ID RB27C_DROME Reviewed; 421 AA. AC P48809; A4V0B8; Q7JPT5; Q9TY67; Q9VM68; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 27-SEP-2005, sequence version 2. DT 02-SEP-2026, entry version 187. DE RecName: Full=Heterogeneous nuclear ribonucleoprotein 27C {ECO:0000305}; DE Short=Hrb27-C; DE AltName: Full=HRP48.1; DE AltName: Full=hnRNP 48; GN Name=Hrb27C {ECO:0000312|FlyBase:FBgn0004838}; GN Synonyms=hrp48 {ECO:0000312|FlyBase:FBgn0004838}, Rbp7 GN {ECO:0000312|FlyBase:FBgn0004838}; GN ORFNames=CG10377 {ECO:0000312|FlyBase:FBgn0004838}; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Altocrustacea; Allotriocarida; OC Hexapoda; Insecta; Pterygota; Neoptera; Eumetabola; Endopterygota; OC Aparaglossata; Panorpida; Diptera; Brachycera; Muscomorpha; Ephydroidea; OC Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7227 {ECO:0000312|Proteomes:UP000000803}; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. 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 [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Ovary; RX PubMed=15917496; DOI=10.1093/molbev/msi175; RA Jagadeeshan S., Singh R.S.; RT "Rapidly evolving genes of Drosophila: differing levels of selective RT pressure in testis, ovary, and head tissues between sibling species."; RL Mol. Biol. Evol. 22:1793-1801(2005). 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. 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]. RC STRAIN=Berkeley; TISSUE=Embryo, and 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 NUCLEOTIDE SEQUENCE [MRNA] OF 10-53. 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 [7] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=9372958; DOI=10.1128/mcb.17.12.7260; RA Hammond L.E., Rudner D.Z., Kanaar R., Rio D.C.; RT "Mutations in the hrp48 gene, which encodes a Drosophila heterogeneous RT nuclear ribonucleoprotein particle protein, cause lethality and RT developmental defects and affect P-element third-intron splicing in vivo."; RL Mol. Cell. Biol. 17:7260-7267(1997). RN [8] RP FUNCTION, AND INTERACTION WITH OTU; SQD AND GRK MRNA. RX PubMed=15056611; DOI=10.1242/dev.01078; RA Goodrich J.S., Clouse K.N., Schuepbach T.; RT "Hrb27C, Sqd and Otu cooperatively regulate gurken RNA localization and RT mediate nurse cell chromosome dispersion in Drosophila oogenesis."; RL Development 131:1949-1958(2004). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177; SER-366; SER-368; RP SER-370; TYR-372 AND SER-379, AND 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: 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. Interacts with grk mRNA (via CC 3' UTR) and involved in its localization to the dorsal anterior region CC of the oocyte during dorsal-ventral axis determination; may function as CC a ribonuclear protein complex together with sqd and otu CC (PubMed:15056611). Required for polytene chromosome dispersal in nurse CC cells during oogenesis (PubMed:15056611). May be involved in the CC regulation of splicing (PubMed:9372958). {ECO:0000269|PubMed:15056611, CC ECO:0000269|PubMed:9372958}. CC -!- SUBUNIT: Interacts with sqd; the interaction is RNA-dependent and may CC be specific for sqd isoform A/sqdA (PubMed:15056611). Interacts with CC otu; the interaction is RNA-independent (PubMed:15056611). CC {ECO:0000269|PubMed:15056611}. CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Nuclear and/or CC cytoplasmic. CC -!