PUF68_DROME
ID PUF68_DROME Reviewed; 637 AA.
AC Q8T6B9; Q0E8J8; Q95S11; Q9U696; Q9W0E6; Q9W0E7;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 02-FEB-2004, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Poly(U)-binding-splicing factor half pint {ECO:0000303|PubMed:11879639};
DE Short=Protein half pint {ECO:0000303|PubMed:11879639};
DE AltName: Full=68 kDa poly(U)-binding-splicing factor {ECO:0000305};
DE AltName: Full=PUF60 homolog {ECO:0000303|PubMed:10606266};
GN Name=hfp {ECO:0000303|PubMed:11879639, ECO:0000312|FlyBase:FBgn0028577};
GN Synonyms=pUf68 {ECO:0000303|PubMed:10606266};
GN ORFNames=CG12085 {ECO:0000312|FlyBase:FBgn0028577};
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 DOMAIN.
RX PubMed=10606266; DOI=10.1017/s1355838299991938;
RA Page-McCaw P.S., Amonlirdviman K., Sharp P.A.;
RT "PUF60: a novel U2AF65-related splicing activity.";
RL RNA 5:1548-1560(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND INTERACTION WITH ENC.
RX PubMed=11879639; DOI=10.1016/s1534-5807(02)00128-4;
RA Van Buskirk C., Schuepbach T.;
RT "Half pint regulates alternative splice site selection in Drosophila.";
RL Dev. Cell 2:343-353(2002).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RC STRAIN=Berkeley; TISSUE=Head;
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13 AND SER-30, 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: Splicing factor that regulates oogenesis and controls both
CC mitosis and mRNA localization in the germline by regulating mRNA
CC splicing of a subset of genes within the ovary. Probably acts by
CC regulating the alternative splice site selection of the otu transcript.
CC Also regulates the alternative splicing of eIF4E1 and grk, while it is
CC not involved in the splicing of par-1, sqd and psq.
CC {ECO:0000269|PubMed:11879639}.
CC -!- SUBUNIT: Interacts with enc. However, given the cytoplasmic
CC localization of enc, the relevance of such interaction is unclear.
CC {ECO:0000269|PubMed:11879639}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11879639}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A; Synonyms=Long;
CC IsoId=Q8T6B9-1; Sequence=Displayed;
CC Name=B; Synonyms=C;
CC IsoId=Q8T6B9-2; Sequence=VSP_009328;
CC -!- TISSUE SPECIFICITY: Expressed in all germline cells and within the
CC follicle cell. {ECO:0000269|PubMed:11879639}.
CC -!- DOMAIN: The third RNA recognition motif, called PUMP domain in
CC PubMed:10606266, is atypical and may rather mediate protein-protein
CC interactions. {ECO:0000269|PubMed:10606266}.
CC -!- SIMILARITY: Belongs to the RRM half pint family. {ECO:0000305}.
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DR EMBL; AF190745; AAF04132.1; -; mRNA.
DR EMBL; AF479079; AAL86452.1; -; mRNA.
DR EMBL; AE014296; AAF47501.1; -; Genomic_DNA.
DR EMBL; AE014296; AAG22221.1; -; Genomic_DNA.
DR EMBL; AY061006; AAL28554.1; -; mRNA.
DR EMBL; BT003317; AAO25077.1; -; mRNA.
DR RefSeq; NP_001163315.1; NM_001169844.2. [Q8T6B9-2]
DR RefSeq; NP_001163316.1; NM_001169845.2. [Q8T6B9-2]
DR RefSeq; NP_001163317.1; NM_001169846.2. [Q8T6B9-2]
DR RefSeq; NP_001163318.1; NM_001169847.2. [Q8T6B9-2]
DR RefSeq; NP_001163319.1; NM_001169848.2. [Q8T6B9-2]
DR RefSeq; NP_001163320.1; NM_001169849.2. [Q8T6B9-2]
DR RefSeq; NP_525123.2; NM_080384.4. [Q8T6B9-1]
DR RefSeq; NP_728610.1; NM_167880.3. [Q8T6B9-2]
DR RefSeq; NP_728611.1; NM_167881.3. [Q8T6B9-2]
DR RefSeq; NP_728612.1; NM_167882.3. [Q8T6B9-2]
DR AlphaFoldDB; Q8T6B9; -.
DR SMR; Q8T6B9; -.
DR BioGRID; 63711; 56.
DR IntAct; Q8T6B9; 16.
DR MINT; Q8T6B9; -.
DR STRING; 7227.FBpp0072593; -.
DR iPTMnet; Q8T6B9; -.
DR PaxDb; Q8T6B9; -.
DR PRIDE; Q8T6B9; -.
DR DNASU; 38173; -.
