuri G., Beyer A.L.;
"The Drosophila Hrb87F gene encodes a new member of the A and B hnRNP
protein group.";
Nucleic Acids Res. 19:25-31(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING, AND
SUBCELLULAR LOCATION.
STRAIN=Canton-S; TISSUE=Embryo;
PubMed=1717937; DOI=10.1093/nar/19.18.4909;
Hovemann B.T., Dessen E., Mechler H., Mack E.;
"Drosophila snRNP associated protein P11 which specifically binds to
heat shock puff 93D reveals strong homology with hnRNP core protein
A1.";
Nucleic Acids Res. 19:4909-4914(1991).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), AND FUNCTION.
STRAIN=Canton-S; TISSUE=Embryo;
PubMed=1730754; DOI=10.1083/jcb.116.2.257;
Matunis E.L., Matunis M.J., Dreyfuss G.;
"Characterization of the major hnRNP proteins from Drosophila
melanogaster.";
J. Cell Biol. 116:257-269(1992).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[5]
GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
STRAIN=Berkeley; TISSUE=Embryo;
Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A.,
Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: This protein is a component of ribonucleosomes. Could be
needed to organize a concentration gradient of a dorsalizing
morphogen (Dm) originating in the germinal vesicle.
{ECO:0000269|PubMed:1730754}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:1717937}.
Cytoplasm {ECO:0000269|PubMed:1717937}. Note=Nuclear and/or
cytoplasmic.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=A;
IsoId=P48810-1; Sequence=Displayed;
Name=B;
IsoId=P48810-2; Sequence=VSP_005807;
-!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
{ECO:0000269|PubMed:1849257}.
-----------------------------------------------------------------------
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EMBL; X54803; CAA38574.1; -; mRNA.
EMBL; X58183; CAA41170.1; -; Genomic_DNA.
EMBL; X58184; CAA41170.1; JOINED; Genomic_DNA.
EMBL; X59691; CAA42212.1; -; Genomic_DNA.
EMBL; X62636; CAA44502.1; -; mRNA.
EMBL; AE014297; AAF54967.1; -; Genomic_DNA.
EMBL; AE014297; AAN13574.1; -; Genomic_DNA.
EMBL; BT012315; AAS77440.1; -; mRNA.
PIR; A41732; A41732.
PIR; S22315; S22315.
RefSeq; NP_001163602.1; NM_001170131.2. [P48810-1]
RefSeq; NP_001262538.1; NM_001275609.1. [P48810-1]
RefSeq; NP_476806.2; NM_057458.5. [P48810-1]
RefSeq; NP_476807.1; NM_057459.5. [P48810-1]
UniGene; Dm.1711; -.
ProteinModelPortal; P48810; -.
SMR; P48810; -.
BioGrid; 71477; 9.
IntAct; P48810; 8.
MINT; MINT-296059; -.
STRING; 7227.FBpp0302741; -.
PaxDb; P48810; -.
PRIDE; P48810; -.
EnsemblMetazoa; FBtr0082851; FBpp0082316; FBgn0004237. [P48810-1]
EnsemblMetazoa; FBtr0300590; FBpp0289817; FBgn0004237. [P48810-1]
EnsemblMetazoa; FBtr0310621; FBpp0302741; FBgn0004237. [P48810-1]
EnsemblMetazoa; FBtr0334495; FBpp0306562; FBgn0004237. [P48810-1]
GeneID; 48535; -.
KEGG; dme:Dmel_CG12749; -.
CTD; 48535; -.
FlyBase; FBgn0004237; Hrb87F.
eggNOG; KOG0118; Eukaryota.
eggNOG; COG0724; LUCA.
GeneTree; ENSGT00760000118873; -.
InParanoid; P48810; -.
KO; K12741; -.
OMA; IMTDRNT; -.
OrthoDB; EOG091G1CPI; -.
PhylomeDB; P48810; -.
Reactome; R-DME-6803529; FGFR2 alternative splicing.
Reactome; R-DME-72163; mRNA Splicing - Major Pathway.
Reactome; R-DME-72203; Processing of Capped Intron-Containing Pre-mRNA.
ChiTaRS; Hrb87F; fly.
GenomeRNAi; 48535; -.
PRO; PR:P48810; -.
Proteomes; UP000000803; Chromosome 3R.
Bgee; FBgn0004237; -.
ExpressionAtlas; P48810; differential.
Genevisible; P48810; DM.
GO; GO:0000785; C:chromatin; IDA:FlyBase.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0000792; C:heterochromatin; IDA:FlyBase.
GO; GO:0030529; C:intracellular ribonucleoprotein complex; IDA:FlyBase.
GO; GO:0005654; C:nucleoplasm; IDA:FlyBase.
GO; GO:0005634; C:nucleus; IDA:FlyBase.
GO; GO:0035062; C:omega speckle; IDA:FlyBase.
GO; GO:0005703; C:polytene chromosome puff; IDA:FlyBase.
GO; GO:0003729; F:mRNA binding; ISS:FlyBase.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:FlyBase.
GO; GO:0001745; P:compound eye morphogenesis; IGI:FlyBase.
GO; GO:0008585; P:female gonad development; IMP:FlyBase.
GO; GO:0000278; P:mitotic cell cycle; IMP:FlyBase.
GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IMP:FlyBase.
GO; GO:0009408; P:response to heat; IMP:FlyBase.
GO; GO:0042594; P:response to starvation; IMP:FlyBase.
InterPro; IPR000504; RRM_dom.
Pfam; PF00076; RRM_1; 2.
SMART; SM00360; RRM; 2.
SUPFAM; SSF54928; SSF54928; 2.
PROSITE; PS50102; RRM; 2.
2: Evidence at transcript level;
Alternative splicing; Complete proteome; Cytoplasm; Nucleus;
Reference proteome; Repeat; Ribonucleoprotein; RNA-binding.
CHAIN 1 385 Heterogeneous nuclear ribonucleoprotein
87F.
/FTId=PRO_0000081750.
DOMAIN 24 101 RRM 1. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 115 192 RRM 2. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
COMPBIAS 200 381 Gly-rich.
VAR_SEQ 310 369 Missing (in isoform B).
{ECO:0000303|PubMed:1730754}.
/FTId=VSP_005807.
CONFLICT 241 241 A -> R (in Ref. 2; CAA41170).
{ECO:0000305}.
CONFLICT 271 271 S -> T (in Ref. 2; CAA41170/CAA42212).
{ECO:0000305}.
CONFLICT 293 293 G -> GG (in Ref. 1, 2 and 3).
{ECO:0000305}.
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


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