- DISRUPTION PHENOTYPE: Lethal due to developmental defects. CC {ECO:0000269|PubMed:9372958}. 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; X62639; CAA44505.1; -; mRNA. DR EMBL; DQ062784; AAY56657.1; -; mRNA. DR EMBL; AE014134; AAF52456.1; -; Genomic_DNA. DR EMBL; AE014134; AAF52457.1; -; Genomic_DNA. DR EMBL; AE014134; AAN10605.1; -; Genomic_DNA. DR EMBL; AY069699; AAL39844.1; -; mRNA. DR EMBL; AY128430; AAM75023.1; -; mRNA. DR EMBL; S51720; AAB24628.1; -; mRNA. DR PIR; D41732; D41732. DR RefSeq; NP_001162897.1; NM_001169426.2. DR RefSeq; NP_001162898.1; NM_001169427.2. DR RefSeq; NP_001245917.1; NM_001258988.2. DR RefSeq; NP_001245918.1; NM_001258989.2. DR RefSeq; NP_001245919.1; NM_001258990.2. DR RefSeq; NP_476869.1; NM_057521.6. DR RefSeq; NP_723228.1; NM_164720.4. DR RefSeq; NP_723229.1; NM_164721.3. DR PDB; 9EN7; X-ray; 1.19 A; A=1-88. DR AlphaFoldDB; P48809; -. DR SMR; P48809; -. DR BioGRID; 60119; 53. DR FunCoup; P48809; 2106. DR IntAct; P48809; 13. DR STRING; 7227.FBpp0297875; -. DR GlyGen; P48809; 1 site. DR iPTMnet; P48809; -. DR PaxDb; 7227-FBpp0297875; -. DR PeptideAtlas; P48809; -. DR DNASU; 33968; -. DR EnsemblMetazoa; FBtr0079346; FBpp0078974; FBgn0004838. DR EnsemblMetazoa; FBtr0079347; FBpp0078975; FBgn0004838. DR EnsemblMetazoa; FBtr0079348; FBpp0078976; FBgn0004838. DR EnsemblMetazoa; FBtr0301403; FBpp0290617; FBgn0004838. DR EnsemblMetazoa; FBtr0301404; FBpp0290618; FBgn0004838. DR EnsemblMetazoa; FBtr0307030; FBpp0297873; FBgn0004838. DR EnsemblMetazoa; FBtr0307031; FBpp0297874; FBgn0004838. DR EnsemblMetazoa; FBtr0307032; FBpp0297875; FBgn0004838. DR GeneID; 33968; -. DR KEGG; dme:Dmel_CG10377; -. DR UCSC; CG10377-RB; d. melanogaster. DR AGR; FB:FBgn0004838; -. DR CTD; 33968; -. DR FlyBase; FBgn0004838; Hrb27C. DR VEuPathDB; VectorBase:FBgn0004838; -. DR eggNOG; KOG4205; Eukaryota. DR HOGENOM; CLU_012062_1_2_1; -. DR InParanoid; P48809; -. DR OMA; PCNPRSQ; -. DR OrthoDB; 1875751at2759; -. DR PhylomeDB; P48809; -. DR SignaLink; P48809; -. DR BioGRID-ORCS; 33968; 1 hit in 3 CRISPR screens. DR CD-CODE; 19A54EA0; Sponge body. DR GenomeRNAi; 33968; -. DR PRO; PR:P48809; -. DR Proteomes; UP000000803; Chromosome 2L. DR Bgee; FBgn0004838; Expressed in spermatogonium in testis and 286 other cell types or tissues. DR ExpressionAtlas; P48809; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase. DR GO; GO:0005654; C:nucleoplasm; IDA:FlyBase. DR GO; GO:0005634; C:nucleus; HDA:FlyBase. DR GO; GO:0043186; C:P granule; IPI:FlyBase. DR GO; GO:0000932; C:P-body; IDA:FlyBase. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IBA:GO_Central. DR GO; GO:0032991; C:protein-containing complex; IPI:FlyBase. DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:FlyBase. DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:FlyBase. DR GO; GO:0048027; F:mRNA 5'-UTR binding; TAS:FlyBase. DR GO; GO:0003729; F:mRNA binding; ISS:FlyBase. DR GO; GO:0034046; F:poly(G) binding; IBA:GO_Central. DR GO; GO:0003697; F:single-stranded DNA binding; IDA:FlyBase. DR GO; GO:0030371; F:translation repressor activity; IMP:CACAO. DR GO; GO:0007319; P:negative regulation of oskar mRNA translation; TAS:FlyBase. DR GO; GO:0045451; P:pole plasm oskar mRNA localization; IMP:FlyBase. DR GO; GO:1903688; P:positive regulation of border follicle cell migration; IMP:FlyBase. DR GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; IBA:GO_Central. DR GO; GO:0045727; P:positive regulation of translation; IDA:FlyBase. DR GO; GO:0048024; P:regulation of mRNA splicing, via spliceosome; IMP:FlyBase. DR GO; GO:0007283; P:spermatogenesis; IBA:GO_Central. DR CDD; cd12325; RRM1_hnRNPA_hnRNPD_like; 1. DR CDD; cd12327; RRM2_DAZAP1; 1. DR FunFam; 3.30.70.330:FF:000427; Heterogeneous nuclear ribonucleoprotein 27C; 1. DR Gene3D; 3.30.70.330; -; 2. DR InterPro; IPR034131; DAZAP1_RRM2. DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf. DR InterPro; IPR035979; RBD_domain_sf. DR InterPro; IPR000504; RRM_dom. DR PANTHER; PTHR48032; RNA-BINDING PROTEIN MUSASHI HOMOLOG RBP6; 1. DR PANTHER; PTHR48032:SF18; RRM DOMAIN-CONTAINING PROTEIN; 1. DR Pfam; PF00076; RRM_1; 2. DR SMART; SM00360; RRM; 2. DR SUPFAM; SSF54928; RNA-binding domain, RBD; 2. DR PROSITE; PS50102; RRM; 2. DR PDBsum; 9EN7; -. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome; KW Repeat; Ribonucleoprotein; RNA-binding. FT CHAIN 1..421 FT /note="Heterogeneous nuclear ribonucleoprotein 27C" FT /id="PRO_0000081748" FT DOMAIN 7..88 FT /note="RRM 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176" FT DOMAIN 96..173 FT /note="RRM 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176" FT REGION 171..191 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 240..373 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 392..421 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 240..250 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 264..273 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 275..284 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 293..302 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 406..421 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 177 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18327897" FT MOD_RES 366 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18327897" FT MOD_RES 368 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18327897" FT MOD_RES 370 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18327897" FT MOD_RES 372 FT /note="Phosphotyrosine" FT /evidence="ECO:0000269|PubMed:18327897" FT MOD_RES 379 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18327897" FT CONFLICT 262..297 FT /note="Missing (in Ref. 1; CAA44505)" FT /evidence="ECO:0000305" FT STRAND 8..12 FT /evidence="ECO:0007829|PDB:9EN7" FT HELIX 20..27 FT /evidence="ECO:0007829|PDB:9EN7" FT HELIX 28..30 FT /evidence="ECO:0007829|PDB:9EN7" FT STRAND 33..40 FT /evidence="ECO:0007829|PDB:9EN7" FT TURN 42..44 FT /evidence="ECO:0007829|PDB:9EN7" FT STRAND 47..57 FT /evidence="ECO:0007829|PDB:9EN7" FT HELIX 60..66 FT /evidence="ECO:0007829|PDB:9EN7" FT STRAND 70..72 FT /evidence="ECO:0007829|PDB:9EN7" FT STRAND 75..81 FT /evidence="ECO:0007829|PDB:9EN7" FT HELIX 83..86 FT /evidence="ECO:0007829|PDB:9EN7" SQ SEQUENCE 421 AA; 44770 MW; D59DD2A647CE23F5 CRC64; MEEDERGKLF VGGLSWETTQ ENLSRYFCRF GDIIDCVVMK NNESGRSRGF GFVTFADPTN VNHVLQNGPH TLDGRTIDPK PCNPRTLQKP KKGGGYKVFL GGLPSNVTET DLRTFFNRYG KVTEVVIMYD QEKKKSRGFG FLSFEEESSV EHVTNERYIN LNGKQVEIKK AEPRDGSGGQ NSNNSTVGGA YGKLGNECSH WGPHHAPINM MQGQNGQMGG PPLNMPIGAP NMMPGYQGWG TSPQQQQYGY GNSGPGSYQG WGAPPGPQGP PPQWSNYAGP QQTQGYGGYD MYNSTSTGAP SGPSGGGSWN SWNMPPNSAG PTGAPGAGAG TATDMYSRAQ AWATGGPSTT GPVGGMPRTG PGNSASKSGS EYDYGGYGSG YDYDYSNYVK QEGASNYGAG PRSAYGNDSS TQPPYATSQA V //