DR EnsemblMetazoa; FBtr0072707; FBpp0072591; FBgn0028577. [Q8T6B9-2]
DR EnsemblMetazoa; FBtr0072708; FBpp0072592; FBgn0028577. [Q8T6B9-2]
DR EnsemblMetazoa; FBtr0072709; FBpp0072593; FBgn0028577. [Q8T6B9-1]
DR EnsemblMetazoa; FBtr0072710; FBpp0072594; FBgn0028577. [Q8T6B9-2]
DR EnsemblMetazoa; FBtr0300416; FBpp0289645; FBgn0028577. [Q8T6B9-2]
DR EnsemblMetazoa; FBtr0300417; FBpp0289646; FBgn0028577. [Q8T6B9-2]
DR EnsemblMetazoa; FBtr0300418; FBpp0289647; FBgn0028577. [Q8T6B9-2]
DR EnsemblMetazoa; FBtr0300419; FBpp0289648; FBgn0028577. [Q8T6B9-2]
DR EnsemblMetazoa; FBtr0300420; FBpp0289649; FBgn0028577. [Q8T6B9-2]
DR EnsemblMetazoa; FBtr0301523; FBpp0290738; FBgn0028577. [Q8T6B9-2]
DR GeneID; 38173; -.
DR KEGG; dme:Dmel_CG12085; -.
DR CTD; 38173; -.
DR FlyBase; FBgn0028577; hfp.
DR VEuPathDB; VectorBase:FBgn0028577; -.
DR eggNOG; KOG0124; Eukaryota.
DR GeneTree; ENSGT00940000155594; -.
DR InParanoid; Q8T6B9; -.
DR PhylomeDB; Q8T6B9; -.
DR Reactome; R-DME-72163; mRNA Splicing - Major Pathway.
DR BioGRID-ORCS; 38173; 0 hits in 1 CRISPR screen.
DR ChiTaRS; pUf68; fly.
DR GenomeRNAi; 38173; -.
DR PRO; PR:Q8T6B9; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0028577; Expressed in brain and 35 other tissues.
DR ExpressionAtlas; Q8T6B9; baseline and differential.
DR Genevisible; Q8T6B9; DM.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; HDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0071011; C:precatalytic spliceosome; HDA:FlyBase.
DR GO; GO:0032991; C:protein-containing complex; IPI:FlyBase.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000380; P:alternative mRNA splicing, via spliceosome; IMP:FlyBase.
DR GO; GO:0007282; P:cystoblast division; IMP:FlyBase.
DR GO; GO:0006376; P:mRNA splice site selection; IMP:FlyBase.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IMP:FlyBase.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:FlyBase.
DR GO; GO:0045926; P:negative regulation of growth; IMP:FlyBase.
DR GO; GO:0048477; P:oogenesis; IEA:UniProtKB-KW.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IMP:FlyBase.
DR GO; GO:0001558; P:regulation of cell growth; IMP:FlyBase.
DR CDD; cd12370; RRM1_PUF60; 1.
DR CDD; cd12371; RRM2_PUF60; 1.
DR CDD; cd12648; RRM3_UHM_PUF60; 1.
DR Gene3D; 3.30.70.330; -; 3.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR006532; PUF60-like.
DR InterPro; IPR034209; PUF60_RRM1.
DR InterPro; IPR034211; PUF60_RRM2.
DR InterPro; IPR034212; PUF60_RRM3.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR003954; RRM_dom_euk.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00360; RRM; 3.
DR SMART; SM00361; RRM_1; 2.
DR SUPFAM; SSF54928; SSF54928; 2.
DR TIGRFAMs; TIGR01645; half-pint; 1.
DR PROSITE; PS50102; RRM; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Developmental protein; Differentiation;
KW mRNA processing; mRNA splicing; Nucleus; Oogenesis; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding.
FT CHAIN 1..637
FT /note="Poly(U)-binding-splicing factor half pint"
FT /id="PRO_0000081744"
FT DOMAIN 130..208
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 227..305
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 537..627
FT /note="RRM 3; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 1..92
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_009328"
FT CONFLICT 583
FT /note="D -> A (in Ref. 2; AAL86452)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 637 AA; 67940 MW; F0AD184D9EEF145F CRC64;
MGSNDRASRS PRSDDQREIS DMPATKRTRS DSGKSTDSKI PYLSQPLYDL KQTGDVKFGP
GTRSALLGLL GGALPKLSSE QHDLVSKAKK YAMEQSIKMV LMKQTLAHQQ QQLATQRTQV
QRQQALALMC RVYVGSISFE LKEDTIRVAF TPFGPIKSIN MSWDPITQKH KGFAFVEYEI
PEGAQLALEQ MNGALMGGRN IKVGRPSNMP QAQQVIDEVQ EEAKSFNRIY VASIHPDLSE
EDIKSVFEAF GPILYCKLAQ GTSLHTHKGY GFIEYANKQA MDEAIASMNL FDLGGQLLRV
GRSITPPNAL ACPTTNSTMP TAAAVAAAAA TAKIQALDAV ASNAVLGLSQ NTPVMAAGAV
VTKVGAMPVV SAATSAAALH PALAQAAPAL LPPGIFQAPT PVAPSLLGVP AGLQPLQAVV
PTLPPPALLA TPTLPMTVGG VGVGLVPTVA TLAGAEASKG AAAAAALSAA ANNAAVTAAN
LSENIKKAHE KQQEELQKKL MDEGDVQTLQ QQENMSIKGQ SARQLVMQRL MRPVDSRVII
LRNMVGPEDV DETLQEEIQE ECSKFGTVSR VIIFNEKQTE NEDDDEAEII VKIFVEFSAG
AEAMRGKEAL DGRFFGGRRV VAELYDQGIF DQGDLSG
