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Heterogeneous nuclear ribonucleoprotein 27C (Hrb27-C) (HRP48.1) (hnRNP 48)

 RB27C_DROME             Reviewed;         421 AA.
P48809; A4V0B8; Q7JPT5; Q9TY67; Q9VM68;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
27-SEP-2005, sequence version 2.
28-MAR-2018, entry version 144.
RecName: Full=Heterogeneous nuclear ribonucleoprotein 27C;
Short=Hrb27-C;
AltName: Full=HRP48.1;
AltName: Full=hnRNP 48;
Name=Hrb27C; Synonyms=hrp48, Rbp7; ORFNames=CG10377;
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].
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).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Ovary;
PubMed=15917496; DOI=10.1093/molbev/msi175;
Jagadeeshan S., Singh R.S.;
"Rapidly evolving genes of Drosophila: differing levels of selective
pressure in testis, ovary, and head tissues between sibling species.";
Mol. Biol. Evol. 22:1793-1801(2005).
[3]
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).
[4]
GENOME REANNOTATION.
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley; TISSUE=Embryo, and Head;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 10-53.
PubMed=8417324; DOI=10.1128/MCB.13.1.174;
Kim Y.-J., Baker B.S.;
"Isolation of RRM-type RNA-binding protein genes and the analysis of
their relatedness by using a numerical approach.";
Mol. Cell. Biol. 13:174-183(1993).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177; SER-366; SER-368;
SER-370; TYR-372 AND SER-379, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Embryo;
PubMed=18327897; DOI=10.1021/pr700696a;
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
J. Proteome Res. 7:1675-1682(2008).
-!- 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.
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Nuclear and/or
cytoplasmic.
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EMBL; X62639; CAA44505.1; -; mRNA.
EMBL; DQ062784; AAY56657.1; -; mRNA.
EMBL; AE014134; AAF52456.1; -; Genomic_DNA.
EMBL; AE014134; AAF52457.1; -; Genomic_DNA.
EMBL; AE014134; AAN10605.1; -; Genomic_DNA.
EMBL; AY069699; AAL39844.1; -; mRNA.
EMBL; AY128430; AAM75023.1; -; mRNA.
EMBL; S51720; AAB24628.1; -; mRNA.
PIR; D41732; D41732.
RefSeq; NP_001162897.1; NM_001169426.2.
RefSeq; NP_001162898.1; NM_001169427.2.
RefSeq; NP_001245917.1; NM_001258988.2.
RefSeq; NP_001245918.1; NM_001258989.2.
RefSeq; NP_001245919.1; NM_001258990.2.
RefSeq; NP_476869.1; NM_057521.6.
RefSeq; NP_723228.1; NM_164720.4.
RefSeq; NP_723229.1; NM_164721.3.
UniGene; Dm.1997; -.
ProteinModelPortal; P48809; -.
SMR; P48809; -.
BioGrid; 60119; 29.
IntAct; P48809; 18.
STRING; 7227.FBpp0297875; -.
iPTMnet; P48809; -.
PaxDb; P48809; -.
PRIDE; P48809; -.
EnsemblMetazoa; FBtr0079346; FBpp0078974; FBgn0004838.
EnsemblMetazoa; FBtr0079347; FBpp0078975; FBgn0004838.
EnsemblMetazoa; FBtr0079348; FBpp0078976; FBgn0004838.
EnsemblMetazoa; FBtr0301403; FBpp0290617; FBgn0004838.
EnsemblMetazoa; FBtr0301404; FBpp0290618; FBgn0004838.
EnsemblMetazoa; FBtr0307030; FBpp0297873; FBgn0004838.
EnsemblMetazoa; FBtr0307031; FBpp0297874; FBgn0004838.
EnsemblMetazoa; FBtr0307032; FBpp0297875; FBgn0004838.
GeneID; 33968; -.
KEGG; dme:Dmel_CG10377; -.
UCSC; CG10377-RB; d. melanogaster.
CTD; 33968; -.
FlyBase; FBgn0004838; Hrb27C.
eggNOG; KOG4205; Eukaryota.
eggNOG; ENOG410YA8Z; LUCA.
GeneTree; ENSGT00900000140835; -.
InParanoid; P48809; -.
KO; K14411; -.
OMA; ALENGPH; -.
OrthoDB; EOG091G1CPI; -.
PhylomeDB; P48809; -.
ChiTaRS; Hrb27C; fly.
GenomeRNAi; 33968; -.
PRO; PR:P48809; -.
Proteomes; UP000000803; Chromosome 2L.
Bgee; FBgn0004838; -.
ExpressionAtlas; P48809; differential.
Genevisible; P48809; DM.
GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
GO; GO:0030529; C:intracellular ribonucleoprotein complex; IDA:FlyBase.
GO; GO:0005654; C:nucleoplasm; IDA:FlyBase.
GO; GO:0005634; C:nucleus; HDA:FlyBase.
GO; GO:0043186; C:P granule; IPI:FlyBase.
GO; GO:0043234; C:protein complex; IPI:FlyBase.
GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:FlyBase.
GO; GO:0048027; F:mRNA 5'-UTR binding; TAS:FlyBase.
GO; GO:0003729; F:mRNA binding; ISS:FlyBase.
GO; GO:0003697; F:single-stranded DNA binding; IDA:FlyBase.
GO; GO:0007411; P:axon guidance; IMP:FlyBase.
GO; GO:0007298; P:border follicle cell migration; IMP:FlyBase.
GO; GO:0007319; P:negative regulation of oskar mRNA translation; TAS:FlyBase.
GO; GO:0045451; P:pole plasm oskar mRNA localization; IMP:FlyBase.
GO; GO:0045727; P:positive regulation of translation; IDA:FlyBase.
GO; GO:0048024; P:regulation of mRNA splicing, via spliceosome; IMP:FlyBase.
CDD; cd12574; RRM1_DAZAP1; 1.
CDD; cd12327; RRM2_DAZAP1; 1.
Gene3D; 3.30.70.330; -; 2.
InterPro; IPR034134; DAZAP1_RRM1.
InterPro; IPR034131; DAZAP1_RRM2.
InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
InterPro; IPR035979; RBD_domain_sf.
InterPro; IPR000504; RRM_dom.
Pfam; PF00076; RRM_1; 2.
SMART; SM00360; RRM; 2.
SUPFAM; SSF54928; SSF54928; 2.
PROSITE; PS50102; RRM; 2.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Nucleus; Phosphoprotein;
Reference proteome; Repeat; Ribonucleoprotein; RNA-binding.
CHAIN 1 421 Heterogeneous nuclear ribonucleoprotein
27C.
/FTId=PRO_0000081748.
DOMAIN 7 88 RRM 1. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 96 173 RRM 2. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
MOD_RES 177 177 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 366 366 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 368 368 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 370 370 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 372 372 Phosphotyrosine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 379 379 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
CONFLICT 262 297 Missing (in Ref. 1; CAA44505).
{ECO:0000305}.
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


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