RB27C_DROME
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 03-AUG-2022, entry version 170.
DE RecName: Full=Heterogeneous nuclear ribonucleoprotein 27C;
DE Short=Hrb27-C;
DE AltName: Full=HRP48.1;
DE AltName: Full=hnRNP 48;
GN Name=Hrb27C; Synonyms=hrp48, Rbp7; ORFNames=CG10377;
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].
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 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.
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Nuclear and/or
CC cytoplasmic.
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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 AlphaFoldDB; P48809; -.
DR SMR; P48809; -.
DR BioGRID; 60119; 51.
DR IntAct; P48809; 8.
DR STRING; 7227.FBpp0297875; -.
DR iPTMnet; P48809; -.
DR PaxDb; P48809; -.
DR PRIDE; 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 CTD; 33968; -.
DR FlyBase; FBgn0004838; Hrb27C.
DR VEuPathDB; VectorBase:FBgn0004838; -.
DR eggNOG; KOG4205; Eukaryota.
DR GeneTree; ENSGT00940000156757; -.
DR HOGENOM; CLU_012062_1_2_1; -.
DR InParanoid; P48809; -.
DR OMA; NWNSWNM; -.
DR OrthoDB; 1565323at2759; -.
DR PhylomeDB; P48809; -.
DR SignaLink; P48809; -.
DR BioGRID-ORCS; 33968; 1 hit in 3 CRISPR screens.
DR ChiTaRS; Hrb27C; fly.
DR GenomeRNAi; 33968; -.
DR PRO; PR:P48809; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0004838; Expressed in cleaving embryo and 27 other tissues.
DR ExpressionAtlas; P48809; baseline and differential.
DR Genevisible; P48809; DM.
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: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; cd12574; RRM1_DAZAP1; 1.
DR CDD; cd12327; RRM2_DAZAP1; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR034134; DAZAP1_RRM1.
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 Pfam; PF00076; RRM_1; 2.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW 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 176..190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..254
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..318
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..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"
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
